GerM is required to assemble the basal platform of the SpoIIIA-SpoIIQ transenvelope complex during sporulation in Bacillus subtilis.

Rodrigues, CD; Ramírez-Guadiana, FH; Meeske, AJ; Wang, X; Rudner, DZ

GerM is required to assemble the basal platform of the SpoIIIA-SpoIIQ transenvelope complex during sporulation in Bacillus subtilis.

Rodrigues, CD Ramírez-Guadiana, FH Meeske, AJ Wang, X Rudner, DZ

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Publisher:: Wiley
Publication Type:: Journal Article
Citation:: Molecular microbiology, 2016, 102, (2), pp. 260-273
Issue Date:: 2016-07-06

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Field	Value	Language
dc.contributor.author	Rodrigues, CD
dc.contributor.author	Ramírez-Guadiana, FH
dc.contributor.author	Meeske, AJ
dc.contributor.author	Wang, X
dc.contributor.author	Rudner, DZ
dc.date.accessioned	2022-03-31T23:17:14Z
dc.date.available	2016-07-02
dc.date.available	2022-03-31T23:17:14Z
dc.date.issued	2016-07-06
dc.identifier.citation	Molecular microbiology, 2016, 102, (2), pp. 260-273
dc.identifier.issn	0950-382X
dc.identifier.issn	1365-2958
dc.identifier.uri	http://hdl.handle.net/10453/155817
dc.description.abstract	Sporulating Bacillus subtilis cells assemble a multimeric membrane complex connecting the mother cell and developing spore that is required to maintain forespore differentiation. An early step in the assembly of this transenvelope complex (called the A-Q complex) is an interaction between the extracellular domains of the forespore membrane protein SpoIIQ and the mother cell membrane protein SpoIIIAH. This interaction provides a platform onto which the remaining components of the complex assemble and also functions as an anchor for cell-cell signaling and morphogenetic proteins involved in spore development. SpoIIQ is required to recruit SpoIIIAH to the sporulation septum on the mother-cell side, however the mechanism by which SpoIIQ specifically localizes to the septal membranes on the forespore side has remained enigmatic. Here, we identify GerM, a lipoprotein previously implicated in spore germination, as the missing factor required for SpoIIQ localization. Our data indicate that GerM and SpoIIIAH, derived from the mother cell, and SpoIIQ, from the forespore, have reciprocal localization dependencies suggesting they constitute a tripartite platform for the assembly of the A-Q complex and a hub for the localization of mother cell and forespore proteins. This article is protected by copyright. All rights reserved.
dc.format	Print-Electronic
dc.language	English
dc.publisher	Wiley
dc.relation.ispartof	Molecular microbiology
dc.relation.isbasedon	10.1111/mmi.13457
dc.rights	info:eu-repo/semantics/closedAccess
dc.subject	06 Biological Sciences, 07 Agricultural and Veterinary Sciences, 11 Medical and Health Sciences
dc.subject.classification	Microbiology
dc.subject.mesh	Bacillus subtilis
dc.subject.mesh	Bacterial Proteins
dc.subject.mesh	Lipoproteins
dc.subject.mesh	Membrane Proteins
dc.subject.mesh	Protein Binding
dc.subject.mesh	Spores, Bacterial
dc.subject.mesh	Bacillus subtilis
dc.subject.mesh	Spores, Bacterial
dc.subject.mesh	Lipoproteins
dc.subject.mesh	Bacterial Proteins
dc.subject.mesh	Membrane Proteins
dc.subject.mesh	Protein Binding
dc.title	GerM is required to assemble the basal platform of the SpoIIIA-SpoIIQ transenvelope complex during sporulation in Bacillus subtilis.
dc.type	Journal Article
utslib.citation.volume	102
utslib.location.activity	England
utslib.for	0605 Microbiology
utslib.for	06 Biological Sciences
utslib.for	07 Agricultural and Veterinary Sciences
utslib.for	11 Medical and Health Sciences
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.consider-herdc	true
dc.date.updated	2022-03-31T23:17:09Z
pubs.issue	2
pubs.publication-status	Published
pubs.volume	102
utslib.citation.issue	2

Abstract:

Sporulating Bacillus subtilis cells assemble a multimeric membrane complex connecting the mother cell and developing spore that is required to maintain forespore differentiation. An early step in the assembly of this transenvelope complex (called the A-Q complex) is an interaction between the extracellular domains of the forespore membrane protein SpoIIQ and the mother cell membrane protein SpoIIIAH. This interaction provides a platform onto which the remaining components of the complex assemble and also functions as an anchor for cell-cell signaling and morphogenetic proteins involved in spore development. SpoIIQ is required to recruit SpoIIIAH to the sporulation septum on the mother-cell side, however the mechanism by which SpoIIQ specifically localizes to the septal membranes on the forespore side has remained enigmatic. Here, we identify GerM, a lipoprotein previously implicated in spore germination, as the missing factor required for SpoIIQ localization. Our data indicate that GerM and SpoIIIAH, derived from the mother cell, and SpoIIQ, from the forespore, have reciprocal localization dependencies suggesting they constitute a tripartite platform for the assembly of the A-Q complex and a hub for the localization of mother cell and forespore proteins. This article is protected by copyright. All rights reserved.

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http://hdl.handle.net/10453/155817