ArticleNucleic acids research2021
A new role for SR1 from Bacillus subtilis: regulation of sporulation by inhibition of kinA translation.
Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 19 citations in OpenAlex.
- Bacterial small regulatory RNAs.Nature reviews. Microbiology · 2026Review
- Small regulatory RNAs modulate lactococcal susceptibility to cell wall-targeting antimicrobials.Nucleic acids research · 2026Article
- Design of orthogonal and portable RNA devices for post-transcriptional regulation by reverse engineering type I toxin-antitoxin systems.Nucleic acids research · 2025Article
- Remodeling of RNA-binding proteome and RNA-mediated regulation as a new layer of control of sporulation.mSystems · 2025Article
- Review
- Autoinducer-2 relieves soil stress-induced dormancy of Bacillus velezensis by modulating sporulation signaling.NPJ biofilms and microbiomes · 2024Article
- Regulatory RNAs inSynthetic and systems biotechnology · 2024Review
- RNA Double-Helix Hybridization Measured by Fluorescence Correlation Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2024Article
- In Vitro Methods for the Investigation of sRNA-mRNA Interactions in Bacillus subtilis.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Small proteins in Gram-positive bacteria.FEMS microbiology reviews · 2023Article
- A network of small RNAs regulates sporulation initiation in Clostridioides difficile.The EMBO journal · 2023Article
- A Sporulation-Specific sRNA Bvs196 Contributing to the Developing Spore inMicroorganisms · 2022Article
- Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SR1 is a dual-function sRNA from Bacillus subtilis. It inhibits translation initiation of ahrC mRNA encoding the transcription activator of the arginine catabolic operons. Base-pairing is promoted by the RNA chaperone CsrA, which induces a slight structural change in the ahrC mRNA to facilitate SR1 binding. Additionally, SR1 encodes the small protein SR1P that interacts with glyceraldehyde-3P dehydrogenase A to promote binding to RNase J1 and enhancing J1 activity. Here, we describe a new target of SR1, kinA mRNA encoding the major histidine kinase of the sporulation phosphorelay. SR1 and kinA mRNA share 7 complementary regions. Base-pairing between SR1 and kinA mRNA decreases kinA translation without affecting kinA mRNA stability and represses transcription of the KinA/Spo0A downstream targets spoIIE, spoIIGA and cotA. The initial interaction between SR1 and kinA mRNA occurs 10 nt downstream of the kinA start codon and is decisive for inhibition. The sr1 encoded peptide SR1P is dispensable for kinA regulation. Deletion of sr1 accelerates sporulation resulting in low quality spores with reduced stress resistance and altered coat protein composition which can be compensated by sr1 overexpression. Neither CsrA nor Hfq influence sporulation or spore properties.
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