ArticleNucleic acids research2013
Structural and functional insights into the molecular mechanism of rRNA m6A methyltransferase RlmJ.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 29 citations in OpenAlex.
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- Plasticity and conditional essentiality of modification enzymes for domain V ofRNA (New York, N.Y.) · 2022Article
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- Role of the Demethylase AlkB Homolog H5 in the Promotion of Dentinogenesis.Frontiers in physiology · 2022Article
- A comprehensive review of m6A/m6Am RNA methyltransferase structures.Nucleic acids research · 2021Review
- Single-nucleotide resolution ofChemical science · 2020Article
- Crystal structure of ErmE - 23S rRNA methyltransferase in macrolide resistance.Scientific reports · 2019Article
- Bisubstrate analogues as structural tools to investigate mRNA biology · 2019Article
- Programming Structured DNA Assemblies to Probe Biophysical Processes.Annual review of biophysics · 2019Review
- Mettl3 Regulates Osteogenic Differentiation and Alternative Splicing of Vegfa in Bone Marrow Mesenchymal Stem Cells.International journal of molecular sciences · 2019Article
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5 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
RlmJ catalyzes the m(6)A2030 methylation of 23S rRNA during ribosome biogenesis in Escherichia coli. Here, we present crystal structures of RlmJ in apo form, in complex with the cofactor S-adenosyl-methionine and in complex with S-adenosyl-homocysteine plus the substrate analogue adenosine monophosphate (AMP). RlmJ displays a variant of the Rossmann-like methyltransferase (MTase) 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. Adenosine monophosphate binds in a partly accommodated state with the target N6 atom 7 Å away from the sulphur of AdoHcy. The active site of RlmJ with motif IV sequence 164DPPY167 is more similar to DNA m(6)A MTases than to RNA m(6)2A MTases, and structural comparison suggests that RlmJ binds its substrate base similarly to DNA MTases T4Dam and M.TaqI. RlmJ methylates in vitro transcribed 23S rRNA, as well as a minimal substrate corresponding to helix 72, demonstrating independence of previous modifications and tertiary interactions in the RNA substrate. RlmJ displays specificity for adenosine, and mutagenesis experiments demonstrate the critical roles of residues Y4, H6, K18 and D164 in methyl transfer.
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