2.1.1.266: 23S rRNA (adenine2030-N6)-methyltransferase
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For detailed information about 23S rRNA (adenine2030-N6)-methyltransferase, go to the full flat file.
Reaction
Synonyms
23S rRNA methyltransferase, adenine-N6 methyltransferase, m6A2030 methyltransferase, ribosomal RNA large subunit methyltransferase J, rlmJ, rRNA m6A methyltransferase, YhiR, YhiR protein
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General Information
General Information on EC 2.1.1.266 - 23S rRNA (adenine2030-N6)-methyltransferase
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evolution
the active site of RlmJ with motif IV sequence 164DPPY167 is more similar to DNA m6A MTases than to RNA m6 2A MTases, and structural comparison suggests that RlmJ binds its substrate base similarly to DNA MTases T4Dam and M.TaqI
malfunction
physiological function
additional information
the phenotype of yhiR knockout gene is very mild under various growth conditions and at the stationary phase, except for a small growth advantage at anaerobic conditions. A very small subset of genes is affected by yhiR inactivation, while the majority of the proteome remains independent of the A2030 modification. Lack of modification at the 23S rRNA nucleotide: A2030 does not cause the accumulation of assembly intermediates. Phenotype of the yhiR gene knockout, overview
malfunction
knockout of rlmJ does not affect the growth rate, but lowers the competitive fitness at long-term growth in stationary phase and provides a small growth advantage under anaerobic conditions
the yhiR gene of Escherichia coli is solely responsible for the N6-methylation of A2030 of the 23S rRNA. Nucleotide m6A2030, buried inside the large ribosomal subunit close to the peptidyltransferase center, forms a strong stacked contact with the U571 residue of the 23S rRNA, thus connecting structural elements of domains II and V located at half-23S rRNA length distance in the primary structure. Modification of the 23S rRNA nucleotide A2030 occurs early in the 50S subunit assembly
physiological function
RlmJ catalyzes the m6A2030 methylation of 23S rRNA during ribosome biogenesis in Escherichia coli
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the yhiR gene should be renamed to rlmJ according to the rRNA methyltransferase nomenclature
additional information
the yhiR gene should be renamed to rlmJ according to the rRNA methyltransferase nomenclature
additional information
enzyme RlmJ displays a variant of the Rossmann-like methyltransferase fold with an inserted helical subdomain. Binding of cofactor and substrate induces a large shift of the N-terminal motif X tail to make it cover the cofactor binding site and trigger active-site changes in motifs IV and VIII, substrate binding site structure, overview. Critical roles of enzyme residues Y4, H6, K18 and D164 in methyl transfer, the enzyme requires only H72 of the RNA substrate for activity, overview. Enzyme apostructure analysis using PDB ID 2OO3, rigid-body refinement of the RlmJAPO structure against the RlmJSAM data. Structural model of a catalytic complex, overview
additional information
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enzyme RlmJ displays a variant of the Rossmann-like methyltransferase fold with an inserted helical subdomain. Binding of cofactor and substrate induces a large shift of the N-terminal motif X tail to make it cover the cofactor binding site and trigger active-site changes in motifs IV and VIII, substrate binding site structure, overview. Critical roles of enzyme residues Y4, H6, K18 and D164 in methyl transfer, the enzyme requires only H72 of the RNA substrate for activity, overview. Enzyme apostructure analysis using PDB ID 2OO3, rigid-body refinement of the RlmJAPO structure against the RlmJSAM data. Structural model of a catalytic complex, overview