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Information on EC 2.1.1.170 - 16S rRNA (guanine527-N7)-methyltransferase and Organism(s) Escherichia coli and UniProt Accession P0A6U5

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IUBMB Comments
The enzyme specifically methylates guanine527 at N7 in 16S rRNA.
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This record set is specific for:
Escherichia coli
UNIPROT: P0A6U5
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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S-adenosyl-L-methionine
+
guanine527 in 16S rRNA
=
S-adenosyl-L-homocysteine
+
N7-methylguanine527 in 16S rRNA
+
guanine527 in 16S rRNA
=
+
N7-methylguanine527 in 16S rRNA
Synonyms
16s rrna methyltransferase, rsmg methyltransferase, ribosomal rna small subunit methyltransferase g, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glucose-inhibited division protein B
-
RsmG methyltransferase
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:16S rRNA (guanine527-N7)-methyltransferase
The enzyme specifically methylates guanine527 at N7 in 16S rRNA.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
show the reaction diagram
-
GidB is a m7G methyltransferase specific for 16S rRNA, identification of methylated nucleotide
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + guanine527 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine527 in 16S rRNA
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
activity of rsmGp slightly increases by fourfold when cells are grown in minimal media supplemented with glycerol instead of glucose
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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
malfunction
-
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
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23840
MALDI-MS
23842
1 * 23842, MALDI-MS
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 23842, MALDI-MS
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant FLAG-tagged RsmG from Escherichia coli TOP10 cells by affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli BL21
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
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team