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2'(3')-O-(N-methylanthraniloyl)ATP + H2O
2'(3')-O-(N-methylanthraniloyl)ADP + phosphate
the fluorescent ATP analogue is used throughout all experiments to provide a complete ATPase cycle for a single nucleotide species
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ATP + H2O
ADP + phosphate
CTP + H2O
CDP + phosphate
dATP + H2O
dADP + phosphate
dCTP + H2O
dCDP + phosphate
dGTP + H2O
dGDP + phosphate
dTTP + H2O
dTDP + phosphate
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NTPs can support helicase activity in order of decreasing efficiency: ATP, GTP, dCTP, UTP, dTTP, CTP, dATP, dGTP
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GTP + H2O
GDP + phosphate
single-stranded M13 viral form DNA annealed to a radiolabeled 91-mer oligonucleotide
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the enzyme possesses an ATPase activity that is strongly stimulated by either single- or double-stranded DNA. Moreover, the enzyme exhibits ATP- and Mg2+-dependent DNA helicase activity that displays 3'-5' directionality
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UTP + H2O
UDP + phosphate
additional information
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ATP + H2O
ADP + phosphate
DNA helicase with 3'-to-5' polarity. No helicase activity in absence of NTP
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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?
ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
involved in DNA recombination, repair and genome stability maintenance
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ATP + H2O
ADP + phosphate
AtMCM3 preferentially utilize ATP and dATP
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
PcrA shows 3' to 5' as well as 5' to 3' helicase activities, with substrates containing a duplex region and a 3' or 5' ss poly(dT) tail. PcrA also efficiently unwinds oligonucleotides containing a duplex region and a 5' or 3' ss tail with the potential to form a secondary structure
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ATP + H2O
ADP + phosphate
-
BcMCM displays 3' to 5' helicase and ssDNA-stimulated ATPase activity. BcMCM is an active ATPase, and this activity is restricted to the MCM-AAA module
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
the SF1A helicase shows direct DNA binding by conserved aromatic (Trp or Phe) and electropositive (Arg) residues within the ARLs via stacking with ssDNA bases and gripping the phosphodiester backbone, respectively
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
the SF1A helicase shows direct DNA binding by conserved aromatic (Trp or Phe) and electropositive (Arg) residues within the ARLs via stacking with ssDNA bases and gripping the phosphodiester backbone, respectively
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ATP + H2O
ADP + phosphate
-
the helicase is capable of displacing DNA fragments up to 140 nucleotides in length, but is unable to displace a DNA fragment 322 nucleotides in length. Preference for displacing primers whose 5' terminus is fully annealed as opposed to primers with a 12 nucleotide 5' unannealed tail. The presence of a 12 nucleotide 3' tail has no effect on the rate of displacement. DNA helicase E is capable of displacing a primer downstream of either a four nucleotide gap, a one nucleotide gap or a nick in the DNA substrate. Helicase E is inactive on a fully duplex DNA 30 base pairs in length
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ATP + H2O
ADP + phosphate
the ability of CeWRN-1 to unwind DNA structures may improve the access for DNA repair and replication proteins that are important for preventing the accumulation of abnormal structures, contributing to genomic stability
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ATP + H2O
ADP + phosphate
ATP-dependent 3' to 5' helicase capable of unwinding a variety of DNA structures such as forked duplexes, Holliday junctions, bubble substrates, D-loops, and flap duplexes, and 3'-tailed duplex substrates
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ATP + H2O
ADP + phosphate
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RECQ5 unwinds duplex DNA with a 3'-5' polarity. Unwinding of longer partial duplex DNA substrates requires a higher protein concentration than does unwinding of the 20bp partial duplex substrate. The unwinding reaction catalyzed by RECQ5 requires a nucleoside 5'-phosphate. dATP is most effective. RECQ5 hydrolyzes dATP more rapidly than ATP regardless of the presence of ssDNA. Both ssDNA cofactors, M13mp18 ssDNA and poly(dT) strongly stimulate the dATPase activity of the protein
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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?
ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
as a DNA-dependent ATPase, helicase II translocates processively along single-stranded DNA. The translocation of helicase II along single-stranded DNA is unidirectional and in th 3 to 5 direction with respect to the DNA strand on which the enzyme is bound
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ATP + H2O
ADP + phosphate
the SF1A helicase shows direct DNA binding by conserved aromatic (Trp or Phe) and electropositive (Arg) residues within the ARLs via stacking with ssDNA bases and gripping the phosphodiester backbone, respectively
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ATP + H2O
ADP + phosphate
an aromatic-rich loop couples DNA binding and ATP hydrolysis in the PriA DNA helicase
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ATP + H2O
ADP + phosphate
rates of DNA unwinding catalyzed by wild-type RecQ and truncated RecQ mutants are measured at the single molecule level using a 1.2 kb hairpin ssDNA substrate, method, overview
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
the chemical cleavage step is the rate-limiting step in the ATPase cycle and is essentially irreversible and results in the bound ATP complex being a major component at steady state. This cleavage step is greatly accelerated by bound DNA, producing the high activation of this protein compared to the protein alone. The data suggest the possibility that ADP is released in two steps, which results in bound ADP also being a major intermediate, with bound ADP*phosphate being a very small component. It therefore seems likely that the major transition in structure occurs during the cleavage step, rather than phosphate release
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ATP + H2O
ADP + phosphate
the SF1A helicase shows direct DNA binding by conserved aromatic (Trp or Phe) and electropositive (Arg) residues within the ARLs via stacking with ssDNA bases and gripping the phosphodiester backbone, respectively
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ATP + H2O
ADP + phosphate
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the C-terminal portion of hepatitis C virus nonstructural protein 3 (NS3) forms a three domain polypeptide that possesses the ability to travel along RNA or single-stranded DNA (ssDNA) in a 3 to 5 direction. Driven by the energy of ATP hydrolysis, this movement allows the protein to displace complementary strands of DNA or RNA
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ATP + H2O
ADP + phosphate
-
the protein binds RNA and DNA in a sequence specific manner. ATP hydrolysis is stimulated by some nucleic acid polymers much better than it is stimulated by others. The range is quite dramatic. Poly(G) RNA does not stimulate at any measurable level, and poly(U) RNA (or DNA) stimulates best (up to 50 fold). HCV helicase unwinds a DNA duplex more efficiently than an RNA duplex. ATP binds HCV helicase between two RecA-like domains, causing a conformational change that leads to a decrease in the affinity of the protein for nucleic acids. One strand of RNA binds in a second cleft formed perpendicular to the ATP-binding cleft and its binding leads to stimulation of ATP hydrolysis. RNA and/or ATP binding likely causes rotation of domain 2 of the enzyme relative to domains 1 and 3, and somehow this conformational change allows the protein to move like a motor
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ATP + H2O
ADP + phosphate
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catalytic DNA helicase activity is coupled with NTPase and is stimulated by ATP
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
3'-5' helicase activity. WRN helicase is involved in preserving DNA integrity during replication. It is proposed that WRN helicase can function in coordinating replication fork progression with replication stress-induced fork remodeling
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ATP + H2O
ADP + phosphate
the DNA-dependent ATPase utilizes the energy from ATP hydrolysis to unwind double-stranded DNA. The enzyme unwinds two important intermediates of replication/repair, a 5'-ssDNA flap substrate and a synthetic replication fork. The enzyme is able to translocate on the lagging strand of the synthetic replication fork to unwind duplex ahead of the fork. For the 5'-flap structure, the enzyme specifically displaces the 5'-flap oligonucleotide, suggesting a role of the enzyme in Okazaki fragment processing. The ability of the enzyme to target DNA replication/repair intermediates may be relevant to its role in genome stability maintenance
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ATP + H2O
ADP + phosphate
3'-5' helicase activity
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ATP + H2O
ADP + phosphate
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ATP-dependent DNA unwinding enzyme. HDH VI unwinds exclusively DNA duplexes with an annealed portion smaller than32 bp and prefers a replication fork-like structure of the substrate. It cannot unwind blunt-end duplexes and is inactive also on DNA-RNA or RNA-RNA hybrids. HDH VI unwinds DNA unidirectionally by moving in the 3' to 5' direction along the bound strand. ATP and dATP are equally good substrates
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ATP + H2O
ADP + phosphate
the DNA-dependent ATPase utilizes the energy from ATP hydrolysis to unwind double-stranded DNA. The enzyme unwinds two important intermediates of replication/repair, a 5'-ssDNA flap substrate and a synthetic replication fork. The enzyme is able to translocate on the lagging strand of the synthetic replication fork to unwind duplex ahead of the fork. For the 5'-flap structure, the enzyme specifically displaces the 5'-flap oligonucleotide
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ATP + H2O
ADP + phosphate
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the enzyme unwinds DNA in the 3'-5' direction with respect to the strand to which the enzyme is bound
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
radioactive enzyme activity assay with gamma-32P-ATP
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ATP + H2O
ADP + phosphate
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during chromosomal DNA replication, the replicative helicase unwinds the duplex DNA to provide the single-stranded DNA substrate for the polymerase. In archaea, the replicative helicase is the minichromosome maintenance complex. The enzyme utilizes the energy of ATP hydrolysis to translocate along one strand of the duplex and unwind the complementary strand
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ATP + H2O
ADP + phosphate
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ATP-dependent 3'-5' helicase activity. During chromosomal DNA replication, the replicative helicase unwinds the duplex DNA to provide the single-stranded DNA substrate for the polymerase. In archaea, the replicative helicase is the minichromosome maintenance complex. The enzyme utilizes the energy of ATP hydrolysis to translocate along one strand of the duplex and unwind the complementary strand. ATP binding enhances DNA binding by the helicase. ATPase activity is substantially enhanced in presence of DNA. MCM protein binds DNA ends better than long circular substrates
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
only ATP and dATP support helicase activity. 80% of the duplex is separated in the presence of 1 mM ATP in a 15 min reaction, 58% is unwound in the presence of 1 mM dATP. ATPase activity is dependent upon the presence of DNA. Oligonucleotides of 4 nucleotides are sufficient to promote the ATPase activity. UvrD preferentially unwinds 3'-single-stranded tailed duplex substrates over 5'-single-stranded ones, indicating that the protein has a duplex-unwinding activity with 3'-to-5' polarity. A 3' single-stranded DNA tail of 18 nucleotides is required for effective unwinding. UvrD has an unwinding preference towards nicked DNA duplexes and stalled replication forks
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
only ATP and dATP support helicase activity. 80% of the duplex is separated in the presence of 1 mM ATP in a 15 min reaction, 58% is unwound in the presence of 1 mM dATP. ATPase activity is dependent upon the presence of DNA. Oligonucleotides of 4 nucleotides are sufficient to promote the ATPase activity. UvrD preferentially unwinds 3'-single-stranded tailed duplex substrates over 5'-single-stranded ones, indicating that the protein has a duplex-unwinding activity with 3'-to-5' polarity. A 3' single-stranded DNA tail of 18 nucleotides is required for effective unwinding. UvrD has an unwinding preference towards nicked DNA duplexes and stalled replication forks
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP is the most active NTP. DNA helicase unwinds DNA unidirectionally from 3 to 5. DNA helicase can unwind a 17-bp duplex whether it has unpaired single-stranded tails at both the 5 end and 3 end, at the 5 end or at the 3 end only, or at neither end. However, it fails to act on a blunt-ended 17-bp duplex DNA
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ATP + H2O
ADP + phosphate
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the enzyme can unwind 17-bp partial duplex substrates with equal efficiency whether or not they contain a fork. It translocates unidirectionally along the bound strand in the 3' to 5' direction. NTPs can support helicase activity in order of decreasing efficiency: ATP, GTP, dCTP, UTP, dTTP, CTP, dATP, dGTP. The optimum concentration of ATP for DNA helicase activity is 1.0 mM. At 8 mM ATP the DNA unwinding activity of PDH120 is inhibited. No significant difference in the DNA unwinding activity of PDH120 with forked or nonforked substrates. The enzyme fails to unwind synthetic blunt-ended duplex DNA suggesting that PDH120 requires ssDNA adjacent to the duplex as a loading zone
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
helicases play an essential role in nearly all the nucleic acid metabolic processes, catalyzing the transient opening of the duplex nucleic acids in an ATP-dependent manner
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ATP + H2O
ADP + phosphate
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the enzyme moves unidirectionally in the 3' to 5' direction along the bound strand and prefers a fork-like substrate structure and could not unwind blunt-ended duplex DNA
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ATP + H2O
ADP + phosphate
the enzyme preferentially binds to fork-related Y-structured DNAs and unwinds their double-stranded regions
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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?
