Literature summary for 5.6.2.3 extracted from

George, T.; Wen, Q.; Griffiths, R.; Ganesh, A.; Meuth, M.; Sanders, C.M.
Human Pif1 helicase unwinds synthetic DNA structures resembling stalled DNA replication forks (2009), Nucleic Acids Res., 37, 6491-6502.

Search for more literature for 5.6.2.3

Cloned(Commentary)

Cloned (Comment)	Organism
human hPif1 (nuclear form amino acids 1641) and the hPif helicase domain (hPifHD, amino acid residues 206620) are cloned as a fusion protein with glutathione S-transferase in pET11c. GST-hPifHD is expressed in Escherichia coli BL21(DE3) cells	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9H611	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O	hPifHD (core helicase domain) only unwinds the substrate with a 5' single-stranded DNA (ssDNA) overhang and is a 5' to 3' helicase. Pif1 specifically recognizes and unwinds DNA structures resembling putative stalled replication forks. Notably, the enzyme requires both arms of the replication fork-like structure to initiate efficient unwinding of the putative leading replication strand of such substrates. This DNA structure-specific mode of initiation of unwinding is intrinsic to the conserved core helicase domain (hPifHD) that also possesses a strand annealing activity	Homo sapiens	ADP + phosphate	-	?

Synonyms

Synonyms	Comment	Organism
hPif1	-	Homo sapiens
PIF1 helicase	-	Homo sapiens

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Release 2023.1 (January 2023)