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Information on EC 2.1.1.174 - 23S rRNA (guanine1835-N2)-methyltransferase and Organism(s) Escherichia coli and UniProt Accession P42596

for references in articles please use BRENDA:EC2.1.1.174
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IUBMB Comments
The enzyme methylates 23S rRNA in vitro, assembled 50S subunits are not a substrate . The enzyme specifically methylates guanine1835 at N2 in 23S rRNA.
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This record set is specific for:
Escherichia coli
UNIPROT: P42596
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide
S-adenosyl-L-methionine
+
guanine1835 in 23S rRNA
=
S-adenosyl-L-homocysteine
+
N2-methylguanine1835 in 23S rRNA
+
guanine1835 in 23S rRNA
=
+
N2-methylguanine1835 in 23S rRNA
Synonyms
m2g1835, n2-methyltransferase rlmg, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23S rRNA methyltransferase
-
N2-methyltransferase RlmG
-
-
ribosomal RNA large subunit methyltransferase G
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + guanine1835 in 23S rRNA = S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA
show the reaction diagram
catalytic mechanism, overview
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:23S rRNA (guanine1835-N2)-methyltransferase
The enzyme methylates 23S rRNA in vitro, assembled 50S subunits are not a substrate [1]. The enzyme specifically methylates guanine1835 at N2 in 23S rRNA.
CAS REGISTRY NUMBER
COMMENTARY hide
50812-26-5
-
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 + guanine1835 in 23S rRNA
S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + guanine1835 in 23S rRNA
S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA
show the reaction diagram
additional information
?
-
molecular modeling of RlmG-AdoMet-rRNA complex
-
-
?
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 + guanine1835 in 23S rRNA
S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + guanine1835 in 23S rRNA
S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA
show the reaction diagram
additional information
?
-
molecular modeling of RlmG-AdoMet-rRNA complex
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
binds in the active site of the C-terminal domain, structure, overview
S-adenosyl-L-methionine
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene rlmG
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
RlmG is a specific S-adenosyl-L-methionine-dependent methyltransferase responsible for N2-methylation of G1835 in 23S rRNA of Escherichia coli. Methylation of m2G1835 specifically enhances association of ribosomal subunits and provides a significant advantage for bacteria in osmotic and oxidative stress
malfunction
physiological function
-
methylation of 23S rRNA nucleotide m2G1835 is important for association of ribosomal subunits. Methylation of G1835 provides a significant advantage for bacteria at osmotic and oxidative stress
additional information
RlmG possesses two homologous domains: the N-terminal domain in the recognition and binding of the substrate, and the C-terminal domain in S-adenosyl-L-methionine-binding and the catalytic process. The N-terminal domain can bind RNA independently and RNA binding is achieved by the N-terminal domain, accomplished by a coordinating role of the C-terminal domain, modeling of the RlmG-AdoMet-RNA complex, overview. RlmG may unfold its substrate RNA in the positively charged cleft between the NTD and CTD, and then G1835 disengages from its Watson-Crick pairing with C1905 and flips out to insert into the active site
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
71000
x * 71000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
monomer status of RlmG in solution
?
x * 71000, SDS-PAGE
additional information
RlmG possesses two homologous domains: the N-terminal domain in the recognition and binding of the substrate, and the C-terminal domain in S-adenosyl-L-methionine-binding and the catalytic process. The N-terminal domain can bind RNA independently and RNA binding is achieved by the N-terminal domain, accomplished by a coordinating role of the C-terminal domain
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
RlmG in complex with S-adenosyl-L-methionine, sitting drop vapor diffusion method, room temperature, mixture of RlmG with S-adenosyl-L-methionine in solution 0.2 M Tris, pH 7.5, and 5% w/v PEG 8000 with the addition of 1% w/v protamine sulfate, and 0.02 M HEPES sodium, pH 6.8, 3-4 days, X-ray diffraction structure determination and analysis at 2.3 A resolution, single-wavelength anomalous dispersion
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of C-terminally His6-tagged full-length enzyme, expression of the C-terminal domain and the N-terminal domain as SUMO fusion proteins, the C-terminal domain is unstable after detagging through ubiquitin-like-specific protease 1 cleavage, while the N-terminal domain is stable
recombinant YgjO protein carrying a C-terminal GFP-His6-tag is expressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sergiev, P.V.; Lesnyak, D.V.; Bogdanov, A.A.; Dontsova, O.A.
Identification of Escherichia coli m2G methyltransferases: II. The ygjO gene encodes a methyltransferase specific for G1835 of the 23 S rRNA
J. Mol. Biol.
364
26-31
2006
Escherichia coli (Q0T0I4), Escherichia coli
Manually annotated by BRENDA team
Sergiev, P.V.; Bogdanov, A.A.; Dontsova, O.A.
Ribosomal RNA guanine-(N2)-methyltransferases and their targets
Nucleic Acids Res.
35
2295-2301
2007
Escherichia coli (Q0T0I4)
Manually annotated by BRENDA team
Osterman, I.A.; Sergiev, P.V.; Tsvetkov, P.O.; Makarov, A.A.; Bogdanov, A.A.; Dontsova, O.A.
Methylated 23S rRNA nucleotide m2G1835 of Escherichia coli ribosome facilitates subunit association
Biochimie
93
725-729
2011
Escherichia coli
Manually annotated by BRENDA team
Zhang, H.; Gao, Z.Q.; Wei, Y.; Wang, W.J.; Liu, G.F.; Shtykova, E.V.; Xu, J.H.; Dong, Y.H.
Structural insights into the function of 23S rRNA methyltransferase RlmG (m2G1835) from Escherichia coli
RNA
18
1500-1509
2012
Escherichia coli (P42596)
Manually annotated by BRENDA team