Evidence that SpoIVFB Is a Novel Type of Membrane Metalloprotease Governing Intercompartmental Communication during Bacillus subtilis Sporulation
Open Access
- 1 June 2000
- journal article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 182 (11) , 3305-3309
- https://doi.org/10.1128/jb.182.11.3305-3309.2000
Abstract
Processing of pro-ς K in the mother cell compartment of sporulating Bacillus subtilis involves SpoIVFB and is governed by a signal from the forespore. SpoIVFB has an HEXXH motif characteristic of metalloproteases embedded in one of its transmembrane segments. Several conservative single amino acid changes in the HEXXH motif abolished function. However, changing the glutamic acid residue to aspartic acid, or changing the isoleucine residue that precedes the motif to proline, permitted SpoIVFB function. Only one other putative metalloprotease, site 2 protease has been shown to tolerate aspartic acid rather than glutamic acid in its HEXXH sequence. Site 2 protease and SpoIVFB share a second region of similarity with a family of putative membrane metalloproteases. A conservative change in this region of SpoIVFB abolished function. Interestingly, SpoIVFA increased the accumulation of certain mutant SpoIVFB proteins but was unnecessary for accumulation of wild-type SpoIVFB.Keywords
This publication has 44 references indexed in Scilit:
- Control of σ factor activity during Bacillus subtilis sporulationMolecular Microbiology, 1999
- A novel clan of zinc metallopeptidases with possible intramembrane cleavage propertiesProtein Science, 1999
- Membrane topology analysis of the Bacillus subtilis BofA protein involved in pro-σ K processingMicrobiology, 1997
- Compartmentalized distribution of the proteins controlling the prespore‐specific transcription factor σF of Bacillus subtilisGenes to Cells, 1996
- Subcellular localization of proteins governing the proteolytic activation of a developmental transcription factor in Bacillus subtilisGenes to Cells, 1996
- Sporulation Regulatory Protein SpoIIID from Bacillus subtilis Activates and Represses Transcription by Both Mother-cell-specific Forms of RNA PolymeraseJournal of Molecular Biology, 1994
- Regulation of the Transcription of a Cluster of Bacillus subtilis Spore Coat GenesJournal of Molecular Biology, 1994
- Sporulation regulatory protein gerE from Bacillus subtilis binds to and can activate or repress transcription from promoters for mother-cell-specific genesJournal of Molecular Biology, 1992
- Sporulation operon spoIVF and the characterization of mutations that uncouple mother-cell from forespore gene expression in Bacillus subtilisJournal of Molecular Biology, 1991
- Post‐transcriptional control of a sporulation regulatory gene encoding transcription factor σH in Bacillus subtilisMolecular Microbiology, 1991