ArticleProceedings of the National Academy of Sciences of the United States of America2009
Intramembrane proteolytic cleavage of a membrane-tethered transcription factor by a metalloprotease depends on ATP.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 35 citations in OpenAlex.
- Inhibitory proteins ofJournal of bacteriology · 2025Article
- Substrate engagement by the intramembrane metalloprotease SpoIVFB.Nature communications · 2024Article
- 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
- Identification of L-Valine-initiated-germination-active genes in Bacillus subtilis using Tn-seq.PloS one · 2019Article
- Evidence that regulation of intramembrane proteolysis is mediated by substrate gating during sporulation in Bacillus subtilis.PLoS genetics · 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
- Role of CBS and Bateman Domains in Phosphorylation-Dependent Regulation of a CLC Anion Channel.Biophysical journal · 2016Article
- Complex Formed between Intramembrane Metalloprotease SpoIVFB and Its Substrate, Pro-σK.The Journal of biological chemistry · 2016Article
- High-Throughput Genetic Screens Identify a Large and Diverse Collection of New Sporulation Genes in Bacillus subtilis.PLoS biology · 2016Article
- Regulated proteolysis in bacterial development.FEMS microbiology reviews · 2014Review
- Biochemical and structural insights into intramembrane metalloprotease mechanisms.Biochimica et biophysica acta · 2013Review
- Function of site-2 proteases in bacteria and bacterial pathogens.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
- Features of Pro-σK important for cleavage by SpoIVFB, an intramembrane metalloprotease.Journal of bacteriology · 2013Article
- Identification and characterization of five intramembrane metalloproteases in Anabaena variabilis.Journal of bacteriology · 2012Article
- Recent progress in Bacillus subtilis sporulation.FEMS microbiology reviews · 2012Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Regulated intramembrane proteolysis (RIP) involves cleavage of a transmembrane segment of a protein. RIP governs diverse processes in a wide variety of organisms and is carried out by different types of intramembrane proteases (IPs), including a large family of metalloproteases. The Bacillus subtilis SpoIVFB protein is a putative metalloprotease that cleaves membrane-tethered Pro-sigma(K), releasing sigma(K) to direct transcription of genes necessary for spore formation. By attaching an extra transmembrane segment to the N terminus of SpoIVFB, expression in E. coli was improved more than 100-fold, facilitating purification and demonstration of metalloprotease activity, which accurately cleaved purified Pro-sigma(K). Uniquely for IPs examined so far, SpoIVFB activity requires ATP, which binds to the C-terminal cystathionine-beta-synthase (CBS) domain of SpoIVFB. Deleting just 10 residues from the C-terminal end of SpoIVFB nearly eliminated cleavage of coexpressed Pro-sigma(K) in E. coli. The CBS domain of SpoIVFB was shown to interact with Pro-sigma(K) and ATP changed the interaction, suggesting that ATP regulates substrate access to the active site and renders cleavage sensitive to the cellular energy level, which may be a general feature of CBS-domain-containing IPs. Incorporation of SpoIVFB into preformed liposomes stimulated its ability to cleave Pro-sigma(K). Cleavage depended on ATP and the correct peptide bond was shown to be cleaved using a rapid and sensitive mass spectrometry assay. A system for biochemical studies of RIP by a metalloprotease in a membrane environment has been established using methods that might be applicable to other IPs.
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