the methyltransferase RsmG methylates the N7 position of nucleotide G535 in 16S rRNA of Bacillus subtilis (corresponding to G527 in Escherichia coli). Nucleotide G527 is situated within a hairpin loop (the socalled 530 loop) that is one of the most highly conserved features of 16S rRNA
the methyltransferase RsmG methylates the N7 position of nucleotide G535 in 16S rRNA of Bacillus subtilis (corresponding to G527 in Escherichia coli), identification of the exact target site of RsmG methylation
the methyltransferase RsmG methylates the N7 position of nucleotide G535 in 16S rRNA of Bacillus subtilis (corresponding to G527 in Escherichia coli). Nucleotide G527 is situated within a hairpin loop (the socalled 530 loop) that is one of the most highly conserved features of 16S rRNA
the methyltransferase RsmG methylates the N7 position of nucleotide G535 in 16S rRNA of Bacillus subtilis (corresponding to G527 in Escherichia coli), identification of the exact target site of RsmG methylation
methylations concentrated in the decoding site of the 30S ribosomal subunit may act to fine tune codon recognition in a manner similar to tRNA modifications. The intact 30S subunit is very unlikely to be the natural substrate for Thermus thermophilus RsmG in vivo. This interpretation is consistent with the position of G527 in the intact 30S subunit, where it is buried and would be inaccessible for methylation without substantial unfolding of the local subunit structure. Deproteinized 16S rRNA is the most active substrate in vitro. In vivo, several ribosomal proteins probably begin binding to the nascent 16S rRNA transcript prior to its completion, making an early assembly intermediate a plausible candidate for the biological substrate of RsmG
the most active substrate for Thermus thermophilus RsmG in vitro is deproteinized 16S rRNA. 30S subunits in their native conformation are not a proper substrate, removal of Mg2+ ions from the subunit is required to open the structure sufficiently to expose elements involved in enzyme binding. Identification of methylated nucleotide
methylations concentrated in the decoding site of the 30S ribosomal subunit may act to fine tune codon recognition in a manner similar to tRNA modifications. The intact 30S subunit is very unlikely to be the natural substrate for Thermus thermophilus RsmG in vivo. This interpretation is consistent with the position of G527 in the intact 30S subunit, where it is buried and would be inaccessible for methylation without substantial unfolding of the local subunit structure. Deproteinized 16S rRNA is the most active substrate in vitro. In vivo, several ribosomal proteins probably begin binding to the nascent 16S rRNA transcript prior to its completion, making an early assembly intermediate a plausible candidate for the biological substrate of RsmG
the most active substrate for Thermus thermophilus RsmG in vitro is deproteinized 16S rRNA. 30S subunits in their native conformation are not a proper substrate, removal of Mg2+ ions from the subunit is required to open the structure sufficiently to expose elements involved in enzyme binding. Identification of methylated nucleotide
the methyltransferase RsmG methylates the N7 position of nucleotide G535 in 16S rRNA of Bacillus subtilis (corresponding to G527 in Escherichia coli). Nucleotide G527 is situated within a hairpin loop (the socalled 530 loop) that is one of the most highly conserved features of 16S rRNA
the methyltransferase RsmG methylates the N7 position of nucleotide G535 in 16S rRNA of Bacillus subtilis (corresponding to G527 in Escherichia coli). Nucleotide G527 is situated within a hairpin loop (the socalled 530 loop) that is one of the most highly conserved features of 16S rRNA
methylations concentrated in the decoding site of the 30S ribosomal subunit may act to fine tune codon recognition in a manner similar to tRNA modifications. The intact 30S subunit is very unlikely to be the natural substrate for Thermus thermophilus RsmG in vivo. This interpretation is consistent with the position of G527 in the intact 30S subunit, where it is buried and would be inaccessible for methylation without substantial unfolding of the local subunit structure. Deproteinized 16S rRNA is the most active substrate in vitro. In vivo, several ribosomal proteins probably begin binding to the nascent 16S rRNA transcript prior to its completion, making an early assembly intermediate a plausible candidate for the biological substrate of RsmG
