ArticleMolecular & cellular proteomics : MCP2011
A proteomic and transcriptomic approach reveals new insight into beta-methylthiolation of Escherichia coli ribosomal protein S12.
Article in Molecular & cellular proteomics : MCP, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 30 citations in OpenAlex.
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- Cell-selective multiplexed bioorthogonal noncanonical amino acid tagging for nascent proteomics.Nature chemical biology · 2026Article
- Essentiality of theInternational journal of molecular sciences · 2023Article
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- Global and gene-specific translational regulation in Escherichia coli across different conditions.PLoS computational biology · 2022Article
- Global analysis of biosynthetic gene clusters reveals conserved and unique natural products in entomopathogenic nematode-symbiotic bacteria.Nature chemistry · 2022Article
- Discovery and characterisation of an amidine-containing ribosomally-synthesised peptide that is widely distributed in nature.Chemical science · 2021Article
- Article
- YcaO-Dependent Posttranslational Amide Activation: Biosynthesis, Structure, and Function.Chemical reviews · 2017Review
- Cyclisation mechanisms in the biosynthesis of ribosomally synthesised and post-translationally modified peptides.Beilstein journal of organic chemistry · 2016Review
- 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
- High-resolution structure of the Escherichia coli ribosome.Nature structural & molecular biology · 2015Article
- Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis.Nature chemical biology · 2014Article
- Recent advances in radical SAM enzymology: new structures and mechanisms.ACS chemical biology · 2014Review
- Diverse and divergent protein post-translational modifications in two growth stages of a natural microbial community.Nature communications · 2014Article
- A predictor for predicting Escherichia coli transcriptome and the effects of gene perturbations.BMC bioinformatics · 2014Article
- Predicting the minimal translation apparatus: lessons from the reductive evolution of mollicutes.PLoS genetics · 2014Article
- Functional role of methylation of G518 of the 16S rRNA 530 loop by GidB in Mycobacterium tuberculosis.Antimicrobial agents and chemotherapy · 2013Article
- A coordinated proteomic approach for identifying proteins that interact with the E. coli ribosomal protein S12.Journal of proteome research · 2013Article
- Dynamics of ribosomal protein S1 on a bacterial ribosome with cross-linking and mass spectrometry.Molecular & cellular proteomics : MCP · 2012Article
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
Abstract
β-methylthiolation is a novel post-translational modification mapping to a universally conserved Asp 88 of the bacterial ribosomal protein S12. This S12 specific modification has been identified on orthologs from multiple bacterial species. The origin and functional significance was investigated with both a proteomic strategy to identify candidate S12 interactors and expression microarrays to search for phenotypes that result from targeted gene knockouts of select candidates. Utilizing an endogenous recombinant E. coli S12 protein with an affinity tag as bait, mass spectrometric analysis identified candidate S12 binding partners including RimO (previously shown to be required for this post-translational modification) and YcaO, a conserved protein of unknown function. Transcriptomic analysis of bacterial strains with deleted genes for RimO and YcaO identified an overlapping transcriptional phenotype suggesting that YcaO and RimO likely share a common function. As a follow up, quantitative mass spectrometry additionally indicated that both proteins dramatically impacted the modification status of S12. Collectively, these results indicate that the YcaO protein is involved in β-methylthiolation of S12 and its absence impairs the ability of RimO to modify S12. Additionally, the proteomic data from this study provides direct evidence that the E. coli specific β-methylthiolation likely occurs when S12 is assembled as part of a ribosomal subunit.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.