ATP + H2O
ADP + phosphate
during chromosomal DNA replication, the replicative helicase unwinds the duplex DNA to provide the single-stranded DNA substrate for the polymerase. In archaea, the replicative helicase is the minichromosome maintenance complex. The enzyme utilizes the energy of ATP hydrolysis to translocate along one strand of the duplex and unwind the complementary strand
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ATP + H2O
ADP + phosphate
ATP-dependent 3'-5' helicase activity. During chromosomal DNA replication, the replicative helicase unwinds the duplex DNA to provide the single-stranded DNA substrate for the polymerase. In archaea, the replicative helicase is the minichromosome maintenance complex. The enzyme utilizes the energy of ATP hydrolysis to translocate along one strand of the duplex and unwind the complementary strand. Very limited stimulation of its ATPase activity by DNA
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ATP + H2O
ADP + phosphate
a steric exclusion and wrapping (SEW) model for MCM helicases is proposed, which the hexamer complex is stabilized by wrapping of the displaced 5'-strand around the exterior surface, resembling a spool of thread
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ATP + H2O
ADP + phosphate
Arg329 is a key residue in the communication between the DNA-binding site of SsoMCM and the trans component of the ATPase active site
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ATP + H2O
ADP + phosphate
ATP-dependent 3'-5' DNA helicase activity in vitro. Preferentially acts on DNA duplexes containing a 5'-tail
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ATP + H2O
ADP + phosphate
ATP-dependent 3'5' DNA-helicase activity. Both monomeric and dimeric forms of Hel112 possess ATPase activity. In the monomeric state the enzyme is able to bind single-stranded DNA with an affinity lower than the one observed for the fork and 3'-mis DNA. In contrast, Hel112 in the dimeric form binds single-stranded DNA with very low affinity
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ATP + H2O
ADP + phosphate
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ATP-dependent DNA helicase activity
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ATP + H2O
ADP + phosphate
ATPase activity of wild-type enzyme is 1.5- to 1.8-fold higher in the presence of DNA. Conformational change in the MCM complex upon binding DNA allows for this increase in the rate of ATP hydrolysis, which is required for rapid unwinding
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ATP + H2O
ADP + phosphate
-
binding preference for forked substrates relative to partial or full duplex substrates. The nature of binding ogf the enzyme to Y-shaped substrates is distinct in that MCM loads on the 3'-tail while interacting with the 5'-tail likely via the MCM surface
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ATP + H2O
ADP + phosphate
dATP and ATP support DNA unwinding reaction
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ATP + H2O
ADP + phosphate
DNA duplexes that contains a 30-nucleotide 5'-tail. The ability of the enzyme to bind single- but not double-stranded DNA is required for the unwinding function
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ATP + H2O
ADP + phosphate
only the monomeric enzyme form has an ATP-dependent 3'-5' DNA-helicase activity, whereas, both the monomeric and dimeric forms possess DNA strand-annealing capability. The Hel112 monomeric form is able to unwind forked and 3'-tailed DNA structures with high efficiency, whereas it is almost inactive on blunt-ended duplexes and bubble-containing molecules
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ATP + H2O
ADP + phosphate
-
the central AAA+ domain possesses ATPase and helicase activity. The degenerate helix-turn-helix domain at the C-terminus of MCM exerts a negative effect on the helicase activity of the complex. Addition of the N-terminus influences both the processivity of the helicase and the choice of substrate that can be melted by the ATPase domain. The degenerate helix-turn-helix domain at the C-terminus of MCM exerts a negative effect on the helicase activity of the complex. Extensive regulatory inter-domain communication within the MCM complex
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ATP + H2O
ADP + phosphate
the enzyme can tolerate catalytically inactive subunits and still function as a helicase. The mode of intersubunit communication within mini-chromosome maintenance complex supports a semisequential model for harnessing the energy of ATP binding, hydrolysis, and release in the generation of helicase activity
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ATP + H2O
ADP + phosphate
-
the enzyme unwinds double-stranded DNA (dsDNA) in a 3'-to-5' direction in the presence of ATP over a wide range of temperatures, from 37°C to 75°C, and possesses DNA-stimulated ATPase activity. dATP can substitute for ATP to a limited extent, the enzyme is unable to bind ssDNA
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ATP + H2O
ADP + phosphate
the protein exterior hairpin reveals critical residues for helicase activity and DNA binding
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
-
the enzyme unwinds double-stranded DNA (dsDNA) in a 3'-to-5' direction in the presence of ATP over a wide range of temperatures, from 37°C to 75°C, and possesses DNA-stimulated ATPase activity. dATP can substitute for ATP to a limited extent, the enzyme is unable to bind ssDNA
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ATP + H2O
ADP + phosphate
-
ATP-dependent DNA helicase activity
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ATP + H2O
ADP + phosphate
ATP-dependent 3'5' DNA-helicase activity. Both monomeric and dimeric forms of Hel112 possess ATPase activity. In the monomeric state the enzyme is able to bind single-stranded DNA with an affinity lower than the one observed for the fork and 3'-mis DNA. In contrast, Hel112 in the dimeric form binds single-stranded DNA with very low affinity
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ATP + H2O
ADP + phosphate
only the monomeric enzyme form has an ATP-dependent 3'-5' DNA-helicase activity, whereas, both the monomeric and dimeric forms possess DNA strand-annealing capability. The Hel112 monomeric form is able to unwind forked and 3'-tailed DNA structures with high efficiency, whereas it is almost inactive on blunt-ended duplexes and bubble-containing molecules
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ATP + H2O
ADP + phosphate
the protein exterior hairpin reveals critical residues for helicase activity and DNA binding
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ATP + H2O
ADP + phosphate
ATP-dependent 3'-5' DNA helicase activity in vitro. Preferentially acts on DNA duplexes containing a 5'-tail
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ATP + H2O
ADP + phosphate
dATP and ATP support DNA unwinding reaction
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ATP + H2O
ADP + phosphate
DNA duplexes that contains a 30-nucleotide 5'-tail. The ability of the enzyme to bind single- but not double-stranded DNA is required for the unwinding function
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ATP + H2O
ADP + phosphate
the enzyme can tolerate catalytically inactive subunits and still function as a helicase. The mode of intersubunit communication within mini-chromosome maintenance complex supports a semisequential model for harnessing the energy of ATP binding, hydrolysis, and release in the generation of helicase activity
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ATP + H2O
ADP + phosphate
ATPase activity of wild-type enzyme is 1.5- to 1.8-fold higher in the presence of DNA. Conformational change in the MCM complex upon binding DNA allows for this increase in the rate of ATP hydrolysis, which is required for rapid unwinding
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
DNA helicase Hmi1p is involved in the maintenance of mitochondrial DNA
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ATP + H2O
ADP + phosphate
meiosis-specific MER3 protein is required for crossing over, which ensures faithful segregation of homologous chromosomes at the first meiotic division
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ATP + H2O
ADP + phosphate
DNA helicase activity has a 3' to 5' polarity with respect to the DNA strand on which this protein translocates
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ATP + H2O
ADP + phosphate
exhibits an ATPase activity in the presence of single- or double-stranded DNA. Displacement of the DNA strand occurs in the 3' to 5' direction with respect to the single-stranded DNA flanking the duplex. The efficiency of unwinding is found to correlate inversely with the length of the duplex region. The recombinant Sgs1 fragment is found to bind more tightly to a forked DNA substrate than to either single or double-stranded DNA. Like the DNA-DNA helicase activity, unwinding of the DNA-RNA hybrid is driven by the hydrolysis of ATP or dATP
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ATP + H2O
ADP + phosphate
unwinds DNA in the 3' to 5' direction relative to single-stranded regions in the DNA substrates
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
PcrA is a chromosomally encoded DNA helicase of gram-positive bacteria involved in replication of rolling circle replicating plasmids
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ATP + H2O
ADP + phosphate
hydrolyzes both ATP and dATP at similar levels. The enzyme shows 5' to 3' and 3' to 5' DNA helicase activities and binds efficiently to partially duplex DNA containing a hairpin structure adjacent to a 6-nucleotide 5' or 3' single-stranded tail and one unpaired (flap) nucleotide in the complementary strand
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ATP + H2O
ADP + phosphate
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the archaeal Rad50-Mre11 complex might act in association with a 5' to 3' exonuclease (NurA) and a bipolar DNA helicase indicating a probable involvement in the initiation step of homologous recombination
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ATP + H2O
ADP + phosphate
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the helicases is able to utilize either 3' or 5' single-stranded DNA extensions for loading and subsequent DNA duplex unwinding
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ATP + H2O
ADP + phosphate
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the archaeal Rad50-Mre11 complex might act in association with a 5' to 3' exonuclease (NurA) and a bipolar DNA helicase indicating a probable involvement in the initiation step of homologous recombination
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ATP + H2O
ADP + phosphate
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the helicases is able to utilize either 3' or 5' single-stranded DNA extensions for loading and subsequent DNA duplex unwinding
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ATP + H2O
ADP + phosphate
the enzyme physically interacts with StoHjc, the Holliday junction-specific endonuclease from Sulfolobus tokodaii. The unwinding activity of the helicase (StoHjm) is inhibited by StoHjc in vitro. These results may suggest that the Hjm/Hel308 family helicases, in association with Hjc endonucleases, are involved in processing of stalled replication forks
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ATP + H2O
ADP + phosphate
-
the Hjm protein is essential for cell viability. The StoHjc protein regulates the helicase activity of StoHjm by inducing conformation change of the enzyme. Hjm/Hjc mediated resolution of stalled replication forks is of crucial importance in archaea. A tentative pathway with which Hjm/Hjc interaction could have occurred at stalled replication forks is discussed
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ATP + H2O
ADP + phosphate
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StoHjm has two main modules, the N-terminal ATPase and DNA binding module (1431) and the C-terminal helicase regulation module (414704). While the N-terminal module is active alone to hydrolyze ATP and to bind different types of DNA substrates, it does not show any helicase activity. DNA unwinding by the StoHjm protein requires the presence of domain III and IV of the C-terminal module in addition to the N-terminal module
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ATP + H2O
ADP + phosphate
the enzyme unwinds DNA in both 3'-to-5' and 5'-to-3' directions. The enzyme exhibits structure-specific single-stranded-DNA-annealing and fork regression activities in vitro
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ATP + H2O
ADP + phosphate
the enzyme unwinds Holliday junction, splayed-armDNA, aswell as 5'- or 3'-overhang with high efficiency
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ATP + H2O
ADP + phosphate
the enzyme unwinds Holliday junction, splayed-armDNA, aswell as 5'- or 3'-overhang with high efficiency
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ATP + H2O
ADP + phosphate
the enzyme physically interacts with StoHjc, the Holliday junction-specific endonuclease from Sulfolobus tokodaii. The unwinding activity of the helicase (StoHjm) is inhibited by StoHjc in vitro. These results may suggest that the Hjm/Hel308 family helicases, in association with Hjc endonucleases, are involved in processing of stalled replication forks
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ATP + H2O
ADP + phosphate
the enzyme unwinds DNA in both 3'-to-5' and 5'-to-3' directions. The enzyme exhibits structure-specific single-stranded-DNA-annealing and fork regression activities in vitro
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ATP + H2O
ADP + phosphate
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?
