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Information on EC 2.1.1.170 - 16S rRNA (guanine527-N7)-methyltransferase
for references in articles please use BRENDA:EC2.1.1.170
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.170 16S rRNA (guanine527-N7)-methyltransferase
IUBMB Comments
The enzyme specifically methylates guanine527 at N7 in 16S rRNA.
The enzyme appears in viruses and cellular organisms
- 2.1.1.170
- aminoglycoside
- amikacin
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esbls
- carbapenemase
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carbapenem-resistant
- 16s-rmtases
- blandm-1
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extended-spectrum
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carbapenemase-producing
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aminoglycoside-resistance
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blaoxa-48
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plazomicin
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coproducing
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rmtases
- kasugamycin
Reaction Schemes
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guanine527 in 16S rRNA
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N7-methylguanine527 in 16S rRNA
Synonyms
16s rrna methyltransferase, rsmg methyltransferase, ribosomal rna small subunit methyltransferase g, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
16S rRNA methyltransferase RsmG
gidB
ribosomal RNA small subunit methyltransferase G
ribosomal small subunit methyltransferase G
rsmG
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + guanine527 in 16S rRNA = S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:16S rRNA (guanine527-N7)-methyltransferase
The enzyme specifically methylates guanine527 at N7 in 16S rRNA.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
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Substrates: 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
Products: -
Products: -
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S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
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Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
-
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
-
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
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Substrates: GidB is a m7G methyltransferase specific for 16S rRNA, identification of methylated nucleotide
Products: -
Products: -
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S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
Substrates: RsmG binds to 30S 5'-domain and methylates N7 of G527 that is located at the highly conserved 530 loop of 16S helix 18. Substrates rRNAs and are 5'-leader rRNA fragments
Products: -
Products: -
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S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
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Substrates: GidB is a m7G methyltransferase specific for 16S rRNA, identification of methylated nucleotide
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
Substrates: RsmG binds to 30S 5'-domain and methylates N7 of G527 that is located at the highly conserved 530 loop of 16S helix 18. Substrates rRNAs and are 5'-leader rRNA fragments
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
-
Substrates: the methyltransferase RsmG methylates the N7 position of nucleotide G535 in 16S rRNA of Bacillus subtilis (corresponding to G527 in Escherichia coli)
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
-
Substrates: the methyltransferase RsmG methylates the N7 position of nucleotide G535 in 16S rRNA of Bacillus subtilis (corresponding to G527 in Escherichia coli)
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
Substrates: 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
Products: -
Products: -
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S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
Substrates: 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
Products: -
Products: -
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S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Substrates: 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
Products: -
Products: -
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S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Substrates: 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
Products: -
Products: -
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additional information
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Substrates: the pseudoknot mutant (PKMut) G505A/C507U for 5'-domain RNA is obtained by site-directed mutagenesis. All 5'-domain RNA constructs are extended at the 3'-end to base pair with a fluorophore-labelled complementary DNA oligomer and in vitro transcribed
Products: -
Products: -
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additional information
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Substrates: RsmG enzyme binds to Escherichia coli small subunit precursor rRNAs. Ability of RsmG to bind various premature small subunit ribosomal RNAs with contrasting affinities, overview. Protein RsmG binds with approximately 15times higher affinity to premature 16S rRNA with the full leader sequence compared to that of mature 16S rRNA. Various r-proteins which bind to the 5'-domain influence RsmG binding. The binding cooperativity between RsmG and r-proteins is sensitive to the maturation status of premature small subunit rRNA. But neither the maturation of 16S rRNA nor the presence of various r-proteins significantly influence the methylation activity of RsmG
Products: -
Products: -
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additional information
?
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Substrates: the pseudoknot mutant (PKMut) G505A/C507U for 5'-domain RNA is obtained by site-directed mutagenesis. All 5'-domain RNA constructs are extended at the 3'-end to base pair with a fluorophore-labelled complementary DNA oligomer and in vitro transcribed
Products: -
Products: -
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additional information
?
