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• W2108294778 abstract "The developmental transcription factor sigmaK is derived from the inactive precursor protein pro-sigmaK by regulated proteolysis during the process of sporulation in the bacterium Bacillus subtilis. The putative pro-sigmaK processing enzyme SpoIVFB is a member of a family of membrane-embedded metalloproteases and is held inactive by two other integral membrane proteins, SpoIVFA and BofA. Herein we show that the processing enzyme and its two regulators exist in a multimeric complex that localizes to the membrane surrounding the developing spore (the forespore). We further show that one of the regulators, SpoIVFA, plays a central role in both the formation of this complex and its subcellular localization. Evidence is presented in support of a model in which SpoIVFA acts as a platform for bringing BofA and SpoIVFB together, whereby BofA inhibits pro-sigmaK processing until a signal has been received from the forespore." @default.
• W2108294778 created "2016-06-24" @default.
• W2108294778 creator A5017903771 @default.
• W2108294778 creator A5065212721 @default.
• W2108294778 date "2002-04-15" @default.
• W2108294778 modified "2023-10-04" @default.
• W2108294778 title "A sporulation membrane protein tethers the pro-ς^K processing enzyme to its inhibitor and dictates its subcellular localization" @default.
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• W2108294778 doi "https://doi.org/10.1101/gad.977702" @default.
• W2108294778 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/152351" @default.
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• W2108294778 hasPublicationYear "2002" @default.
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