ATP + H2O
ADP + phosphate
helicase UvrD protein plays an important role in nucleotide excision repair, mismatch repair, rolling circular plasmid replication, and in DNA replication
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?
ATP + H2O
ADP + phosphate
the enzyme hydrolyzes nucleoside triphosphates in order of decreasing efficiency: ATP, dATP, dGTP, GTP, CTP, dCTP, UTP. The enzyme is highly active on a double-stranded DNA with 5' recessed ends in comparison with substrates with 3' recessed or blunt ends, and supports enzyme translocation in a 3'-5' direction relative to the strand bound by the enzyme
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?
CTP + H2O
CDP + phosphate
DNA helicase with 3'-to-5' polarity. No helicase activity in absence of NTP
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?
CTP + H2O
CDP + phosphate
-
RECQ5 unwinds duplex DNA with a 3'-5' polarity. The unwinding reaction catalyzed RECQ5 requires a nucleoside 5'-phosphate. dATP is most effective. ATP supports helicase reaction with 10% of the efficiency obtained with dATP
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-
?
CTP + H2O
CDP + phosphate
-
NTPs can support helicase activity in order of decreasing efficiency: ATP, GTP, dCTP, UTP, dTTP, CTP, dATP, dGTP
-
-
?
CTP + H2O
CDP + phosphate
the enzyme hydrolyzes nucleoside triphosphates in order of decreasing efficiency: ATP, dATP, dGTP, GTP, CTP, dCTP, UTP. The enzyme is highly active on a double-stranded DNA with 5' recessed ends in comparison with substrates with 3' recessed or blunt ends, and supports enzyme translocation in a 3'-5' direction relative to the strand bound by the enzyme
-
-
?
dATP + H2O
dADP + phosphate
DNA helicase with 3'-to-5' polarity. No helicase activity in absence of NTP. dATP is as efficient as ATP
-
-
?
dATP + H2O
dADP + phosphate
AtMCM3 preferentially utilize ATP and dATP
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-
?
dATP + H2O
dADP + phosphate
-
RECQ5 unwinds duplex DNA with a 3'-5' polarity. Unwinding of longer partial duplex DNA substrates requires a higher protein concentration than does unwinding of the 20bp partial duplex substrate. The unwinding reaction catalyzed by RECQ5 requires a nucleoside 5'-phosphate. RECQ5 hydrolyzes dATP more rapidly than ATP regardless of the presence of ssDNA. dATP is most effective. ATP supports helicase reaction with 45% of the efficiency obtained with dATP. Both ssDNA cofactors, M13mp18 ssDNA and poly(dT) strongly stimulate the ATPase activity of the protein
-
-
?
dATP + H2O
dADP + phosphate
-
structure-specific DNA helicase. DmRECQ5 preferentially unwinds specific DNA structures including a 3'flap, a three-strand junction and a three-way junction. Unwinding of a Holliday junction, 5'flap and 12 nt bubble structures, which can be unwound by other RecQ proteins (WRN, BLM and/or Escherichia coli RecQ), can not be detected or requires significantly higher protein concentrations
-
-
?
dATP + H2O
dADP + phosphate
-
ATP-dependent DNA unwinding enzyme. HDH VI unwinds exclusively DNA duplexes with an annealed portion smaller than32 bp and prefers a replication fork-like structure of the substrate. It cannot unwind blunt-end duplexes and is inactive also on DNA-RNA or RNA-RNA hybrids. HDH VI unwinds DNA unidirectionally by moving in the 3' to 5' direction along the bound strand. ATP and dATP are equally good substrates
-
-
?
dATP + H2O
dADP + phosphate
-
-
-
-
?
dATP + H2O
dADP + phosphate
-
-
-
?
dATP + H2O
dADP + phosphate
only ATP and dATP support helicase activity. 80% of the duplex is separated in the presence of 1 mM ATP in a 15 min reaction, 58% is unwound in the presence of 1 mM dATP. ATPase activity is dependent upon the presence of DNA. Oligonucleotides of 4 nucleotides are sufficient to promote the ATPase activity. UvrD preferentially unwinds 3'-single-stranded tailed duplex substrates over 5'-single-stranded ones, indicating that the protein has a duplex-unwinding activity with 3'-to-5' polarity. A 3' single-stranded DNA tail of 18 nucleotides is required for effective unwinding. UvrD has an unwinding preference towards nicked DNA duplexes and stalled replication forks
-
-
?
dATP + H2O
dADP + phosphate
-
-
-
?
dATP + H2O
dADP + phosphate
only ATP and dATP support helicase activity. 80% of the duplex is separated in the presence of 1 mM ATP in a 15 min reaction, 58% is unwound in the presence of 1 mM dATP. ATPase activity is dependent upon the presence of DNA. Oligonucleotides of 4 nucleotides are sufficient to promote the ATPase activity. UvrD preferentially unwinds 3'-single-stranded tailed duplex substrates over 5'-single-stranded ones, indicating that the protein has a duplex-unwinding activity with 3'-to-5' polarity. A 3' single-stranded DNA tail of 18 nucleotides is required for effective unwinding. UvrD has an unwinding preference towards nicked DNA duplexes and stalled replication forks
-
-
?
dATP + H2O
dADP + phosphate
-
dATP shows 25% of the activity compared to ATP. DNA helicase unwinds DNA unidirectionally from 3 to 5
-
-
?
dATP + H2O
dADP + phosphate
-
NTPs can support helicase activity in order of decreasing efficiency: ATP, GTP, dCTP, UTP, dTTP, CTP, dATP, dGTP
-
-
?
dATP + H2O
dADP + phosphate
-
the enzyme moves unidirectionally in the 3' to 5' direction along the bound strand and prefers a fork-like substrate structure and could not unwind blunt-ended duplex DNA. dATP supports unwinding at 42% of the efficiency of ATP
-
-
?
dATP + H2O
dADP + phosphate
exhibits an ATPase activity in the presence of single- or double-stranded DNA. Displacement of the DNA strand occurs in the 3' to 5' direction with respect to the single-stranded DNA flanking the duplex. The efficiency of unwinding is found to correlate inversely with the length of the duplex region. The recombinant Sgs1 fragment is found to bind more tightly to a forked DNA substrate than to either single or double-stranded DNA. Like the DNA-DNA helicase activity, unwinding of the DNA-RNA hybrid is driven by the hydrolysis of ATP or dATP
-
-
?
dATP + H2O
dADP + phosphate
hydrolyzes both ATP and dATP at similar levels. The enzyme shows 5' to 3' and 3' to 5' helicase activities and binds efficiently to partially duplex DNA containing a hairpin structure adjacent to a 6-nucleotide 5' or 3' single-stranded tail and one unpaired (flap) nucleotide in the complementary strand
-
-
?
dATP + H2O
dADP + phosphate
the enzyme hydrolyzes nucleoside triphosphates in order of decreasing efficiency: ATP, dATP, dGTP, GTP, CTP, dCTP, UTP. The enzyme is highly active on a double-stranded DNA with 5' recessed ends in comparison with substrates with 3' recessed or blunt ends, and supports enzyme translocation in a 3'-5' direction relative to the strand bound by the enzyme
-
-
?
dCTP + H2O
dCDP + phosphate
-
NTPs can support helicase activity in order of decreasing efficiency: ATP, GTP, dCTP, UTP, dTTP, CTP, dATP, dGTP
-
-
?
dCTP + H2O
dCDP + phosphate
the enzyme hydrolyzes nucleoside triphosphates in order of decreasing efficiency: ATP, dATP, dGTP, GTP, CTP, dCTP, UTP. The enzyme is highly active on a double-stranded DNA with 5' recessed ends in comparison with substrates with 3' recessed or blunt ends, and supports enzyme translocation in a 3'-5' direction relative to the strand bound by the enzyme
-
-
?
dGTP + H2O
dGDP + phosphate
-
RECQ5 unwinds duplex DNA with a 3'-5' polarity. The unwinding reaction catalyzed by RECQ5 requires a nucleoside 5'-phosphate. dATP is most effective. ATP supports helicase reaction with 30% of the efficiency obtained with dATP
-
-
?
dGTP + H2O
dGDP + phosphate
-
NTPs can support helicase activity in order of decreasing efficiency: ATP, GTP, dCTP, UTP, dTTP, CTP, dATP, dGTP
-
-
?
dGTP + H2O
dGDP + phosphate
the enzyme hydrolyzes nucleoside triphosphates in order of decreasing efficiency: ATP, dATP, dGTP, GTP, CTP, dCTP, UTP. The enzyme is highly active on a double-stranded DNA with 5' recessed ends in comparison with substrates with 3' recessed or blunt ends, and supports enzyme translocation in a 3'-5' direction relative to the strand bound by the enzyme
-
-
?