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Substrates: RsmG enzyme binds to Escherichia coli small subunit precursor rRNAs. Ability of RsmG to bind various premature small subunit ribosomal RNAs with contrasting affinities, overview. Protein RsmG binds with approximately 15times higher affinity to premature 16S rRNA with the full leader sequence compared to that of mature 16S rRNA. Various r-proteins which bind to the 5'-domain influence RsmG binding. The binding cooperativity between RsmG and r-proteins is sensitive to the maturation status of premature small subunit rRNA. But neither the maturation of 16S rRNA nor the presence of various r-proteins significantly influence the methylation activity of RsmG
Products: -
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
-
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
-
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: the pseudoknot mutant (PKMut) G505A/C507U for 5'-domain RNA is obtained by site-directed mutagenesis. All 5'-domain RNA constructs are extended at the 3'-end to base pair with a fluorophore-labelled complementary DNA oligomer and in vitro transcribed
Products: -
Products: -
-
additional information
?
-
Substrates: the pseudoknot mutant (PKMut) G505A/C507U for 5'-domain RNA is obtained by site-directed mutagenesis. All 5'-domain RNA constructs are extended at the 3'-end to base pair with a fluorophore-labelled complementary DNA oligomer and in vitro transcribed
Products: -
Products: -
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-adenosyl-L-methionine
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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
activity of rsmGp slightly increases by fourfold when cells are grown in minimal media supplemented with glycerol instead of glucose
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additional information
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activity of rsmGp slightly increases by fourfold when cells are grown in minimal media supplemented with glycerol instead of glucose
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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.
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
activity of rsmGp slightly increases by fourfold when cells are grown in minimal media supplemented with glycerol instead of glucose
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
the enzyme is part of a SAM-dependent methyltransferase superfamily
evolution
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the enzyme is part of a SAM-dependent methyltransferase superfamily
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malfunction
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
malfunction
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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
malfunction
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
malfunction
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the rsmG mutants are as fit as the wild-type strain under the various culture conditions tested
malfunction
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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
malfunction
loss of the m7G527 modification confers low-level streptomycin resistance and may affect ribosomal functioning
malfunction
enzyme loss confers low-level streptomycin resistance and may affect ribosomal functioning
malfunction
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the rsmG mutants are as fit as the wild-type strain under the various culture conditions tested
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malfunction
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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
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malfunction
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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
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malfunction
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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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
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physiological function
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
physiological function
protein RsmG is a methyltransferase enzyme that is responsible for N7 methylation in G527 of 16S rRNA. The capability of RsmG to bind to premature small subunit rRNA and alter its binding preference to various RNA-protein complexes based on the maturation of rRNA indicates its ability to influence ribosome assembly
physiological function
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protein RsmG is a methyltransferase enzyme that is responsible for N7 methylation in G527 of 16S rRNA. The capability of RsmG to bind to premature small subunit rRNA and alter its binding preference to various RNA-protein complexes based on the maturation of rRNA indicates its ability to influence ribosome assembly
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additional information
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
additional information
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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
additional information
ribosomal assembly proteins differentially stabilize RsmG complexes formed by mature and precursor 30S 5'-domain rRNA, positive and negative cooperativity, respectively, independency of the Mg2+ concentration, overview RsmG preferably binds to a native-like helix 18 structure
additional information
