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
|
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: | 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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