GTP + H2O
GDP + phosphate
DNA helicase with 3'-to-5' polarity. No helicase activity in absence of NTP
-
-
?
GTP + H2O
GDP + phosphate
-
RECQ5 unwinds duplex DNA with a 3'-5' polarity. The unwinding reaction catalyzed by RECQ5 requires a nucleoside 5'-phosphate. dATP is most effective. ATP supports helicase reaction with 35% of the efficiency obtained with dATP
-
-
?
GTP + H2O
GDP + phosphate
-
NTPs can support helicase activity in order of decreasing efficiency: ATP, GTP, dCTP, UTP, dTTP, CTP, dATP, dGTP
-
-
?
GTP + H2O
GDP + phosphate
the enzyme hydrolyzes nucleoside triphosphates in order of decreasing efficiency: ATP, dATP, dGTP, GTP, CTP, dCTP, UTP. The enzyme is highly active on a double-stranded DNA with 5' recessed ends in comparison with substrates with 3' recessed or blunt ends, and supports enzyme translocation in a 3'-5' direction relative to the strand bound by the enzyme
-
-
?
partial duplex DNA
?
32P-labelled 47-mer DNA oligodeoxynucleotide annealed to M13mp19 single-stranded DNA. The enzyme has single-stranded DNA-dependent ATPase activity and DNA helicase activity in the 3' to 5' direction. The enzyme shows up to 58% unwinding with the 3' to 5' direction-specific substrate and is unable to show the activity with 5' to 3' direction-specific substrate
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-
?
partial duplex DNA
?
-
32P-labelled oligodeoxynucleotide (17 mer, 5'-GTAAAACGACGGCCAGT-3') annealed to single-stranded M13mp19 (+) DNA. The enzyme moves unidirectionally in the 3' to 5' direction along the bound strand and prefers a fork-like substrate structure
-
-
?
UTP + H2O
UDP + phosphate
-
NTPs can support helicase activity in order of decreasing efficiency: ATP, GTP, dCTP, UTP, dTTP, CTP, dATP, dGTP
-
-
?
UTP + H2O
UDP + phosphate
the enzyme hydrolyzes nucleoside triphosphates in order of decreasing efficiency: ATP, dATP, dGTP, GTP, CTP, dCTP, UTP. The enzyme is highly active on a double-stranded DNA with 5' recessed ends in comparison with substrates with 3' recessed or blunt ends, and supports enzyme translocation in a 3'-5' direction relative to the strand bound by the enzyme
-
-
?
additional information
?
-
no helicase activity is observed with UTP, dCTP or dTTP, low levels of helicase activity is observed with dGTP
-
-
?
additional information
?
-
-
no helicase activity is observed with UTP, dCTP or dTTP, low levels of helicase activity is observed with dGTP
-
-
?
additional information
?
-
MCM3 binds ATP and possess ATPase and ATP-dependent helicase activities. AtMCM3 shows a greater unwinding activity with 5' forked partial DNA duplex substrate as compared to 3' forked and non-forked substrates. ATP and magnesium ion are indispensable for its DNA helicase activity. Specifically, ATP and dATP are the preferred nucleotides for its unwinding activity. The directionality of the AtMCM3 is in 3' to 5' direction. The helicase activity is determined by strand displacement assay using oligomeric ds DNA substrate. Other nucleotides such as CTP, GTP, UTP, dCTP, dGTP, and dTTP do not support DNA unwinding by AtMCM3. Thus, the AtMCM3 specifically utilizes only ATP or dATP for the in vitro helicase activity
-
-
-
additional information
?
-
-
MCM3 binds ATP and possess ATPase and ATP-dependent helicase activities. AtMCM3 shows a greater unwinding activity with 5' forked partial DNA duplex substrate as compared to 3' forked and non-forked substrates. ATP and magnesium ion are indispensable for its DNA helicase activity. Specifically, ATP and dATP are the preferred nucleotides for its unwinding activity. The directionality of the AtMCM3 is in 3' to 5' direction. The helicase activity is determined by strand displacement assay using oligomeric ds DNA substrate. Other nucleotides such as CTP, GTP, UTP, dCTP, dGTP, and dTTP do not support DNA unwinding by AtMCM3. Thus, the AtMCM3 specifically utilizes only ATP or dATP for the in vitro helicase activity
-
-
-
additional information
?
-
-
the enzyme has DNA-dependent ATPase activity and helicase activity that proceeds in the 3'-5' direction and needs at least five 3' overhanging nucleotides. The enzyme is also able to unwind DNA structures including D-loops and Holliday junctions. The enzyme does not unwind blunt-ended DNA duplexes
-
-
-
additional information
?
-
-
the enzyme has a DNA-dependent ATPase activity and is a 3'-5' DNA helicase dependent on hydrolysis of ATP. The enzyme can unwind substrate with a single-stranded region 3' but not 5' of a double-stranded region, and can also anneal complementary single strands. The enzyme shows no activity in the absence of nucleotide cofactor or in the presence of ADP or the nonhydrolyzable homolog AMPPNP
-
-
-
additional information
?
-
usage of a four-stranded DNA substrate
-
-
-
additional information
?
-
-
the mature NS3 protein comprises 5 domains: the N-terminal 2 domains form the serine protease along with the NS4A cofactor, and the C-terminal 3 domains form the helicase. The helicase portion of NS3 can be separated form the protease portion by cleaving a linker. Since the protease portion is more hydrophobic, removing it allows the NS3 helicase fragment to be expressed as a more soluble protein at higher levels in Escherichia coli. The fragment of NS3 possessing helicase activity is referred to as HCV helicase
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-
?
additional information
?
-
DNA replicase E1 is conferring processivity to cellular DNA polymerase epsilon by directly tethering pol epsilon to the DNA parental strand and towing epsilon behind the E1 helicase as the replication fork progresses. The stimulation of pol epsilon by PV E1 is helicase-specific and dependent on ATP hydrolysis
-
-
-
additional information
?
-
HPV E1 physically interacts with DNA polymerases epsilon and delta. The stimulation of pol epsilon by PV E1 is helicase-specific and dependent on ATP hydrolysis. HPV E1 does not stimulate Escherichia coli DNA polymerase I or human pol delta
-
-
-
additional information
?
-
-
the helicase is capable of unwinding DNA substrates coated with various proteins, including histones, transcription inhibitors, and the transcription initiation complex. Thus, the helicase can displace at least some of the proteins associated with chromatin
-
-
?
additional information
?
-
-
Mtb XPB efficiently catalyzes DNA unwinding. Enzyme requires a DNA substrate with a 39 overhang of 15 nucleotides or more. Enzyme is not active on substrates containing a 39 RNA tail. Mtb XPB efficiently catalyzes ATP-independent annealing of complementary DNA strands
-
-
?
additional information
?
-
Mycobacterium tuberculosis UvrB (MtUvrB) possesses intrinsic ATPase activity that is greatly stimulated by both single- and double-stranded DNA. MtUvrB binds to DNA in a structure-dependent manner. MtUvrB substrate specificity is analyzed, revealing that it associates preferentially with single-stranded DNA, duplexes with 3' or 5' overhangs, and linear duplex DNA with splayed arms. MtUvrB possesses DNA unwinding activity characteristic of an ATP-dependent DNA helicase. The helicase activity of MtUvrB proceeds in the 3' to 5' direction and is strongly modulated by a nontranslocating 5' single-stranded tail, indicating that in addition to the translocating strand it also interacts with the 5' end of the substrate. The fraction of DNA unwound by MtUvrB decreases significantly as the length of the duplex increases: it fails to unwind duplexes longer than 70 bp. No or poor activity with GTP, dGTP, CTP, dCTP, UTP, dUTP, ATPgammaS, and AMP-PNP
-
-
-
additional information
?
-
-
Mycobacterium tuberculosis UvrB (MtUvrB) possesses intrinsic ATPase activity that is greatly stimulated by both single- and double-stranded DNA. MtUvrB binds to DNA in a structure-dependent manner. MtUvrB substrate specificity is analyzed, revealing that it associates preferentially with single-stranded DNA, duplexes with 3' or 5' overhangs, and linear duplex DNA with splayed arms. MtUvrB possesses DNA unwinding activity characteristic of an ATP-dependent DNA helicase. The helicase activity of MtUvrB proceeds in the 3' to 5' direction and is strongly modulated by a nontranslocating 5' single-stranded tail, indicating that in addition to the translocating strand it also interacts with the 5' end of the substrate. The fraction of DNA unwound by MtUvrB decreases significantly as the length of the duplex increases: it fails to unwind duplexes longer than 70 bp. No or poor activity with GTP, dGTP, CTP, dCTP, UTP, dUTP, ATPgammaS, and AMP-PNP
-
-
-
additional information
?
-
Mycobacterium tuberculosis UvrB (MtUvrB) possesses intrinsic ATPase activity that is greatly stimulated by both single- and double-stranded DNA. MtUvrB binds to DNA in a structure-dependent manner. MtUvrB substrate specificity is analyzed, revealing that it associates preferentially with single-stranded DNA, duplexes with 3' or 5' overhangs, and linear duplex DNA with splayed arms. MtUvrB possesses DNA unwinding activity characteristic of an ATP-dependent DNA helicase. The helicase activity of MtUvrB proceeds in the 3' to 5' direction and is strongly modulated by a nontranslocating 5' single-stranded tail, indicating that in addition to the translocating strand it also interacts with the 5' end of the substrate. The fraction of DNA unwound by MtUvrB decreases significantly as the length of the duplex increases: it fails to unwind duplexes longer than 70 bp. No or poor activity with GTP, dGTP, CTP, dCTP, UTP, dUTP, ATPgammaS, and AMP-PNP
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-
-
additional information
?
-
the enzyme efficiently unwinds partial duplex DNA substrate in a 3' to 5' direction, but the enzyme cannot unwind substrates with both 5' and 3' overhangs, those with a 5' overhang, or blunt-ended DNA duplexes. Unwinding of DNA helicase activity is driven by the hydrolysis of ATP. The helicase reaction requires the presence of ATP as a cofactor, although dATP supports the unwinding at 89% of the efficiency of ATP
-
-
?
additional information
?
-
-
the purified enzyme is unable to unwind blunt-ended duplex DNA substrate or 31-mer partial duplex substrate with hanging tail at 5'- or 3'-end
-
-
-
additional information
?
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-
Hel112 physically interacts with the Saccharolobus solfataricus DNA topoisomerase SsTop3, and the two enzymes show synergic and opposing activities. SsTop3 inhibits the Hel112 helicase activity on Holliday junctions and stimulates formation and stabilization of such structures
-
-
-
additional information
?