methylations concentrated in the decoding site of the 30S ribosomal subunit may act to fine tune codon recognition in a manner similar to tRNA modifications. The intact 30S subunit is very unlikely to be the natural substrate for Thermus thermophilus RsmG in vivo. This interpretation is consistent with the position of G527 in the intact 30S subunit, where it is buried and would be inaccessible for methylation without substantial unfolding of the local subunit structure. Deproteinized 16S rRNA is the most active substrate in vitro. In vivo, several ribosomal proteins probably begin binding to the nascent 16S rRNA transcript prior to its completion, making an early assembly intermediate a plausible candidate for the biological substrate of RsmG
S-adenosyl-L-methionine is bound in a canonical conformation above the beta-sheet and close to the conserved GxGxG methyltransferase signature motif (residues 8892 between strand beta1 and helix alpha4). The AdoMet cofactor is tightly bound in RsmG and copurifies with the recombinant protein
the 30S subunits in their native conformation are not a proper substrate and removal of Mg2+ ions from the subunit is required to open the structure sufficiently to expose elements involved in enzyme binding
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Sepsis
High Prevalence of 16S rRNA Methyltransferase Genes in Carbapenem-Resistant Klebsiella pneumoniae Clinical Isolates Associated with Bloodstream Infections in 11 Chinese Teaching Hospitals.
RsmG is an S-adenosyl-L-methionine-dependent methyltransferase responsible for the synthesis of m7G527 in the 530 loop of bacterial 16S rRNA. This loop is universally conserved, plays a key role in ribosomal accuracy, and is a target for streptomycin binding, mechanisms controlling RsmG expression and activity, overview. Gene rsmG as part of a bicistronic operon also has its own promoter, which appears, in actively growing cells, as a control device to offset both the relatively low stability of RsmG and inhibition of the operon promoter. Critical importance of some residues located in the active site of Escherichia coli RsmG for the m7G modification process, the residues play a role in rRNA binding and catalysis
construction of an rsmG null allele by deleting the rsmG coding sequence and replacing it with htk, encoding a heat-stable kanamycin adenyltransferase. This null allele retains the very N- and C-terminal rsmG coding sequences, in-frame with the htk coding sequence, in order to maintain the rsmGparA overlap and minimize any effects on parA expression. This allele is designated DrsmGThtk2 and the mutant containing this allele is designated HG 917. Thermus thermophilus rsmG mutants are weakly resistant to the aminoglycoside antibiotic streptomycin. Growth competition experiments indicate a physiological cost to loss of RsmG activity, consistent with the conservation of the modification site in the decoding region of the ribosome
mutations within the gene gidB confer low-level streptomycin resistance. gidB Mmutations emerge spontaneously at a high frequency of 0.000001 and, once emerged, result in vigorous emergence of high-level streptomycin-resistant mutants at a frequency more than 2000 times greater than that seen in wild-type strains
that the DELTArsmG mutant lacks a 7-methylguanosine modification in the 16S rRNA (possibly at position G518, which corresponds to G527 of Escherichia coli). The DELTArsmG mutant exhibits enhanced protein synthetic activity during the late growth phase. The DELTArsmG mutant shows neither greater stability of the 70S ribosomal complex nor increased expression of ribosome recycling factor
the rsmG mutants show impaired ability to form aerial mycelia, and are somewhat deficient in sporulation. rsmG mutants show greater ability (two- to threefold) to produce streptomycin. The rsmG mutant exhibits elevated levels of metK, strR, strB1, strF and strD expression compared with the wild-type strain at late growth phase (36 h), thus underlying the enhanced production of streptomycin in the rsmG mutant. rsmG mutation is effective not only for enhancement of streptomycin production but also for activation of silent or poorly expressed genes in Streptomyces griseus
that the DELTArsmG mutant lacks a 7-methylguanosine modification in the 16S rRNA (possibly at position G518, which corresponds to G527 of Escherichia coli). The DELTArsmG mutant exhibits enhanced protein synthetic activity during the late growth phase. The DELTArsmG mutant shows neither greater stability of the 70S ribosomal complex nor increased expression of ribosome recycling factor
mutations within the gene gidB confer low-level streptomycin resistance. gidB Mmutations emerge spontaneously at a high frequency of 0.000001 and, once emerged, result in vigorous emergence of high-level streptomycin-resistant mutants at a frequency more than 2000 times greater than that seen in wild-type strains
