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CtpB assembles a gated protease tunnel regulating cell-cell signaling during spore formation in Bacillus subtilis
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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. doi:10.1016/j.cell.2013.09.050 ISSN 0092-8674.
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Official URL: http://dx.doi.org/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: | Journal Article | ||||||
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||||
Journal or Publication Title: | Cell | ||||||
Publisher: | Elsevier | ||||||
ISSN: | 0092-8674 | ||||||
Official Date: | 24 October 2013 | ||||||
Dates: |
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Volume: | 155 | ||||||
Number: | 3 | ||||||
Page Range: | pp. 647-658 | ||||||
DOI: | 10.1016/j.cell.2013.09.050 | ||||||
Status: | Peer Reviewed | ||||||
Publication Status: | Published | ||||||
Access rights to Published version: | Restricted or Subscription Access |
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