ArticleThe Journal of biological chemistry2010
Post-translational modification of ribosomal proteins: structural and functional characterization of RimO from Thermotoga maritima, a radical S-adenosylmethionine methylthiotransferase.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 62 citations in OpenAlex.
- Assessing Metal Ion Assignment Accuracy in Protein Data Bank Models via Elemental Spectroscopy.Journal of chemical information and modeling · 2026Article
- RiboScreenBiomedicines · 2026Review
- Novel chemistry and structural perspectives in vitamin BChemical science · 2026Review
- Discovery of a Biotin Synthase That Utilizes an Auxiliary 4Fe-5S Cluster for Sulfur Insertion.Journal of the American Chemical Society · 2024Article
- Text-Mining to Identify Gene Sets Involved in Biocorrosion by Sulfate-Reducing Bacteria: A Semi-Automated Workflow.Microorganisms · 2023Article
- Characterization of LipS1 and LipS2 fromACS bio & med chem Au · 2022Article
- Biochemical Approaches to Probe the Role of the Auxiliary Iron-Sulfur Cluster of Lipoyl Synthase from Mycobacterium Tuberculosis.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Radical SAM Enzymes and Ribosomally-Synthesized and Post-translationally Modified Peptides: A Growing Importance in the Microbiomes.Frontiers in chemistry · 2021Review
- Functional characterization of asnC family transcriptional regulator in Pseudomonas aeruginosa PGPR2 during root colonization.Molecular biology reports · 2020Article
- Genome-Wide Identification, Evolution and Expression of the Complete Set of Cytoplasmic Ribosomal Protein Genes in Nile Tilapia.International journal of molecular sciences · 2020Article
- New contribution to the morphology and molecular mechanism of Euplotes encysticus encystment.Scientific reports · 2018Article
- Cluster-Dependent Charge-Transfer Dynamics in Iron-Sulfur Proteins.Biochemistry · 2018Article
- Post-translational modification of ribosomally synthesized peptides by a radical SAM epimerase in Bacillus subtilis.Nature chemistry · 2017Article
- Genome-Wide Identification and Comprehensive Expression Profiling of Ribosomal Protein Small Subunit (RPS) Genes and their Comparative Analysis with the Large Subunit (RPL) Genes in Rice.Frontiers in plant science · 2017Article
- On the Role of Additional [4Fe-4S] Clusters with a Free Coordination Site in Radical-SAM Enzymes.Frontiers in chemistry · 2017Review
- Transformations of the FeS Clusters of the Methylthiotransferases MiaB and RimO, Detected by Direct Electrochemistry.Biochemistry · 2016Article
- Unanticipated coordination of tris buffer to the Radical SAM cluster of the RimO methylthiotransferase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Article
- Single-residue posttranslational modification sites at the N-terminus, C-terminus or in-between: To be or not to be exposed for enzyme access.Proteomics · 2015Article
- Recent advances in radical SAM enzymology: new structures and mechanisms.ACS chemical biology · 2014Review
- Evidence for a catalytically and kinetically competent enzyme-substrate cross-linked intermediate in catalysis by lipoyl synthase.Biochemistry · 2014Article
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Authors and funding
13 authors at 6 institutions in 2 countries.
Funding
Abstract
Post-translational modifications of ribosomal proteins are important for the accuracy of the decoding machinery. A recent in vivo study has shown that the rimO gene is involved in generation of the 3-methylthio derivative of residue Asp-89 in ribosomal protein S12 (Anton, B. P., Saleh, L., Benner, J. S., Raleigh, E. A., Kasif, S., and Roberts, R. J. (2008) Proc. Natl. Acad. Sci. U. S. A. 105, 1826-1831). This reaction is formally identical to that catalyzed by MiaB on the C2 of adenosine 37 near the anticodon of several tRNAs. We present spectroscopic evidence that Thermotoga maritima RimO, like MiaB, contains two [4Fe-4S] centers, one presumably bound to three invariant cysteines in the central radical S-adenosylmethionine (AdoMet) domain and the other to three invariant cysteines in the N-terminal UPF0004 domain. We demonstrate that holo-RimO can specifically methylthiolate the aspartate residue of a 20-mer peptide derived from S12, yielding a mixture of mono- and bismethylthio derivatives. Finally, we present the 2.0 A crystal structure of the central radical AdoMet and the C-terminal TRAM (tRNA methyltransferase 2 and MiaB) domains in apo-RimO. Although the core of the open triose-phosphate isomerase (TIM) barrel of the radical AdoMet domain was conserved, RimO showed differences in domain organization compared with other radical AdoMet enzymes. The unusually acidic TRAM domain, likely to bind the basic S12 protein, is located at the distal edge of the radical AdoMet domain. The basic S12 protein substrate is likely to bind RimO through interactions with both the TRAM domain and the concave surface of the incomplete TIM barrel. These biophysical results provide a foundation for understanding the mechanism of methylthioation by radical AdoMet enzymes in the MiaB/RimO family.
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