ArticleJournal of the American Chemical Society2014
Characterization of a cross-linked protein-nucleic acid substrate radical in the reaction catalyzed by RlmN.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 45 citations in OpenAlex.
- Structural and Spectroscopic Basis for Catalysis by a Class C RadicalJournal of the American Chemical Society · 2026Article
- Structural Basis for CbioRxiv : the preprint server for biology · 2026Article
- Structural and Spectroscopic Basis for Catalysis by a Class C RadicalbioRxiv : the preprint server for biology · 2026Article
- CNature communications · 2024Article
- Structure and Catalytic Mechanism of Radical SAM Methylases.Life (Basel, Switzerland) · 2022Review
- Structural Insight into the Substrate Scope of Viperin and Viperin-like Enzymes from Three Domains of Life.Biochemistry · 2021Article
- miCLIP-MaPseq Identifies Substrates of Radical SAM RNA-Methylating Enzyme Using Mechanistic Cross-Linking and Mismatch Profiling.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Viperin Reveals Its True Function.Annual review of virology · 2020Review
- Mechanism of Rate Acceleration of Radical C-C Bond Formation Reaction by a Radical SAM GTP 3',8-Cyclase.Journal of the American Chemical Society · 2020Article
- Analysis of RNA Methylation by Phylogenetically Diverse Cfr RadicalBiochemistry · 2019Article
- Analysis of Electrochemical Properties ofJournal of the American Chemical Society · 2019Article
- Capturing Intermediates in the Reaction Catalyzed by NosN, a Class C Radical S-Adenosylmethionine Methylase Involved in the Biosynthesis of the Nosiheptide Side-Ring System.Journal of the American Chemical Society · 2019Article
- Investigation of Solvent Hydron Exchange in the Reaction Catalyzed by the Antibiotic Resistance Protein Cfr.Biochemistry · 2018Article
- Article
- miCLIP-MaPseq, a Substrate Identification Approach for Radical SAM RNA Methylating Enzymes.Journal of the American Chemical Society · 2018Article
- Organometallic and radical intermediates reveal mechanism of diphthamide biosynthesis.Science (New York, N.Y.) · 2018Article
- Enhanced Solubilization of Class B Radical S-Adenosylmethionine Methylases by Improved Cobalamin Uptake in Escherichia coli.Biochemistry · 2018Article
- Substrate-Dependent Cleavage Site Selection by Unconventional Radical S-Adenosylmethionine Enzymes in Diphthamide Biosynthesis.Journal of the American Chemical Society · 2017Article
- Antibiotic resistance evolved via inactivation of a ribosomal RNA methylating enzyme.Nucleic acids research · 2016Article
- Structural basis for tRNA modification by Elp3 from Dehalococcoides mccartyi.Nature structural & molecular biology · 2016Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
RlmN and Cfr are methyltransferases/methylsynthases that belong to the radical S-adenosylmethionine superfamily of enzymes. RlmN catalyzes C2 methylation of adenosine 2503 (A2503) of 23S rRNA, while Cfr catalyzes C8 methylation of the exact same nucleotide, and will subsequently catalyze C2 methylation if the site is unmethylated. A key feature of the unusual mechanisms of catalysis proposed for these enzymes is the attack of a methylene radical, derived from a methylcysteine residue, onto the carbon center undergoing methylation to generate a paramagnetic protein-nucleic acid cross-linked species. This species has been thoroughly characterized during Cfr-dependent C8 methylation, but does not accumulate to detectible levels in RlmN-dependent C2 methylation. Herein, we show that inactive C118S/A variants of RlmN accumulate a substrate-derived paramagnetic species. Characterization of this species by electron paramagnetic resonance spectroscopy in concert with strategic isotopic labeling shows that the radical is delocalized throughout the adenine ring of A2503, although predominant spin density is on N1 and N3. Moreover, (13)C hyperfine interactions between the radical and the methylene carbon of the formerly [methyl-(13)C]Cys355 residue show that the radical species exists in a covalent cross-link between the protein and the nucleic acid substrate. X-ray structures of RlmN C118A show that, in the presence of SAM, the substitution does not alter the active site structure compared to that of the wild-type enzyme. Together, these findings have new mechanistic implications for the role(s) of C118 and its counterpart in Cfr (C105) in catalysis, and suggest involvement of the residue in resolution of the cross-linked species via a radical mediated process.
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