ArticleNucleic acids research2024
The previously uncharacterized RnpM (YlxR) protein modulates the activity of ribonuclease P in Bacillus subtilis in vitro.
Article in Nucleic acids research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 8 citations in OpenAlex.
- Identification of a putative RocS homolog through phenotypic profiling of uncharacterized essential genes inbioRxiv : the preprint server for biology · 2026Article
- In Situ Bacterioplankton Growth Partitioning by High-Resolution Metatranscriptomics.Environmental microbiology reports · 2026Article
- Pleiotropic roles of elongation factor P inMicrobiology spectrum · 2026Article
- FrlP, an ABC type I importer component ofJournal of bacteriology · 2025Article
- Chemical crosslinking extends and complements UV crosslinking in analysis of RNA/DNA nucleic acid-protein interaction sites by mass spectrometry.Nucleic acids research · 2025Article
- The DnaJK chaperone ofmBio · 2025Article
- Interactors and effects of overexpressing YlxR/RnpM, a conserved RNA binding protein in cyanobacteria.RNA biology · 2024Article
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
Abstract
Even though Bacillus subtilis is one of the most studied organisms, no function has been identified for about 20% of its proteins. Among these unknown proteins are several RNA- and ribosome-binding proteins suggesting that they exert functions in cellular information processing. In this work, we have investigated the RNA-binding protein YlxR. This protein is widely conserved in bacteria and strongly constitutively expressed in B. subtilis suggesting an important function. We have identified the RNA subunit of the essential RNase P as the binding partner of YlxR. The main activity of RNase P is the processing of 5' ends of pre-tRNAs. In vitro processing assays demonstrated that the presence of YlxR results in reduced RNase P activity. Chemical cross-linking studies followed by in silico docking analysis and experiments with site-directed mutant proteins suggest that YlxR binds to the region of the RNase P RNA that is important for binding and cleavage of the pre-tRNA substrate. We conclude that the YlxR protein is a novel interaction partner of the RNA subunit of RNase P that serves to finetune RNase P activity to ensure appropriate amounts of mature tRNAs for translation. We rename the YlxR protein RnpM for RNase P modulator.
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