construction of an rsmG null allele by deleting the rsmG coding sequence and replacing it with htk, encoding a heat-stable kanamycin adenyltransferase. This null allele retains the very N- and C-terminal rsmG coding sequences, in-frame with the htk coding sequence, in order to maintain the rsmGparA overlap and minimize any effects on parA expression. This allele is designated DrsmGThtk2 and the mutant containing this allele is designated HG 917. Thermus thermophilus rsmG mutants are weakly resistant to the aminoglycoside antibiotic streptomycin. Growth competition experiments indicate a physiological cost to loss of RsmG activity, consistent with the conservation of the modification site in the decoding region of the ribosome
the rsmG mutants show impaired ability to form aerial mycelia, and are somewhat deficient in sporulation. rsmG mutants show greater ability (two- to threefold) to produce streptomycin. The rsmG mutant exhibits elevated levels of metK, strR, strB1, strF and strD expression compared with the wild-type strain at late growth phase (36 h), thus underlying the enhanced production of streptomycin in the rsmG mutant. rsmG mutation is effective not only for enhancement of streptomycin production but also for activation of silent or poorly expressed genes in Streptomyces griseus
positively charged residues on the protein surface around the active site, K100/R101, R123, K165, and R197, might play a role in the binding of the incoming 530 loop since their change to alanine impairs the modification function of RsmG
positively charged residues on the protein surface around the active site, K100/R101, R123, K165, and R197, might play a role in the binding of the incoming 530 loop since their change to alanine impairs the modification function of RsmG
microbatch technique under oil at 4°C. Determination of the structure of RsmG (249 amino acids) in three different crystal forms: the enzyme in complex with the cofactor S-adensosyl-L-methionine, the enzyme in complex with S-adenosyl-L-homocysteine, the enzyme in complex with adenosine monophosphate and S-adenosyl-L-methionine. RsmG X-ray crystal structures at up to 1.5 A resolution. Cofactor-bound crystal structures of RsmG reveals a positively charged surface area remote from the active site that binds an adenosine monophosphate molecule
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-sensitive and shows reduced activity compared to the wild-type enzyme
site-directed mutagenesis of the catalytic residue, the mutant is partly streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
site-directed mutagenesis of the RNA binding residue, the mutant is streptomycin-sensitive, but shows reduced activity compared to the wild-type enzyme
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
site-directed mutagenesis of the RNA-binding residue, the mutant is streptomycin-sensitive, but shows reduced activity compared to the wild-type enzyme
site-directed mutagenesis of the catalytic residue, the mutant is partly streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
mutations within the gene gidB confer low-level streptomycin resistance. gidB mutations emerge spontaneously at a high frequency of 0.000001 and, once emerged, result in vigorous emergence of high-level streptomycin-resistant mutants at a frequency more than 2000 times greater than that seen in wild-type strains
mutations within the gene gidB confer low-level streptomycin resistance. gidB mutations emerge spontaneously at a high frequency of 0.000001 and, once emerged, result in vigorous emergence of high-level streptomycin-resistant mutants at a frequency more than 2000 times greater than that seen in wild-type strains
gene rsmG is the second member in a bicistronic operon, rsmG also has its own promoter, RsmG expression might depend on the activity of an inverted repeated region, located between the rsmG promoter and ribosome binding site, which works as a weak transcriptional terminator. Expression of C-terminally His6-tagged and FLAG-tagged RsmG in Escherichia coli TOP10 cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
RsmG levels decrease under conditions that down-regulate rRNA synthesis, but coordination between rRNA and RsmG expression does not seem to occur at the level of transcription initiation
Nishimura, K.; Hosaka, T.; Tokuyama, S.; Okamoto, S.; Ochi, K.
Mutations in rsmG, encoding a 16S rRNA methyltransferase, result in low-level streptomycin resistance and antibiotic overproduction in Streptomyces coelicolor A3(2)