%0 Journal Article
%A Mastny, Markus
%A Heuck, Alexander
%A Kurzbauer, Robert
%A Heiduk, Anja
%A Boisguerin, Prisca
%A Volkmer, Rudolf
%A Ehrmann, Michael
%A Rodrigues, Christopher D. A.
%A Rudner, David Z.
%A Clausen, Tim
%T CtpB Assembles a Gated Protease Tunnel Regulating Cell-Cell Signaling during Spore Formation in Bacillus subtilis
%J Cell
%V 155
%N 3
%@ 0092-8674
%C [Cambridge, Mass.]
%I Cell Press
%M DESY-2014-02420
%P 647 - 658
%D 2013
%Z (c) Elsevier Inc.
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000326571800018
%$ pmid:24243021
%R 10.1016/j.cell.2013.09.050
%U https://bib-pubdb1.desy.de/record/168215