XCtpB assembles a gated protease tunnel regulating cell-cell signaling during spore formation in bacillus subtilis

Mastny, M; Heuck, A; Kurzbauer, R; Heiduk, A; Boisguerin, P; Volkmer, R; Ehrmann, M; Rodrigues, CDA; Rudner, DZ; Clausen, T

XCtpB assembles a gated protease tunnel regulating cell-cell signaling during spore formation in bacillus subtilis

Mastny, M Heuck, A Kurzbauer, R Heiduk, A Boisguerin, P Volkmer, R Ehrmann, M Rodrigues, CDA

Rudner, DZ Clausen, T

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Publication Type:: Journal Article
Citation:: Cell, 2013, 155 (3), pp. 647 - ?
Issue Date:: 2013-10-24

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Field	Value	Language
dc.contributor.author	Mastny, M	en_US
dc.contributor.author	Heuck, A	en_US
dc.contributor.author	Kurzbauer, R	en_US
dc.contributor.author	Heiduk, A	en_US
dc.contributor.author	Boisguerin, P	en_US
dc.contributor.author	Volkmer, R	en_US
dc.contributor.author	Ehrmann, M	en_US
dc.contributor.author	Rodrigues, CDA https://orcid.org/0000-0003-4541-0145	en_US
dc.contributor.author	Rudner, DZ	en_US
dc.contributor.author	Clausen, T	en_US
dc.date.available	2013-09-18	en_US
dc.date.issued	2013-10-24	en_US
dc.identifier.citation	Cell, 2013, 155 (3), pp. 647 - ?	en_US
dc.identifier.issn	0092-8674	en_US
dc.identifier.uri	http://hdl.handle.net/10453/116943
dc.description.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. © 2013 Elsevier Inc.	en_US
dc.relation.ispartof	Cell	en_US
dc.relation.isbasedon	10.1016/j.cell.2013.09.050	en_US
dc.subject.classification	Developmental Biology	en_US
dc.subject.mesh	Bacillus subtilis	en_US
dc.subject.mesh	Spores, Bacterial	en_US
dc.subject.mesh	Bacterial Proteins	en_US
dc.subject.mesh	Sequence Alignment	en_US
dc.subject.mesh	Signal Transduction	en_US
dc.subject.mesh	Allosteric Site	en_US
dc.subject.mesh	Amino Acid Sequence	en_US
dc.subject.mesh	Models, Molecular	en_US
dc.subject.mesh	Molecular Sequence Data	en_US
dc.subject.mesh	PDZ Domains	en_US
dc.title	XCtpB assembles a gated protease tunnel regulating cell-cell signaling during spore formation in bacillus subtilis	en_US
dc.type	Journal Article
utslib.citation.volume	3	en_US
utslib.citation.volume	155	en_US
utslib.for	0605 Microbiology	en_US
utslib.for	0601 Biochemistry and Cell Biology	en_US
utslib.for	06 Biological Sciences	en_US
utslib.for	11 Medical and Health Sciences	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Strength - ithree - Institute of Infection, Immunity and Innovation
utslib.copyright.status	closed_access
pubs.issue	3	en_US
pubs.publication-status	Published	en_US
pubs.volume	155	en_US

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. © 2013 Elsevier Inc.

Please use this identifier to cite or link to this item:

http://hdl.handle.net/10453/116943