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CtpB assembles a gated protease tunnel regulating cell-cell signaling during spore formation in Bacillus subtilis

Mastny, Markus, Heuck, Alexander, Kurzbauer, Robert, Heiduk, Anja, Boisguerin, Prisca, Volkmer, Rudolf, Ehrmann, Michael, Rodrigues, Christopher D. A., Rudner, David Z. and Clausen, Tim 2013. CtpB assembles a gated protease tunnel regulating cell-cell signaling during spore formation in Bacillus subtilis. Cell 155 (3) , pp. 647-658. 10.1016/j.cell.2013.09.050

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Spore formation in Bacillus subtilis relies on a regulated intramembrane proteolysis (RIP) pathway that synchronizes mother-cell and forespore development. To address the molecular basis of this SpoIV transmembrane signaling, we carried out a structure-function analysis of the activating protease CtpB. Crystal structures reflecting distinct functional states show that CtpB constitutes a ring-like protein scaffold penetrated by two narrow tunnels. Access to the proteolytic sites sequestered within these tunnels is controlled by PDZ domains that rearrange upon substrate binding. Accordingly, CtpB resembles a minimal version of a self-compartmentalizing protease regulated by a unique allosteric mechanism. Moreover, biochemical analysis of the PDZ-gated channel combined with sporulation assays reveal that activation of the SpoIV RIP pathway is induced by the concerted activity of CtpB and a second signaling protease, SpoIVB. This proteolytic mechanism is of broad relevance for cell-cell communication, illustrating how distinct signaling pathways can be integrated into a single RIP module.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Subjects: Q Science > QR Microbiology
Publisher: Elsevier
ISSN: 0092-8674
Last Modified: 04 Jun 2017 05:33

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