-
Saccharomyces cerevisiae Hrq1 and Pif1 DNA helicases synergistically modulate telomerase activity in vitro. The helicases alone have equal-but-opposite biphasic effects on telomerase, with Hrq1 stimulating activity at high concentrations. When the helicases are combined in reactions, they synergistically inhibit or stimulate telomerase activity depending on which helicase is catalytically active. Hrq1 affects telomerase activity by a different mechanism than Pif1. The in vitro helicase activity of Hrq1 is decreased about 4fold when unwinding a fork substrate with an RNA-DNA hybrid duplex region relative to a DNA-DNA duplex. Hrq1 has only subtle effects on telomerase activity on a 15-to-30-nt substrate, but on a long (50 nt) primer. Lower concentrations of Hrq1 slightly inhibit telomerase activity, but significant stimulation occurs at higher Hrq1 concentrations
-
-
-
additional information
?
-
-
the helicase translocates 3'-5' along the leading-strand template. The enzyme does not bind a 16-mer 5' (CCGA)4 ssDNA tail
-
-
-
additional information
?
-
Saccharomyces cerevisiae Hrq1 and Pif1 DNA helicases synergistically modulate telomerase activity in vitro. The helicases alone have equal-but-opposite biphasic effects on telomerase, with Hrq1 stimulating activity at high concentrations. When the helicases are combined in reactions, they synergistically inhibit or stimulate telomerase activity depending on which helicase is catalytically active. Hrq1 affects telomerase activity by a different mechanism than Pif1. The in vitro helicase activity of Hrq1 is decreased about 4fold when unwinding a fork substrate with an RNA-DNA hybrid duplex region relative to a DNA-DNA duplex. Hrq1 has only subtle effects on telomerase activity on a 15-to-30-nt substrate, but on a long (50 nt) primer. Lower concentrations of Hrq1 slightly inhibit telomerase activity, but significant stimulation occurs at higher Hrq1 concentrations
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-
-
additional information
?
-
the enzyme is inefficient in in vitro replication of pT181, and perhaps as a consequence, this plasmid can not be established in Streptococcus pneumoniae
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?
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evolution
superfamilies 1 and 2 (SF1 and SF2) comprise the largest number of helicase families and members are involved in a wide array of cellular functions that require manipulation of DNA or RNA structures, the helicases belong to the AAA+ ATPases. Helicase superfamilies can also be subdivided into those that translocate along DNA and unwind in a 3'-5' direction, e.g., SF1A, or a 5'-3 direction, e.g., SF1B. SF1 and SF2 helicases can be identified based on evolutionary conservation of seven sequence motifs (I, Ia, II-VI) that are required for ATP binding/hydrolysis, nucleic acid binding, and/or translocation. SF1 and SF2 helicases include a conserved core helicase domain that is comprised of two subdomains that share similarity with RecA ATPase/recombinase enzyme family
evolution
superfamilies 1 and 2 (SF1 and SF2) comprise the largest number of helicase families and members are involved in a wide array of cellular functions that require manipulation of DNA or RNA structures, the helicases belong to the AAA+ ATPases. Helicase superfamilies can also be subdivided into those that translocate along DNA and unwind in a 3'-5' direction, e.g., SF1A, or a 5'-3 direction, e.g., SF1B. SF1 and SF2 helicases can be identified based on evolutionary conservation of seven sequence motifs (I, Ia, II-VI) that are required for ATP binding/hydrolysis, nucleic acid binding, and/or translocation. SF1 and SF2 helicases include a conserved core helicase domain that is comprised of two subdomains that share similarity with RecA ATPase/recombinase enzyme family
evolution
superfamilies 1 and 2 (SF1 and SF2) comprise the largest number of helicase families and members are involved in a wide array of cellular functions that require manipulation of DNA or RNA structures, the helicases belong to the AAA+ ATPases. Helicase superfamilies can also be subdivided into those that translocate along DNA and unwind in a 3'-5' direction, e.g., SF1A, or a 5'-3 direction, e.g., SF1B. SF1 and SF2 helicases can be identified based on evolutionary conservation of seven sequence motifs (I, Ia, II-VI) that are required for ATP binding/hydrolysis, nucleic acid binding, and/or translocation. SF1 and SF2 helicases include a conserved core helicase domain that is comprised of two subdomains that share similarity with RecA ATPase/recombinase enzyme family
evolution
superfamilies 1 and 2 (SF1 and SF2) comprise the largest number of helicase families and members are involved in a wide array of cellular functions that require manipulation of DNA or RNA structures, the helicases belong to the AAA+ ATPases. Helicase superfamilies can also be subdivided into those that translocate along DNA and unwind in a 3'-5' direction, e.g., SF1A, or a 5'-3 direction, e.g., SF1B. SF1 and SF2 helicases can be identified based on evolutionary conservation of seven sequence motifs (I, Ia, II-VI) that are required for ATP binding/hydrolysis, nucleic acid binding, and/or translocation. SF1 and SF2 helicases include a conserved core helicase domain that is comprised of two subdomains that share similarity with RecA ATPase/recombinase enzyme family
evolution
superfamilies 1 and 2 (SF1 and SF2) comprise the largest number of helicase families and members are involved in a wide array of cellular functions that require manipulation of DNA or RNA structures, the helicases belong to the AAA+ ATPases. Helicase superfamilies can also be subdivided into those that translocate along DNA and unwind in a 3'-5' direction, e.g., SF1A, or a 5'-3 direction, e.g., SF1B. SF1 and SF2 helicases can be identified based on evolutionary conservation of seven sequence motifs (I, Ia, II-VI) that are required for ATP binding/hydrolysis, nucleic acid binding, and/or translocation. SF1 and SF2 helicases include a conserved core helicase domain that is comprised of two subdomains that share similarity with RecA ATPase/recombinase enzyme family
evolution
conserved helicase domains of EcUvrB and MtUvrB
evolution
-
the enzyme belongs to the RecQ protein family, a group of helicases highly conserved from bacteria to humans and playing a critical role in transcription, DNA replication, DNA recombination, and DNA repair
evolution
the enzyme demonstrates a unique capacity of a viral helicase having evolved to stimulate a cellular replicative DNA polymerase
evolution
-
superfamilies 1 and 2 (SF1 and SF2) comprise the largest number of helicase families and members are involved in a wide array of cellular functions that require manipulation of DNA or RNA structures, the helicases belong to the AAA+ ATPases. Helicase superfamilies can also be subdivided into those that translocate along DNA and unwind in a 3'-5' direction, e.g., SF1A, or a 5'-3 direction, e.g., SF1B. SF1 and SF2 helicases can be identified based on evolutionary conservation of seven sequence motifs (I, Ia, II-VI) that are required for ATP binding/hydrolysis, nucleic acid binding, and/or translocation. SF1 and SF2 helicases include a conserved core helicase domain that is comprised of two subdomains that share similarity with RecA ATPase/recombinase enzyme family
-
evolution
-
superfamilies 1 and 2 (SF1 and SF2) comprise the largest number of helicase families and members are involved in a wide array of cellular functions that require manipulation of DNA or RNA structures, the helicases belong to the AAA+ ATPases. Helicase superfamilies can also be subdivided into those that translocate along DNA and unwind in a 3'-5' direction, e.g., SF1A, or a 5'-3 direction, e.g., SF1B. SF1 and SF2 helicases can be identified based on evolutionary conservation of seven sequence motifs (I, Ia, II-VI) that are required for ATP binding/hydrolysis, nucleic acid binding, and/or translocation. SF1 and SF2 helicases include a conserved core helicase domain that is comprised of two subdomains that share similarity with RecA ATPase/recombinase enzyme family
-
evolution
-
conserved helicase domains of EcUvrB and MtUvrB
-
malfunction
loss of RECQ4A leads to elevated homologous recombination frequencies and hypersensitivity to genotoxic agents. Loss of helicase activity or deletion of the N-terminus only partially complemented the mutant hyper-recombination phenotype. The helicase-deficient protein lacking its N-terminus does not complement the hyper-recombination phenotype at all. The recq4A-4 mutant is hypersensitive to treatment with cisplatin. The loss of RECQ4A also leads to a hypersensitivity to the DNA methylating agent MMS. Deletion of the RECQ4A N-terminus does not affect the viability of plants but results in a DNA repair defect
malfunction
gene RECQL4 mutations are associated with Rothmund Thomson syndrome (RTS), RAPADILINO syndrome and Baller-Gerold syndrome. These patients display a range of benign skeletal abnormalities such as low bone mass. In addition, RTS patients have a highly increased incidence of osteosarcoma (OS). Mechanism for the benign skeletal phenotypes of RECQL4 mutation syndromes, overview
malfunction
mechanism for the benign skeletal phenotypes of RECQL4 mutation syndromes, overview. Recql4 deletion in vivo at the osteoblastic progenitor stage of differentiation results in mice with shorter bones and reduced bone volume, assessed at 9 weeks of age. This is associated with an osteoblast intrinsic decrease in mineral apposition rate and bone formation rate in the Recql4-deficient cohorts. Deletion of Recql4 in mature osteoblasts/osteocytes in vivo, does not cause a detectable phenotype. Acute deletion of Recql4 in primary osteoblasts or shRNA knockdown in an osteoblastic cell line cause failed proliferation, accompanied by cell cycle arrest, induction of apoptosis and impaired differentiation. Tumor suppression and osteosarcoma susceptibility are most likely a function of mutant, not null, alleles of RECQL4. Reduced skeletal growth in Osx-Cre Recql4fl/fl mice. The concurrent loss of p53 does not rescue Recql4 deficient osteoblast proliferation
malfunction
-
PfRecQ1enzyme knockout completely abolishes expression of the var gene family. The PfRecQ1DELTA mutation alters heterochromatin, overview
malfunction
-
enzyme gene mutations lead to Bloom's syndrome, an autosomal recessive condition characterized by short stature, immunodeficiency, and a greatly elevated frequency of many types of cancer
malfunction
-
genetic disruption of the enzyme human cells enhances cellular sensitivity and chromosome radial formation by the interstrand crosslink-inducing agent mitomycin C
malfunction
-
homozygous null mutants do not survive past the first instar because of severe defects in replication
malfunction
-
PfRecQ1enzyme knockout completely abolishes expression of the var gene family. The PfRecQ1DELTA mutation alters heterochromatin, overview
-
metabolism
-
expression of the var gene family is regulated by two RecQ DNA helicase family members, PfRecQ1 and PfWRN, in Plasmodium falciparum. PfRecQ1, but not PfWRN, is essential for maintaining the clonal expression of var genes. PfRecQ1 and PfWRN display disparate chromosomal localizations
metabolism
Saccharomyces cerevisiae Hrq1 and Pif1 DNA helicases synergistically modulate telomerase activity in vitro. The helicases alone have equal-but-opposite biphasic effects on telomerase, with Hrq1 stimulating activity at high concentrations. When the helicases are combined in reactions, they synergistically inhibit or stimulate telomerase activity depending on which helicase is catalytically active. Hrq1 and Pif1 interact and their concerted activities ensure proper telomere length homeostasis in vivo. Modelling of Hrq1 and Pif1 cooperatively contributing to telomere length homeostasis in yeast, overview. Hrq1 affects telomerase activity by a different mechanism than Pif1
