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Enzyme Nomenclature
Information on EC 2.1.1.174 - 23S rRNA (guanine1835-N2)-methyltransferase
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The expected taxonomic range for this enzyme is: Escherichia coli
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EC NUMBER 
COMMENTARY 
2.1.1.174
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RECOMMENDED NAME
GeneOntology No.
23S rRNA (guanine1835-N2)-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + guanine1835 in 23S rRNA = S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA
S-adenosyl-L-methionine + guanine1835 in 23S rRNA = S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA
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S-adenosyl-L-methionine + guanine1835 in 23S rRNA = S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA
catalytic mechanism, overview
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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.
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CAS REGISTRY NUMBER
COMMENTARY
50812-26-5
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
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
malfunction
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knock-out of the ygjO gene leads to loss of modification at G1835. Lack of the G1835 methylation causes growth retardation, especially at temperatures higher than optimal and in poor media
malfunction
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lack of G1835 methylation in rlmG(ygjO) knockout strain does not lead to significant growth retardation at the optimal growth conditions. However, in the poor medium and at elevated temperature, the rlmG(ygjO) knockout strain has significantly decreased fitness
malfunction
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absence of 23S rRNA nucleotide G1835 methylation does not influence the fidelity of translation or ribosome interaction with translation GTPases and decreases bacterial cell survival at osmotic and oxidative stress. Cells devoid of the rlmG gene are hypersensitive to osmotic and oxidative stress
physiological function
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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
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
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + guanine1835 in 23S rRNA
S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA
additional information
?
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molecular modeling of RlmG-AdoMet-rRNA complex
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S-adenosyl-L-methionine + guanine1835 in 23S rRNA
S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA
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-
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?
S-adenosyl-L-methionine + guanine1835 in 23S rRNA
S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA
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?
S-adenosyl-L-methionine + guanine1835 in 23S rRNA
S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA
the nucleotide m2G1835 is located in a functionally extremely important region of the ribosome, being located within intersubunit bridges of group B2
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?
S-adenosyl-L-methionine + guanine1835 in 23S rRNA
S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA
recombinant YgjO protein is able to methylate in vitro protein-free 23S rRNA, but not assembled 50S subunits purified from the ygjO knock-out strain
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S-adenosyl-L-methionine + guanine1835 in 23S rRNA
S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA
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RlmG possessing an additional RNA-binding domain act on naked ribosomal RNA or early assembly intermediates in the cell
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S-adenosyl-L-methionine + guanine1835 in 23S rRNA
S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA
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m2G1835 is located at ribosomal subunits 50S and 30S interface
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?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + guanine1835 in 23S rRNA
S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA
additional information
?
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P42596
molecular modeling of RlmG-AdoMet-rRNA complex
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S-adenosyl-L-methionine + guanine1835 in 23S rRNA
S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA
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?
S-adenosyl-L-methionine + guanine1835 in 23S rRNA
S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA
P42596
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?
S-adenosyl-L-methionine + guanine1835 in 23S rRNA
S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA
Q0T0I4
the nucleotide m2G1835 is located in a functionally extremely important region of the ribosome, being located within intersubunit bridges of group B2
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?
S-adenosyl-L-methionine + guanine1835 in 23S rRNA
S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA
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m2G1835 is located at ribosomal subunits 50S and 30S interface
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-adenosyl-L-methionine
binds in the active site of the C-terminal domain, structure, overview
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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generation of rlmG knock-out cells, ribosomes purified from the rlmG knockout strain do not have methyl group attached to nucleotide G1835 of the 23S rRNA
additional information
construction of two deletion mutants corresponding to the isolated N-terminal domain and C-terminal domain
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LINKS TO OTHER DATABASES (specific for EC-Number 2.1.1.174)
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