Abstract
The developmental transcription factor ςK is derived from the inactive precursor protein pro-ςK by regulated proteolysis during the process of sporulation in the bacteriumBacillus subtilis. The putative pro-ςK 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-ςK processing until a signal has been received from the forespore.
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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 26, 2002, 8 p.m.) |
Deposited | 3 years, 9 months ago (Nov. 15, 2021, 11:06 a.m.) |
Indexed | 2 months, 4 weeks ago (June 4, 2025, 6:29 a.m.) |
Issued | 23 years, 4 months ago (April 15, 2002) |
Published | 23 years, 4 months ago (April 15, 2002) |
Published Online | 23 years, 4 months ago (April 15, 2002) |
Published Print | 23 years, 4 months ago (April 15, 2002) |
@article{Rudner_2002, title={A sporulation membrane protein tethers the pro-ςK processing enzyme to its inhibitor and dictates its subcellular localization}, volume={16}, ISSN={1549-5477}, url={http://dx.doi.org/10.1101/gad.977702}, DOI={10.1101/gad.977702}, number={8}, journal={Genes & Development}, publisher={Cold Spring Harbor Laboratory}, author={Rudner, David Z. and Losick, Richard}, year={2002}, month=apr, pages={1007–1018} }