metabolism
the enzyme is involved in the nucleotide excision repair (NER) pathway
metabolism
the formation of prereplicative complex (pre-RC) is a requisite for the DNA replication initiation in eukaryotes. The pre-RC is composed of several replication factors which includes origin recognition complex (ORC), cell division cycle 6 (Cdc6), Cdc10-dependent transcript 1 (Cdt1), and minichromosome maintenance 2-7 (MCM2-7) complex. The subcomplex MCM4/6/7 possess in vitro helicase activity, while the MCM3 single subunit shows in vitro unwinding and ATPase activities
metabolism
-
expression of the var gene family is regulated by two RecQ DNA helicase family members, PfRecQ1 and PfWRN, in Plasmodium falciparum. PfRecQ1, but not PfWRN, is essential for maintaining the clonal expression of var genes. PfRecQ1 and PfWRN display disparate chromosomal localizations
-
metabolism
-
Saccharomyces cerevisiae Hrq1 and Pif1 DNA helicases synergistically modulate telomerase activity in vitro. The helicases alone have equal-but-opposite biphasic effects on telomerase, with Hrq1 stimulating activity at high concentrations. When the helicases are combined in reactions, they synergistically inhibit or stimulate telomerase activity depending on which helicase is catalytically active. Hrq1 and Pif1 interact and their concerted activities ensure proper telomere length homeostasis in vivo. Modelling of Hrq1 and Pif1 cooperatively contributing to telomere length homeostasis in yeast, overview. Hrq1 affects telomerase activity by a different mechanism than Pif1
-
metabolism
-
the enzyme is involved in the nucleotide excision repair (NER) pathway
-
physiological function
-
in Sulfolobus acidocaldarius, the Mre11 protein and the RadA recombinase might play an active role in the repair of DNA damage introduced by gamma rays and/or may act as DNA damage sensors. The functional interaction between Mre11, Rad50 and the HerA helicase suggest that each protein play different roles when acting on its own or in association with its partners. Interaction of the Mre11 protein with both Rad50 and the HerA bipolar helicase
physiological function
-
in thermophilic archaea, the HerA helicase and NurA nuclease cooperate with the highly conserved Mre11 and Rad50 proteins during homologous recombination-dependent DNA repair
physiological function
the enzyme physically interacts with StoHjc, the Holliday junction-specific endonuclease from Sulfolobus tokodaii. The unwinding activity of the helicase (StoHjm) is inhibited by StoHjc in vitro. These results may suggest that the Hjm/Hel308 family helicases, in association with Hjc endonucleases, are involved in processing of stalled replication forks
physiological function
one function of the enzyme may be in the removal of bound proteins at stalled replication forks and recombination intermediates
physiological function
aromatic-rich loops as coupling motifs that link DNA binding and ATP hydrolysis, the conserved SF1 and SF2 helicase motifs mediate ATP binding and hydrolysis and convert the released chemical energy into the mechanical energy required for translocation and DNA unwinding
physiological function
aromatic-rich loops as coupling motifs that link DNA binding and ATP hydrolysis, the conserved SF1 and SF2 helicase motifs mediate ATP binding and hydrolysis and convert the released chemical energy into the mechanical energy required for translocation and DNA unwinding
physiological function
aromatic-rich loops as coupling motifs that link DNA binding and ATP hydrolysis, the conserved SF1 and SF2 helicase motifs mediate ATP binding and hydrolysis and convert the released chemical energy into the mechanical energy required for translocation and DNA unwinding
physiological function
aromatic-rich loops as coupling motifs that link DNA binding and ATP hydrolysis, the conserved SF1 and SF2 helicase motifs mediate ATP binding and hydrolysis and convert the released chemical energy into the mechanical energy required for translocation and DNA unwinding
physiological function
aromatic-rich loops as coupling motifs that link DNA binding and ATP hydrolysis, the conserved SF1 and SF2 helicase motifs mediate ATP binding and hydrolysis and convert the released chemical energy into the mechanical energy required for translocation and DNA unwinding
physiological function
RecQ helicases are critical for the maintenance of genomic stability, RECQ4A performs critical roles in regulation of homologous recombination and DNA repair. The N-terminal region and the helicase activity of RECQ4A are both essential for the cellular response to replicative stress induced by methyl methanesulfonate and cisplatin. RECQ4A seems to possess at least two different and independent sub-functions involved in the suppression of homologous recombination
physiological function
-
DNA helicase RecQ1 regulates mutually exclusive expression of virulence genes in Plasmodium falciparum via heterochromatin alteration
physiological function
helicases couple ATP hydrolysis to nucleic acid binding and unwinding
physiological function
-
in hyperthermophilic archaea the exo-endonuclease NurA and the ATPase HerA cooperate with the highly conserved Mre11-Rad50 complex in 3' single-stranded DNA (ssDNA) end processing to coordinate repair of double-stranded DNA breaks. RecQ-like DNA helicase Hel112 inhibits the NurA/HerA complex exonuclease activity on linear dsDNA and ssDNA substrates. This effect is not dependent on the directionality of the complex activity. Inhibition occurs both in the presence and in the absence of HerA, but is much stronger when NurA is in complex with HerA. The endonuclease activity of NurA is not affected by the presence of Hel112. The functional interaction between NurA/HerA and Hel112 is important for DNA endresection in archaeal homologous recombination. But Hel112 has no effect on NurA/HerA nicking activity, the inhibitory effect of Hel112 is specific for NurA/HerA exonuclease activity
physiological function
Mycobacterium tuberculosis UvrB is a robust DNA-stimulated ATPase that also possesses structure-specific ATP-dependent DNA helicase activity. It plays an alternative role in the processing of key DNA replication intermediates
physiological function
RecQ DNA helicases are motor proteins that convert the chemical energy of ATP hydrolysis to the mechanical energy required for single-stranded (ss) DNA translocation or double-stranded (ds) DNA unwinding. These activities are critical for RecQ's roles in genome maintenance in organisms ranging from bacteria to humans. In Escherichia coli, RecQ is a component of the RecF pathway of recombinational repair, which repairs ssDNA gaps and dsDNA breaks when the main repair pathway, RecBCD, is inactivated by mutation. ssDNA-binding protein (SSB) is the classical partner of helicases, which slows down DNA re-annealing by sequestering ssDNA. ssDNA and dsDNA binding sites play a crucial role in helicase activity, overview
physiological function
role of RECQL4 in normal adult bone development and homeostasis. Recql4 is required for normal skeletal development and both benign and malignant osteoblast function
physiological function
role of RECQL4 in normal adult bone development and homeostasis. Recql4 is required for normal skeletal development and both benign and malignant osteoblast function
physiological function
Saccharomyces cerevisiae Hrq1 DNA helicase synergistically modulates telomerase activity. Hrq1, the yeast homologue of the disease-linked human RecQ-like helicase 4 (RECQL4), is a catalytic inhibitor of telomerase. Hrq1 functions in telomere length homeostasis. The enzyme is involved in telomerase regulation together with DNA helicase Pif1. Hrq1 also promotes the formation of type I survivors in telomerase-null (tlc1DELTA) cells
physiological function
the human papillomavirus DNA helicase E1 binds, stimulates, and confers processivity to cellular DNA polymerase epsilon. The papillomavirus (PV) helicase protein E1 recruits components of the cellular DNA replication machinery to the PV replication fork, such as replication protein A (RPA), DNA polymerase alpha-primase (polalpha) and topoisomerase I (topo I). E1 binds to DNA polymerase epsilon (pol epsilon) and dramatically stimulates the DNA synthesis activity of pol epsilon. This stimulation of pol epsilon by E1 is highly specific and occurs even in the absence of the known pol epsilon cofactors replication Factor C (RFC), proliferating cell nuclear antigen (PCNA) and RPA. This stimulation is due to an increase in the processivity of pol epsilon and occurs independently of pol epsilon's replication cofactors. The increase in processivity is dependent on the ability of the E1 helicase to hydrolyze ATP, suggesting it is dependent on E1's helicase action. RPA is dispensable for processive synthesis by pol epsilon in the presence of E1. HPV E1 does not stimulate Escherichia coli DNA polymerase I or human pol delta
physiological function
the MCM3 single subunit of MCM2-7 complex functions as 3' to 5' DNA helicase
physiological function
-
the enzyme is essential for maintaining genomic stability
physiological function
-
the enzyme is essential for maintaining genomic stability
physiological function
-
the enzyme operates in DNA repair and cell cycle checkpoint signalling in response to interstrand crosslinks. The enzyme participates in a pathway of resistance to DNA interstrand crosslinks and is associated with the RAD51 paralogs RAD51B/C/D and XRCC2, and with the DNA damage-responsive kinase ATR which suggests the enzyme as a candidate ovarian cancer gene
physiological function
-
the enzyme plays an essential role in replication
physiological function
-
in thermophilic archaea, the HerA helicase and NurA nuclease cooperate with the highly conserved Mre11 and Rad50 proteins during homologous recombination-dependent DNA repair
-
physiological function
-
aromatic-rich loops as coupling motifs that link DNA binding and ATP hydrolysis, the conserved SF1 and SF2 helicase motifs mediate ATP binding and hydrolysis and convert the released chemical energy into the mechanical energy required for translocation and DNA unwinding
-
physiological function
-
aromatic-rich loops as coupling motifs that link DNA binding and ATP hydrolysis, the conserved SF1 and SF2 helicase motifs mediate ATP binding and hydrolysis and convert the released chemical energy into the mechanical energy required for translocation and DNA unwinding
-
physiological function
-
the enzyme physically interacts with StoHjc, the Holliday junction-specific endonuclease from Sulfolobus tokodaii. The unwinding activity of the helicase (StoHjm) is inhibited by StoHjc in vitro. These results may suggest that the Hjm/Hel308 family helicases, in association with Hjc endonucleases, are involved in processing of stalled replication forks
-
physiological function
-
one function of the enzyme may be in the removal of bound proteins at stalled replication forks and recombination intermediates
-
physiological function
-
DNA helicase RecQ1 regulates mutually exclusive expression of virulence genes in Plasmodium falciparum via heterochromatin alteration
-
physiological function
-
Saccharomyces cerevisiae Hrq1 DNA helicase synergistically modulates telomerase activity. Hrq1, the yeast homologue of the disease-linked human RecQ-like helicase 4 (RECQL4), is a catalytic inhibitor of telomerase. Hrq1 functions in telomere length homeostasis. The enzyme is involved in telomerase regulation together with DNA helicase Pif1. Hrq1 also promotes the formation of type I survivors in telomerase-null (tlc1DELTA) cells
-
physiological function
-
