ArticleJournal of the American Chemical Society2013
Identification of an intermediate methyl carrier in the radical S-adenosylmethionine methylthiotransferases RimO and MiaB.
Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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35 citing papers in PubMed, 57 citations in OpenAlex.
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- Biochemical and genetic studies define the functions of methylthiotransferases in methanogenic and methanotrophic archaea.Frontiers in microbiology · 2023Article
- Characterization of LipS1 and LipS2 fromACS bio & med chem Au · 2022Article
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- Biosynthesis and Degradation of Sulfur Modifications in tRNAs.International journal of molecular sciences · 2021Review
- The Multifaceted Bacterial Cysteine Desulfurases: From Metabolism to Pathogenesis.Antioxidants (Basel, Switzerland) · 2021Review
- Overall Retention of Methyl Stereochemistry during BBiochemistry · 2021Article
- Implications for an imidazol-2-yl carbene intermediate in the rhodanase-catalyzed C-S bond formation reaction of anaerobic ergothioneine biosynthesis.ACS catalysis · 2021Article
- Single-step Replacement of an Unreactive C-H Bond by a C-S Bond Using Polysulfide as the Direct Sulfur Source in Anaerobic Ergothioneine Biosynthesis.ACS catalysis · 2020Article
- First Step in Catalysis of the RadicalJournal of the American Chemical Society · 2020Article
- Methanogenesis marker protein 10 (Mmp10) fromThe Journal of biological chemistry · 2019Article
- Parsing redox potentials of five ferredoxins found within Thermotoga maritima.Protein science : a publication of the Protein Society · 2019Article
- Ferredoxins as interchangeable redox components in support of MiaB, a radical S-adenosylmethionine methylthiotransferase.Protein science : a publication of the Protein Society · 2019Article
- Recent Advances in Our Understanding of the Biosynthesis of Sulfur Modifications in tRNAs.Frontiers in microbiology · 2018Article
- The RicAFT (YmcA-YlbF-YaaT) complex carries two [4Fe-4S]Molecular microbiology · 2017Article
- Substrate-Dependent Cleavage Site Selection by Unconventional Radical S-Adenosylmethionine Enzymes in Diphthamide Biosynthesis.Journal of the American Chemical Society · 2017Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
RimO and MiaB are radical S-adenosylmethionine (SAM) enzymes that catalyze the attachment of methylthio (-SCH3) groups to macromolecular substrates. RimO attaches a methylthio group at C3 of aspartate 89 of protein S12, a component of the 30S subunit of the bacterial ribosome. MiaB attaches a methylthio group at C2 of N(6)-(isopentenyl)adenosine, found at nucleotide 37 in several prokaryotic tRNAs. These two enzymes are prototypical members of a subclass of radical SAM enzymes called methylthiotransferases (MTTases). It had been assumed that the sequence of steps in MTTase reactions involves initial sulfur insertion into the organic substrate followed by capping of the inserted sulfur atom with a SAM-derived methyl group. In this work, however, we show that both RimO and MiaB from Thermotoga maritima catalyze methyl transfer from SAM to an acid/base labile acceptor on the protein in the absence of their respective macromolecular substrates. Consistent with the assignment of the acceptor as an iron-sulfur cluster, denaturation of the SAM-treated protein with acid results in production of methanethiol. When RimO or MiaB is first incubated with SAM in the absence of substrate and reductant and then incubated with excess S-adenosyl-l-[methyl-d3]methionine in the presence of substrate and reductant, production of the unlabeled product precedes production of the deuterated product, showing that the methylated species is chemically and kinetically competent to be an intermediate.
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