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 ORCID: https://orcid.org/0000-0002-1927-260X, 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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Abstract

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:	25 Oct 2022 08:14
URI:	https://orca.cardiff.ac.uk/id/eprint/51946

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