ArticleEMBO reports2025
RagB stimulates the activity of the peptidoglycan polymerase RodA in Bacillus subtilis.
Article in EMBO reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed.
- The phenotypic landscape of the model firmicuteProceedings of the National Academy of Sciences of the United States of America · 2026Article
- A broadly conserved gram-positive lipoprotein regulates cell elongation.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Multilevel Regulation of Peptidoglycan Dynamics in Bacteria: From Molecular Mechanisms to Applied Perspectives.Biomolecules · 2026Review
- ThebioRxiv : the preprint server for biology · 2025Article
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Authors and funding
9 authors.
Funding
Abstract
The bacterial cell wall is primarily composed of peptidoglycan (PG), a polymer essential for its protective envelope function, and any defect in its synthesis or repair can potentially result in bacterial lysis. Class A Penicillin-Binding Proteins (aPBPs) and Shape, Elongation, Division, and Sporulation (SEDS) proteins are PG polymerases acting in concert to ensure bacterial cell wall growth. Here, we identify the first regulator of the SEDS protein RodA in the Gram-positive model bacterium Bacillus subtilis. In the presence of the antibiotic moenomycin, which specifically inhibits glycosyltransferase activity of aPBPs, or in a strain deleted for all four aPBPs, bacterial survival depends on the presence of the YrrS protein (renamed RagB) and can be rescued by overexpression of RodA. No effect of RagB is observed on the rodA gene expression level or on the speed of circumferentially moving RodA associated with PG elongation by the Rod complex. However, we demonstrate that RagB interacts with RodA. We propose that RagB stimulates RodA activity and becomes essential in the absence of aPBPs and in particular of the major aPBP, PBP1.
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Registered trials
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 Socratic graph.