ArticleMolecular & cellular proteomics : MCP2014
Quantitative phosphoproteomics reveals the role of protein arginine phosphorylation in the bacterial stress response.
Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed.
- Pushing the limits of single-cell proteomics to investigate bacterial heterogeneity using bacSCP.Nature communications · 2026Article
- Phosphoarginine modulates oligomerization and repressor activity of mycobacterial ClpC2.bioRxiv : the preprint server for biology · 2026Article
- UniPTMs: a unified multi-type PTM site prediction model via master-slave architecture-based multi-stage fusion strategy and hierarchical contrastive loss.BMC bioinformatics · 2026Article
- UniGraphPTMs: a contrastive learning-enhanced universal framework for PTM site prediction via GNN and multimodal fusion.BMC genomics · 2026Article
- Decoding protein N-phosphorylation functionality and sequence patterns.Briefings in bioinformatics · 2025Article
- Long-read methylome analysis of Oleidesulfovibrio alaskensis G20 biofilm under copper stress.Scientific reports · 2025Article
- Are you having a LaPh? Diverse roles of Labile Phosphorylation in mammalian cells.Biochemical Society transactions · 2025Review
- The regulatory impact of serine/threonine-specific protein phosphorylation among cyanobacteria.Frontiers in plant science · 2025Review
- Inactivation of the conserved protease LonA increases production of xylanase and amylase in Bacillus subtilis.Microbial cell factories · 2024Article
- The Transcriptomic Response of Cells of the Thermophilic BacteriumInternational journal of molecular sciences · 2024Article
- Nphos: Database and Predictor of Protein N-phosphorylation.Genomics, proteomics & bioinformatics · 2024Article
- [Progress in enrichment methods for proteinSe pu = Chinese journal of chromatography · 2024Review
- Review
- Structural insights into the regulation of protein-arginine kinase McsB by McsA.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Toxin-based screening of C-terminal tags inbioRxiv : the preprint server for biology · 2024Article
- Processing of stalled replication forks in Bacillus subtilis.FEMS microbiology reviews · 2024Review
- BacPROTACs targeting Clp protease: a promising strategy for anti-mycobacterial drug discovery.Frontiers in chemistry · 2024Article
- Giving a signal: how protein phosphorylation helps Bacillus navigate through different life stages.FEMS microbiology reviews · 2023Review
- A Review of the Bacterial Phosphoproteomes of Beneficial Microbes.Microorganisms · 2023Review
- PROTAC antibiotics: the time is now.Expert opinion on drug discovery · 2023Article
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7 authors.
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Abstract
Arginine phosphorylation is an emerging protein modification implicated in the general stress response of Gram-positive bacteria. The modification is mediated by the arginine kinase McsB, which phosphorylates and inactivates the heat shock repressor CtsR. In this study, we developed a mass spectrometric approach accounting for the peculiar chemical properties of phosphoarginine. The improved methodology was used to analyze the dynamic changes in the Bacillus subtilis arginine phosphoproteome in response to different stress situations. Quantitative analysis showed that a B. subtilis mutant lacking the YwlE arginine phosphatase accumulated a strikingly large number of arginine phosphorylations (217 sites in 134 proteins), however only a minor fraction of these sites was increasingly modified during heat shock or oxidative stress. The main targets of McsB-mediated arginine phosphorylation comprise central factors of the stress response system including the CtsR and HrcA heat shock repressors, as well as major components of the protein quality control system such as the ClpCP protease and the GroEL chaperonine. These findings highlight the impact of arginine phosphorylation in orchestrating the bacterial stress response.
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