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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The enzyme appears in viruses and cellular organisms
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.
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
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
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
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
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
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
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
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
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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
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2.1.1.174 23S rRNA (guanine1835-N2)-methyltransferase
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