Peptidoglycan hydrolysis is required for assembly and activity of the transenvelope secretion complex during sporulation in Bacillus subtilis

Rodrigues, CDA; Marquis, KA; Meisner, J; Rudner, DZ

Peptidoglycan hydrolysis is required for assembly and activity of the transenvelope secretion complex during sporulation in Bacillus subtilis

Rodrigues, CDA

Marquis, KA Meisner, J Rudner, DZ

Permalink

Publication Type:: Journal Article
Citation:: Molecular Microbiology, 2013, 89 (6), pp. 1039 - 1052
Issue Date:: 2013-09-01

Closed Access

	Filename	Description	Size
	Rodrigues_et_al-2013-Molecular_Microbiology.pdf	Published Version	1.14 MB	Adobe PDF	View/Open

Copyright Clearance Process

Recently Added
In Progress
Closed Access

This item is closed access and not available.

Full metadata record

Field	Value	Language
dc.contributor.author	Rodrigues, CDA https://orcid.org/0000-0003-4541-0145	en_US
dc.contributor.author	Marquis, KA	en_US
dc.contributor.author	Meisner, J	en_US
dc.contributor.author	Rudner, DZ	en_US
dc.date.available	2013-07-05	en_US
dc.date.issued	2013-09-01	en_US
dc.identifier.citation	Molecular Microbiology, 2013, 89 (6), pp. 1039 - 1052	en_US
dc.identifier.issn	0950-382X	en_US
dc.identifier.uri	http://hdl.handle.net/10453/116944
dc.description.abstract	Summary: Sporulating Bacillus subtilis cells assemble a transenvelope secretion complex that connects the mother cell and developing spore. The forespore protein SpoIIQ and the mother-cell protein SpoIIIAH interact across the double membrane septum and are thought to assemble into a channel that serves as the basement layer of this specialized secretion system. SpoIIQ is absolutely required to recruit SpoIIIAH to the sporulation septum on the mother-cell side, however the mechanism by which SpoIIQ is localized has been unclear. Here, we show that SpoIIQ localization requires its partner protein SpoIIIAH and degradation of the septal peptidoglycan (PG) by the two cell wall hydrolases SpoIID and SpoIIP. Our data suggest that PG degradation enables a second mother-cell-produced protein to interact with SpoIIQ. Cells in which both mother-cell anchoring mechanisms have been disabled have a synergistic sporulation defect suggesting that both localization factors function in the secretion complex. Finally, we show that septal PG degradation is critical for the assembly of an active complex. Altogether, these results suggest that the specialized secretion system that links the mother cell and forespore has a complexity approaching those found in Gram-negative bacteria and reveal that the sporulating cell must overcome similar challenges in assembling a transenvelope complex. © 2013 John Wiley & Sons Ltd.	en_US
dc.relation.ispartof	Molecular Microbiology	en_US
dc.relation.isbasedon	10.1111/mmi.12322	en_US
dc.subject.classification	Microbiology	en_US
dc.subject.mesh	Bacillus subtilis	en_US
dc.subject.mesh	Spores, Bacterial	en_US
dc.subject.mesh	Peptidoglycan	en_US
dc.subject.mesh	Bacterial Proteins	en_US
dc.subject.mesh	Hydrolysis	en_US
dc.subject.mesh	Bacterial Secretion Systems	en_US
dc.title	Peptidoglycan hydrolysis is required for assembly and activity of the transenvelope secretion complex during sporulation in Bacillus subtilis	en_US
dc.type	Journal Article
utslib.citation.volume	6	en_US
utslib.citation.volume	89	en_US
utslib.for	0605 Microbiology	en_US
utslib.for	06 Biological Sciences	en_US
utslib.for	07 Agricultural and Veterinary 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	6	en_US
pubs.publication-status	Published	en_US
pubs.volume	89	en_US

Abstract:

Summary: Sporulating Bacillus subtilis cells assemble a transenvelope secretion complex that connects the mother cell and developing spore. The forespore protein SpoIIQ and the mother-cell protein SpoIIIAH interact across the double membrane septum and are thought to assemble into a channel that serves as the basement layer of this specialized secretion system. SpoIIQ is absolutely required to recruit SpoIIIAH to the sporulation septum on the mother-cell side, however the mechanism by which SpoIIQ is localized has been unclear. Here, we show that SpoIIQ localization requires its partner protein SpoIIIAH and degradation of the septal peptidoglycan (PG) by the two cell wall hydrolases SpoIID and SpoIIP. Our data suggest that PG degradation enables a second mother-cell-produced protein to interact with SpoIIQ. Cells in which both mother-cell anchoring mechanisms have been disabled have a synergistic sporulation defect suggesting that both localization factors function in the secretion complex. Finally, we show that septal PG degradation is critical for the assembly of an active complex. Altogether, these results suggest that the specialized secretion system that links the mother cell and forespore has a complexity approaching those found in Gram-negative bacteria and reveal that the sporulating cell must overcome similar challenges in assembling a transenvelope complex. © 2013 John Wiley & Sons Ltd.

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

http://hdl.handle.net/10453/116944