ArticleJournal of the American Chemical Society2011
Cfr and RlmN contain a single [4Fe-4S] cluster, which directs two distinct reactivities for S-adenosylmethionine: methyl transfer by SN2 displacement and radical generation.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 66 citations in OpenAlex.
- Beyond native reactivity: radical SAM enzymes as platforms for new-to-nature chemistry.RSC chemical biology · 2026Review
- Structural Basis for CbioRxiv : the preprint server for biology · 2026Article
- tRNA modification profiling reveals epitranscriptome regulatory networks in Pseudomonas aeruginosa.Nucleic acids research · 2025Article
- Facile and dynamic cleavage of every iron-sulfide bond in cuboidal iron-sulfur clusters.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structure and Catalytic Mechanism of Radical SAM Methylases.Life (Basel, Switzerland) · 2022Review
- Methyltransferases: Functions and Applications.Chembiochem : a European journal of chemical biology · 2022Review
- Flagellin lysine methyltransferase FliB catalyzes a [4Fe-4S] mediated methyl transfer reaction.PLoS pathogens · 2021Article
- Structural Insight into the Substrate Scope of Viperin and Viperin-like Enzymes from Three Domains of Life.Biochemistry · 2021Article
- Overall Retention of Methyl Stereochemistry during BBiochemistry · 2021Article
- Metal utilization in genome-reduced bacteria: Do human mycoplasmas rely on iron?Computational and structural biotechnology journal · 2021Review
- Viperin Reveals Its True Function.Annual review of virology · 2020Review
- New Insight into the Mechanism of Anaerobic Heme Degradation.Biochemistry · 2019Article
- Analysis of RNA Methylation by Phylogenetically Diverse Cfr RadicalBiochemistry · 2019Article
- Investigation of Solvent Hydron Exchange in the Reaction Catalyzed by the Antibiotic Resistance Protein Cfr.Biochemistry · 2018Article
- Probing the coordination and function of FeNature communications · 2018Article
- X-ray and EPR Characterization of the Auxiliary Fe-S Clusters in the Radical SAM Enzyme PqqE.Biochemistry · 2018Article
- Substrate-Dependent Cleavage Site Selection by Unconventional Radical S-Adenosylmethionine Enzymes in Diphthamide Biosynthesis.Journal of the American Chemical Society · 2017Article
- 7-Carboxy-7-deazaguanine Synthase: A Radical S-Adenosyl-l-methionine Enzyme with Polar Tendencies.Journal of the American Chemical Society · 2017Article
- On the Role of Additional [4Fe-4S] Clusters with a Free Coordination Site in Radical-SAM Enzymes.Frontiers in chemistry · 2017Review
- Crystallographic capture of a radical S-adenosylmethionine enzyme in the act of modifying tRNA.Science (New York, N.Y.) · 2016Article
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4 authors at 1 institution in 1 country.
Funding
Abstract
The radical SAM (RS) proteins RlmN and Cfr catalyze methylation of carbons 2 and 8, respectively, of adenosine 2503 in 23S rRNA. Both reactions are similar in scope, entailing the synthesis of a methyl group partially derived from S-adenosylmethionine (SAM) onto electrophilic sp(2)-hybridized carbon atoms via the intermediacy of a protein S-methylcysteinyl (mCys) residue. Both proteins contain five conserved Cys residues, each required for turnover. Three cysteines lie in a canonical RS CxxxCxxC motif and coordinate a [4Fe-4S]-cluster cofactor; the remaining two are at opposite ends of the polypeptide. Here we show that each protein contains only the one "radical SAM" [4Fe-4S] cluster and the two remaining conserved cysteines do not coordinate additional iron-containing species. In addition, we show that, while wild-type RlmN bears the C355 mCys residue in its as-isolated state, RlmN that is either engineered to lack the [4Fe-4S] cluster by substitution of the coordinating cysteines or isolated from Escherichia coli cultured under iron-limiting conditions does not bear a C355 mCys residue. Reconstitution of the [4Fe-4S] cluster on wild-type apo RlmN followed by addition of SAM results in rapid production of S-adenosylhomocysteine (SAH) and the mCys residue, while treatment of apo RlmN with SAM affords no observable reaction. These results indicate that in Cfr and RlmN, SAM bound to the unique iron of the [4Fe-4S] cluster displays two reactivities. It serves to methylate C355 of RlmN (C338 of Cfr), or to generate the 5'-deoxyadenosyl 5'-radical, required for substrate-dependent methyl synthase activity.
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