ArticleProceedings of the National Academy of Sciences of the United States of America2004
BofA protein inhibits intramembrane proteolysis of pro-sigmaK in an intercompartmental signaling pathway during Bacillus subtilis sporulation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 52 citations in OpenAlex.
- Genetic Engineering of Escherichia coli W for Linalool Production Using Beet Juice as the Sole Carbon Source.Applied biochemistry and biotechnology · 2025Article
- Inhibitory proteins ofJournal of bacteriology · 2025Article
- Structural characterization and biophysical analysis of recombinant SpoIVB variants: insights into PDZ and serine protease domain interactions.Microbiology spectrum · 2025Article
- To Sporulate or Not to Sporulate: Developmental Checkpoints MonitoringAnnual review of microbiology · 2025Review
- Substrate engagement by the intramembrane metalloprotease SpoIVFB.Nature communications · 2024Article
- Article
- The role of site-2-proteases in bacteria: a review on physiology, virulence, and therapeutic potential.microLife · 2023Review
- Article
- Conserved Proline Residues of Bacillus subtilis Intramembrane Metalloprotease SpoIVFB Are Important for Substrate Interaction and Cleavage.Journal of bacteriology · 2022Article
- Channels modestly impact compartment-specific ATP levels during Bacillus subtilis sporulation and a rise in the mother cell ATP level is not necessary for Pro-σMolecular microbiology · 2020Article
- From Root to Tips: Sporulation Evolution and Specialization in Bacillus subtilis and the Intestinal Pathogen Clostridioides difficile.Molecular biology and evolution · 2019Article
- Diversity, versatility and complexity of bacterial gene regulation mechanisms: opportunities and drawbacks for applications in synthetic biology.FEMS microbiology reviews · 2019Review
- NagRFrontiers in microbiology · 2018Article
- Interaction of intramembrane metalloprotease SpoIVFB with substrate Pro-σProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Bacillus subtilis Intramembrane Protease RasP Activity in Escherichia coli andJournal of bacteriology · 2017Article
- AAA+ Machines of Protein Destruction in Mycobacteria.Frontiers in molecular biosciences · 2017Review
- Complex Formed between Intramembrane Metalloprotease SpoIVFB and Its Substrate, Pro-σK.The Journal of biological chemistry · 2016Article
- Regulated proteolysis in bacterial development.FEMS microbiology reviews · 2014Review
- Biochemical and structural insights into intramembrane metalloprotease mechanisms.Biochimica et biophysica acta · 2013Review
- Residues in conserved loops of intramembrane metalloprotease SpoIVFB interact with residues near the cleavage site in pro-σK.Journal of bacteriology · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Bacillus subtilis is a bacterium that undergoes a developmental program of sporulation in response to starvation. At the core of the program are sigma factors, whose regulated spatiotemporal activation controls much of the gene expression. Activation of pro-sigma(K) in the mother cell compartment involves regulated intramembrane proteolysis (RIP) in response to a signal from the forespore. RIP is a poorly understood process that is conserved in prokaryotes and eukaryotes. Here, we report a powerful system for studying RIP of pro-sigma(K). Escherichia coli was engineered to coexpress the putative membrane-embedded metalloprotease SpoIVFB with pro-sigma(K) and potential inhibitors of RIP. Overproduction of SpoIVFB and pro-sigma(K) in E. coli allowed accurate and abundant proteolytic processing of pro-sigma(K) with the characteristics expected for SpoIVFB acting as an intramembrane-cleaving protease (I-Clip). Coexpression of BofA in this system led to formation of a BofA-SpoIVFB complex and marked inhibition of pro-sigma(K) processing. Mutational analysis identified amino acids in BofA that are necessary for complex formation and inhibition of processing, leading us to propose that BofA inhibits SpoIVFB metalloprotease activity by providing a metal ligand, analogous to the cysteine switch mechanism of matrix metalloprotease regulation. The approach described herein should be applicable to studies of other RIP events and amenable to developing in vitro assays for I-Clips.
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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.