2.1.1.174: 23S rRNA (guanine1835-N2)-methyltransferase
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For detailed information about 23S rRNA (guanine1835-N2)-methyltransferase, go to the full flat file.
Reaction
Synonyms
23S rRNA methyltransferase, EC 2.1.1.51, EC 2.1.1.52, m2G1835, N2-methyltransferase RlmG, ribosomal RNA large subunit methyltransferase G, RlmG, ygjO
ECTree
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General Information on EC 2.1.1.174 - 23S rRNA (guanine1835-N2)-methyltransferase
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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
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
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