Mycobacterium tuberculosis UvrB is a robust DNA-stimulated ATPase that also possesses structure-specific ATP-dependent DNA helicase activity. It plays an alternative role in the processing of key DNA replication intermediates
-
additional information
residue K481 in the Walker A box is an essential amino acid for the helicase activity of the enzyme. Both the N-terminal region and the helicase activity contribute to the suppression of homologous recombination, only the N-terminus, not the C-terminus, defines the functional specificity. Structure-function relationship analysis
additional information
structure comparisons of SF1 and SF2 helicases, SF1 and SF2 helicase domains structures and substrate-bound SF1 and SF2 helicase structures, structure-function relationship, overview
additional information
structure comparisons of SF1 and SF2 helicases, SF1 and SF2 helicase domains structures and substrate-bound SF1 and SF2 helicase structures, structure-function relationship, overview
additional information
structure comparisons of SF1 and SF2 helicases, SF1 and SF2 helicase domains structures and substrate-bound SF1 and SF2 helicase structures, structure-function relationship, overview
additional information
structure comparisons of SF1 and SF2 helicases, SF1 and SF2 helicase domains structures and substrate-bound SF1 and SF2 helicase structures, structure-function relationship, overview
additional information
structure comparisons of SF1 and SF2 helicases, SF1 and SF2 helicase domains structures and substrate-bound SF1 and SF2 helicase structures, structure-function relationship, overview
additional information
structure comparisons of SF1 and SF2 helicases, SF1 and SF2 helicase domains structures and substrate-bound SF1 and SF2 helicase structures, structure-function relationship, overview
additional information
protein-DNA crosslinking defines strand-specific interactions for the PriA ARL, 3'BD and helicase core with a DNA replication fork substrate. PriA-DNA fork crosslinking maps strand- and residue-specific interactions. Modeling of PriA domains predicted to bind to specific DNA regions of an abandoned DNA fork, with location of Bpa incorporation, overview. Reproducible crosslinks to the four-stranded DNA substrate are observed with D17Bpa, Q329Bpa (low level), Q330Bpa, E331Bpa and E492Bpa
additional information
some unwinding events occur with a uniform rate, denoted as the normal (N) mode whereas other events present a slower and non-uniform unwinding rate denoted as the slow (S) mode. This bimodal behavior has not been previously identified in ensemble assays. The N mode is characterized by a uniform rate of 62 bp/s at saturating ATP and 29°C (90 bp/s at 37°C), whereas the S mode unwinding is characterized by frequent pauses and backtracks in an apparent persistent random walk at a rate of 15-25 bp/s at 29°C. Individual helicases can switch between the two modes within a single event. Wild-type RecQ can also pass the loop apex of the DNA hairpin and continue translocating on the ssDNA produced by unwinding. In this case, the extent to which the hairpin refolds is dictated by the position of the helicase, which blocks DNA reannealing at the enzyme position. The WH domain plays a role in DNA binding and in DNA unwinding. Structure-function analysis of wild-type and mutant RecQ enzymes, detailed overview. The strand-switching behavior is observed with RecQ proteins that contain a WH domain (wild-type RecQ and RecQ-DELTAC) but not in the variant lacking the WH domain
additional information
-
some unwinding events occur with a uniform rate, denoted as the normal (N) mode whereas other events present a slower and non-uniform unwinding rate denoted as the slow (S) mode. This bimodal behavior has not been previously identified in ensemble assays. The N mode is characterized by a uniform rate of 62 bp/s at saturating ATP and 29°C (90 bp/s at 37°C), whereas the S mode unwinding is characterized by frequent pauses and backtracks in an apparent persistent random walk at a rate of 15-25 bp/s at 29°C. Individual helicases can switch between the two modes within a single event. Wild-type RecQ can also pass the loop apex of the DNA hairpin and continue translocating on the ssDNA produced by unwinding. In this case, the extent to which the hairpin refolds is dictated by the position of the helicase, which blocks DNA reannealing at the enzyme position. The WH domain plays a role in DNA binding and in DNA unwinding. Structure-function analysis of wild-type and mutant RecQ enzymes, detailed overview. The strand-switching behavior is observed with RecQ proteins that contain a WH domain (wild-type RecQ and RecQ-DELTAC) but not in the variant lacking the WH domain
additional information
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structure comparisons of SF1 and SF2 helicases, SF1 and SF2 helicase domains structures and substrate-bound SF1 and SF2 helicase structures, structure-function relationship, overview
-
additional information
-
structure comparisons of SF1 and SF2 helicases, SF1 and SF2 helicase domains structures and substrate-bound SF1 and SF2 helicase structures, structure-function relationship, overview
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K116H
an MBP-Rep52 chimera bearing K116H mutation within a consensus helicase- and ATPase-associated motif (motif I or Walker A site) is deficient for both DNA helicase and ATPase activities
K340H
in a Rep78 A-site mutant protein bearing mutation K340H, the MBP-Rep52 A-site mutant protein fails to exhibit a trans-dominant negative effect when it is mixed with wild-type MBP-Rep52 or MBP-Rep78 in vitro
K481M
site-directed mutagenesis in the Walker A motif of the helicase domain
C261A
-
mutant with a disrupted zinc-binding site. One mol of the C261A mutant contains 0.03 atoms
K653A
-
mutation of the ATP-binding site reduces activity to about 30% of wild-type. This drop in ATPase activity corresponds to an abrogation of helicase activity observed in the same mutant
K898N
-
ATPase-dead mutant which does not exhibit helicase activity
K230A
site-directed mutagenesis, a Walker A mutant, mutation of a lysine from motif I that is essential for ATPase activity, inactive mutant, used as negative control
K328A
site-directed mutagenesis, 3-4fold reduced kcat compared to wild-type
Q329A
site-directed mutagenesis, 2fold reduced kcat compared to wild-type
Q330A
site-directed mutagenesis, 3-4fold reduced kcat compared to wild-type
R334A
site-directed mutagenesis, 3-4fold reduced kcat compared to wild-type
W333A
site-directed mutagenesis, 12fold reduced kcat compared to wild-type
Y335A
site-directed mutagenesis, 14fold reduced kcat compared to wild-type
H293A
-
mutation results in a protein with a significantly higher level of ATPase in the absence of RNA. The mutant protein still unwinds RNA. In the presence of RNA, the H293A mutant hydrolyzes ATP slower than wild-type
D523N
DNA binding and ATPase activity is comparable to wild-type enzyme, no in vitro replication activity
D542N
DNA binding and ATPase activity is comparable to wild-type enzyme, no in vitro replication activity
K484E
mutant enzyme binds the immunoaffinity column poorly, the heparin purified E1/K484E is tested for the above activities. The protein that is recovered shows no activity
P479S
DNA binding and ATPase activity is comparable to wild-type enzyme, 50% of in vitro replication activity compared to wild-type enzyme
D327A
about 75% of wild-type helicase activity
D488A
mutant has an apparent increase in helicase activity but a reduction in ATPase activity to approximately one third of wild-type levels. This mutant has a gel filtration profile compatible with a dimer or trimer. All other proteins appear hexameric
E202G/E203G/V204G
mutant shows no helicase activity
E307A
-
inactive in DNA unwinding and partially active in the ATPase assay
E326A
about 95% of wild-type helicase activity
E326A/D327A
about 85% of wild-type helicase activity
E326A/D327A/R329A
mutant shows no helicase activity
E422A
up to 2fold higher affinity for the DNA substrate than the wild-type enzyme. ATPase activity and helicase activity are similar to wild-type enzyme
E422R
has the same affinity as the wild-type enzyme. No ability to hydrolyse ATP, no helicase activity
E422R/R329E
mutant lacks detectable ATPase and helicase activities
I555D/L556S/I557D
mutant shows no helicase activity
K246A/R247A
indistinguishable from wild-type protein with respect to heat stability. ATPase activity of the mutated protein does not increase in the presence of DNA. Mutation reduces DNA binding
K246A/R247A/K430A
completely inactive as a helicase, ATPase activity of the mutated protein does not increase in the presence of DNA, indistinguishable from wild-type protein with respect to heat stability
K265A/E307A
-
completely abolished ATPase activity
K265A/R372I
-
completely abolished ATPase activity
K323A/R440A
reduced helicase activity
K366E
severely compromised helicase activity but only a modest reduction in ATPase activity
K430A
completely inactive as a helicase, ATPase activity of the mutated protein does not increase in the presence of DNA, indistinguishable from wild-type protein with respect to heat stability
K52A
mutant is unable to function as a helicase
K646stop
mutant lacking domain 5 shows significantly faster rates of DNA unwinding than the wild-type protein
L325A
about 40% of wild-type helicase activity
L565D
has the same affinity as the wild-type enzyme. ATPase properties similar to wild-type enzyme, significant stimulation of helicase activity
L565K
up to 2fold lower affinity for the DNA substrate than the wild-type enzyme. ATPase properties similar to wild-type enzyme, significant stimulation of helicase activity
R255A
mutant shows significantly reduced helicase activity
R320A
mutant shows significantly reduced helicase activity
R329A
about 50% of wild-type helicase activity
R329E
up to 2fold lower affinity for the DNA substrate than the wild-type enzyme. Low and non-DNA-stimulated ATPase activity. Helicase activity is similar to wild-type enzyme
R331A
no ATPase activity, no helicase activity
R331I
has the same affinity as the wild-type enzyme. No ability to hydrolyse ATP, no helicase activity
R331K
up to 2fold higher affinity for the DNA substrate than the wild-type enzyme. ATPase properties similar to wild-type enzyme. Helicase activity at approximately half the level of wild-type enzyme
R359A
severely compromised helicase activity but only a modest reduction in ATPase activity
R372I
-
very low levels of ATPase activity and no helicase activity
R440A
reduced helicase activity
R662A
mutant lacking the first arginine of the RAR motif in domain 5 shows significantly faster rates of DNA unwinding than the wild-type protein
T374A
reduced but detectable helicase activity with an increase in ATPase activity
T550G/P551G/D552G/S553G/P554G
mutant shows no helicase activity
V324A
about 90% of wild-type helicase activity
V324A/L325A
about 80% of wild-type helicase activity
K52A
-
mutant is unable to function as a helicase
-
K646stop
-
mutant lacking domain 5 shows significantly faster rates of DNA unwinding than the wild-type protein
-
R255A
-
mutant shows significantly reduced helicase activity
-
R320A
-
mutant shows significantly reduced helicase activity
-
R662A
-
mutant lacking the first arginine of the RAR motif in domain 5 shows significantly faster rates of DNA unwinding than the wild-type protein
-
D327A
-
about 75% of wild-type helicase activity
-
D488A
-
mutant has an apparent increase in helicase activity but a reduction in ATPase activity to approximately one third of wild-type levels. This mutant has a gel filtration profile compatible with a dimer or trimer. All other proteins appear hexameric
-
E307A
-
inactive in DNA unwinding and partially active in the ATPase assay
-
E326A
-
