Home > Publications database > CtpB Assembles a Gated Protease Tunnel Regulating Cell-Cell Signaling during Spore Formation in Bacillus subtilis > print

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024 7 _ |a 10.1016/j.cell.2013.09.050
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100 1 _ |a Mastny, Markus
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245 _ _ |a CtpB Assembles a Gated Protease Tunnel Regulating Cell-Cell Signaling during Spore Formation in Bacillus subtilis
260 _ _ |a [Cambridge, Mass.]
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520 _ _ |a 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.
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700 1 _ |a Heuck, Alexander
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700 1 _ |a Kurzbauer, Robert
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700 1 _ |a Heiduk, Anja
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700 1 _ |a Boisguerin, Prisca
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700 1 _ |a Volkmer, Rudolf
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700 1 _ |a Ehrmann, Michael
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700 1 _ |a Rodrigues, Christopher D. A.
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700 1 _ |a Rudner, David Z.
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700 1 _ |a Clausen, Tim
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773 _ _ |a 10.1016/j.cell.2013.09.050
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