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ribosomal assembly proteins differentially stabilize RsmG complexes formed by mature and precursor 30S 5'-domain rRNA, positive and negative cooperativity, respectively, independency of the Mg2+ concentration, overview RsmG preferably binds to a native-like helix 18 structure
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Show AA Sequence and Transmembrane Helices (7236 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapor diffusion at 4°C against a reservoir containing 0.1 M of sodium citrate pH 6.5, 15% polyethylene glycol 4000, and 10% isopropanol
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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D56A
site-directed mutagenesis of the catalytic residue, the mutant is streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
D71A
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-resistant and catalytically inactive
D96A
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-resistant and catalytically inactive
G73A
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
G75A
G77A
site-directed mutagenesis of the S-adenosyl-L-methionine-binding residue, the mutant is streptomycin-resistant and catalytically inactive
H53A
site-directed mutagenesis of the catalytic residue, the mutant is partly streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
K100A/R101A
site-directed mutagenesis of the RNA-binding residues, the mutant is streptomycin-resistant and catalytically inactive
K165A
site-directed mutagenesis of the RNA binding residue, the mutant is streptomycin-sensitive, but shows reduced activity compared to the wild-type enzyme
P79A
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
R123A
site-directed mutagenesis of the RNA-binding residue, the mutant is streptomycin-sensitive, but shows reduced activity compared to the wild-type enzyme
R139A
site-directed mutagenesis of the catalytic residue, the mutant is streptomycin-resistant and catalytically inactive
R139K
site-directed mutagenesis of the catalytic residue, the mutant is partly streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
R197A
site-directed mutagenesis of the RNA binding residue, the mutant is streptomycin-resistant and shows reduced activity compared to the wild-type enzyme
additional information
G75A
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
G75A
the mutation directly affects the S-adenosyl-L-methionine binding site, presents an almost 4fold loss of affinity and maintains the enzyme active
additional information
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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
additional information
-
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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant FLAG-tagged RsmG from Escherichia coli TOP10 cells by affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
the AdoMet cofactor is tightly bound in RsmG and copurifies with the recombinant protein
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
gene rsmG, recombinant overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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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
slight induction of rsmGp during stationary phase is independent of the stress-inducible sigma factor RpoS
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tanaka, Y.; Tokuyama, S.; Ochi, K.
Activation of secondary metabolite-biosynthetic gene clusters by generating rsmG mutations in Streptomyces griseus
J. Antibiot.
62
669-673
2009
Streptomyces griseus, Streptomyces griseus IFO13189
brenda
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)
J. Bacteriol.
189
3876-3883
2007
Streptomyces coelicolor (O54571), Streptomyces coelicolor
brenda
Nishimura, K.; Johansen, S.K.; Inaoka, T.; Hosaka, T.; Tokuyama, S.; Tahara, Y.; Okamoto, S.; Kawamura, F.; Douthwaite, S.; Ochi, K.
Identification of the RsmG methyltransferase target as 16S rRNA nucleotide G527 and characterization of Bacillus subtilis rsmG mutants
J. Bacteriol.
189
6068-6073
2007
Bacillus subtilis, Bacillus subtilis 168
brenda
Okamoto, S.; Tamaru, A.; Nakajima, C.; Nishimura, K.; Tanaka, Y.; Tokuyama, S.; Suzuki, Y.; Ochi, K.
Loss of a conserved 7-methylguanosine modification in 16S rRNA confers low-level streptomycin resistance in bacteria
Mol. Microbiol.
63
1096-1106
2007
Escherichia coli, Escherichia coli BW25113
brenda
Romanowski, M.J.; Bonanno, J.B.; Burley, S.K.
Crystal structure of the Escherichia coli glucose-inhibited division protein B (GidB) reveals a methyltransferase fold
Proteins
47
563-567
2002
Escherichia coli (P0A6U5), Escherichia coli
brenda
Gregory, S.T.; Demirci, H.; Belardinelli, R.; Monshupanee, T.; Gualerzi, C.; Dahlberg, A.E.; Jogl, G.
Structural and functional studies of the Thermus thermophilus 16S rRNA methyltransferase RsmG
RNA
15
1693-1704
2009
Thermus thermophilus (Q9LCY2), Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q9LCY2)
brenda
Benitez-Paez, A.; Villarroya, M.; Armengod, M.E.
Regulation of expression and catalytic activity of Escherichia coli RsmG methyltransferase
RNA
18
795-806
2012
Escherichia coli (P0A6U5), Escherichia coli
brenda
Benitez-Paez, A.; Cardenas-Brito, S.; Corredor, M.; Villarroya, M.; Armengod, M.E.
Impairing methylations at ribosome RNA, a point mutation-dependent strategy for aminoglycoside resistance: The rsmG case
Biomedica
34
41-49
2014
Escherichia coli (P0A6U5)
brenda
Abedeera, S.M.; Hawkins, C.M.; Abeysirigunawardena, S.C.
RsmG forms stable complexes with premature small subunit rRNA during bacterial ribosome biogenesis
RSC Adv.
10
22361-22369
2020
Escherichia coli (P0A6U5), Escherichia coli K12 (P0A6U5)
brenda
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