about 95% of wild-type helicase activity
-
K134A
-
mutation affects binding to duplex DNA molecules, whereas it has no effect on binding to single-stranded DNA and on the DNA unwinding activity
-
K246A/R247A
-
indistinguishable from wild-type protein with respect to heat stability. ATPase activity of the mutated protein does not increase in the presence of DNA. Mutation reduces DNA binding
-
K246A/R247A/K430A
-
completely inactive as a helicase, ATPase activity of the mutated protein does not increase in the presence of DNA, indistinguishable from wild-type protein with respect to heat stability
-
K265A/E307A
-
completely abolished ATPase activity
-
K265A/R372I
-
completely abolished ATPase activity
-
K323A
-
about 40% of wild-type helicase activity
-
K366E
-
severely compromised helicase activity but only a modest reduction in ATPase activity
-
K430A
-
completely inactive as a helicase, ATPase activity of the mutated protein does not increase in the presence of DNA, indistinguishable from wild-type protein with respect to heat stability
-
R331A
-
no ATPase activity, no helicase activity
-
R359A
-
severely compromised helicase activity but only a modest reduction in ATPase activity
-
R372I
-
very low levels of ATPase activity and no helicase activity
-
T374A
-
reduced but detectable helicase activity with an increase in ATPase activity
-
A416R/A420R
mutant shows no helicase activity
A416R/A420R
near abrogation of helicase activity
A416R/A420R
no helicase activity detectable, wild-type protein exists as hexamers, mutants protein elutes predominantly in the monomer peak
H146A
mutant enzyme is unable to bind DNA either in single- or double-stranded form and does not display helicase activity
H146A
the purified mutant enzyme retains full ATPase activity
K129A
mutant enzyme is unable to bind DNA either in single- or double-stranded form and does not display helicase activity
K129A
the purified mutant enzyme retains full ATPase activity
K134A
mutation affects binding to duplex DNA molecules, whereas it has no effect on binding to single-stranded DNA and on the DNA unwinding activity
K134A
the purified mutant enzyme retains full ATPase activity
K194A
mutant enzyme is unable to bind DNA either in single- or double-stranded form and does not display helicase activity
K194A
the purified mutant enzyme retains full ATPase activity
K323A
about 40% of wild-type helicase activity
K323A
reduced helicase activity
K346A
ATPase activity of the mutant is noticeably reduced, although not completely abolished, it is almost completely devoid of helicase activity
K346A
no ATPase activity, no helicase activity
L189D/D191R
mutant shows no helicase activity
L189D/D191R
near abrogation of helicase activity
L189D/D191R
no helicase activity detectable, wild-type protein exists as hexamers, mutants protein elutes predominantly in the monomer peak
A416R/A420R
-
mutant shows no helicase activity
-
A416R/A420R
-
near abrogation of helicase activity
-
H146A
-
mutant enzyme is unable to bind DNA either in single- or double-stranded form and does not display helicase activity
-
H146A
-
the purified mutant enzyme retains full ATPase activity
-
K129A
-
mutant enzyme is unable to bind DNA either in single- or double-stranded form and does not display helicase activity
-
K129A
-
the purified mutant enzyme retains full ATPase activity
-
K346A
-
no ATPase activity, no helicase activity
-
K346A
-
ATPase activity of the mutant is noticeably reduced, although not completely abolished, it is almost completely devoid of helicase activity
-
L189D/D191R
-
mutant shows no helicase activity
-
L189D/D191R
-
near abrogation of helicase activity
-
L189D/D191R
-
no helicase activity detectable, wild-type protein exists as hexamers, mutants protein elutes predominantly in the monomer peak
-
K318A
site-directed mutagenesis, the mutant shows reduced activity and DNA binding, and increased KD value compared to wild-type. Neither wild-type Hrq1 nor Hrq1-K318A have any effect on overall telomerase activity, no effect on telomerase extension of the Tel15 and Tel30 primers
K318A
-
site-directed mutagenesis, the mutant shows reduced activity and DNA binding, and increased KD value compared to wild-type. Neither wild-type Hrq1 nor Hrq1-K318A have any effect on overall telomerase activity, no effect on telomerase extension of the Tel15 and Tel30 primers
-
E355A
mutation results in loss of ATPase and DNA helicase activities, and also dsDNA-binding ability, indicating that this residue is involved in the coupling of ATP hydrolysis, dsDNA-binding, and helicase activities
E355A
-
mutation results in loss of ATPase and DNA helicase activities, and also dsDNA-binding ability, indicating that this residue is involved in the coupling of ATP hydrolysis, dsDNA-binding, and helicase activities
-
additional information
the helicase core is able to regress an artificial replication fork. Swapping of the terminal regions of RECQ4A with the closely related but functionally distinct helicase RECQ4B indicates that in contrast to the C-terminus, the N-terminus of RECQ4A is required for its specific functions in DNA repair and recombination. Generation of diverse enzyme mutants and transgenic Arabidopsis thaliana plants, complementation of the recq4A-4 mutant, different RECQ4A constructs are cloned including a full-length wild-type construct (RECQ4A) and different variants of the RECQ4A ORF in which individual domains are modified or deleted, RECQ4A-HD, RECQ4A-DN, RECQ4A-DN-HD, RECQ-(4B)4A and RECQ-4A(4B), respectively. The recq4A-4 mutant is hypersensitive to treatment with cisplatin
additional information
construction of PriA incorporated with 4-benzoyl-L-phenylalanine (Bpa), the priA open reading frame is subcloned from pET15-EcPriA into pBAD/His B vector and subjected to site-directed mutagenesis to substitute an amber stop codon (TAG) at specific EcPriA codons targeted for Bpa substitution
additional information
generation of several truncated RecQ enzyme mutants, i.e. RecQ-DELTAC and RecQ-DELTADELTAC proteins. The strand-switching behavior is observed with RecQ proteins that contain a WH domain (wild-type RecQ and RecQ-DELTAC) but not in the variant lacking the WH domain. Structure-function analysis of wild-type and mutant RecQ enzymes, overview. SSB strongly stimulates the unwinding activity of the RecQ-DELTADELTAC protein
additional information
-
generation of several truncated RecQ enzyme mutants, i.e. RecQ-DELTAC and RecQ-DELTADELTAC proteins. The strand-switching behavior is observed with RecQ proteins that contain a WH domain (wild-type RecQ and RecQ-DELTAC) but not in the variant lacking the WH domain. Structure-function analysis of wild-type and mutant RecQ enzymes, overview. SSB strongly stimulates the unwinding activity of the RecQ-DELTADELTAC protein
additional information
-
a mutation of the zinc finger motif of the MCM protein reduces single-stranded and double-stranded DNA binding and abolishes helicase activity. Removal of the HTH domain from the MCM protein results in an enzyme with increased ATPase and helicase activity. A mutation of the MCM N-terminal beta-hairpin completely abolishes DNA binding and helicase activity
additional information
generation of osteoblast-specific Recql4 deficient mice. Acute deletion of Recql4 in primary osteoblasts or shRNA knockdown in an osteoblastic cell line causing failed proliferation, accompanied by cell cycle arrest, induction of apoptosis and impaired differentiation. When cohorts of animals are aged long term, the loss of Recql4 alone is not sufficient to initiate OS. The Recql4fl/fl allele is crossed to a fully penetrant OS model (Osx-Cre p53fl/fl). The Osx-Cre p53fl/flRecql4fl/fl (dKO) animals have a significantly increased OS-free survival compared to Osx-Cre p53fl/fl or Osx-Cre p53fl/flRecql4fl/+ (het) animals. The extended survival is explained when the Recql4 status in the tumors that arose is assessed, and in no case is there complete deletion of Recql4 in the dKO OS. Tumor suppression and osteosarcoma susceptibility are most likely a function of mutant, not null, alleles of RECQL4. Reduced skeletal growth in Osx-Cre Recql4fl/fl mice
additional information
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generation of osteoblast-specific Recql4 deficient mice. Acute deletion of Recql4 in primary osteoblasts or shRNA knockdown in an osteoblastic cell line causing failed proliferation, accompanied by cell cycle arrest, induction of apoptosis and impaired differentiation. When cohorts of animals are aged long term, the loss of Recql4 alone is not sufficient to initiate OS. The Recql4fl/fl allele is crossed to a fully penetrant OS model (Osx-Cre p53fl/fl). The Osx-Cre p53fl/flRecql4fl/fl (dKO) animals have a significantly increased OS-free survival compared to Osx-Cre p53fl/fl or Osx-Cre p53fl/flRecql4fl/+ (het) animals. The extended survival is explained when the Recql4 status in the tumors that arose is assessed, and in no case is there complete deletion of Recql4 in the dKO OS. Tumor suppression and osteosarcoma susceptibility are most likely a function of mutant, not null, alleles of RECQL4. Reduced skeletal growth in Osx-Cre Recql4fl/fl mice
additional information
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construction of an enzyme knockout PfRecQ1DELTA strain D3. Deletion of PfRecQ1 increases the heterochromatin mark trimethylated (H3K9me3) at the transcription start site (TSS) of the var gene upsC1, that deletion has no effect on the global distribution of H3K9me3 over gene bodies, including those for the var genes. Upon PfRecQ1 deletion, the upsC1 var gene moves from the active perinuclear transcription region to a silenced region of the upsC type, implying that PfRecQ1, but not PfWRN, is essential for maintaining the clonal expression of var genes
additional information
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construction of an enzyme knockout PfRecQ1DELTA strain D3. Deletion of PfRecQ1 increases the heterochromatin mark trimethylated (H3K9me3) at the transcription start site (TSS) of the var gene upsC1, that deletion has no effect on the global distribution of H3K9me3 over gene bodies, including those for the var genes. Upon PfRecQ1 deletion, the upsC1 var gene moves from the active perinuclear transcription region to a silenced region of the upsC type, implying that PfRecQ1, but not PfWRN, is essential for maintaining the clonal expression of var genes
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additional information
a mutation of the MCM N-terminal beta-hairpin reduces but does not abolish DNA binding and helicase activity
additional information
the enzyme can tolerate catalytically inactive subunits and still function as a helicase. A mode of intersubunit communication within mini-chromosome maintenance complex supports a semisequential model for harnessing the energy of ATP binding, hydrolysis, and release in the generation of helicase activity
additional information
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the enzyme can tolerate catalytically inactive subunits and still function as a helicase. A mode of intersubunit communication within mini-chromosome maintenance complex supports a semisequential model for harnessing the energy of ATP binding, hydrolysis, and release in the generation of helicase activity
additional information
-
the enzyme can tolerate catalytically inactive subunits and still function as a helicase. A mode of intersubunit communication within mini-chromosome maintenance complex supports a semisequential model for harnessing the energy of ATP binding, hydrolysis, and release in the generation of helicase activity
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Plasmodium falciparum (Q8IAR1), Plasmodium falciparum
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