Structural characterization of the sporulation protein GerM from Bacillus subtilis

Trouve, J; Mohamed, A; Leisico, F; Contreras-Martel, C; Liu, B; Mas, C; Rudner, DZ; Rodrigues, CDA; Morlot, C

Structural characterization of the sporulation protein GerM from Bacillus subtilis

Trouve, J Mohamed, A Leisico, F Contreras-Martel, C Liu, B Mas, C Rudner, DZ Rodrigues, CDA

Morlot, C

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Publication Type:: Journal Article
Citation:: Journal of Structural Biology, 2018, 204 (3), pp. 481 - 490
Issue Date:: 2018-12-01

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Field	Value	Language
dc.contributor.author	Trouve, J	en_US
dc.contributor.author	Mohamed, A	en_US
dc.contributor.author	Leisico, F	en_US
dc.contributor.author	Contreras-Martel, C	en_US
dc.contributor.author	Liu, B	en_US
dc.contributor.author	Mas, C	en_US
dc.contributor.author	Rudner, DZ	en_US
dc.contributor.author	Rodrigues, CDA https://orcid.org/0000-0003-4541-0145	en_US
dc.contributor.author	Morlot, C	en_US
dc.date.available	2018-09-24	en_US
dc.date.issued	2018-12-01	en_US
dc.identifier.citation	Journal of Structural Biology, 2018, 204 (3), pp. 481 - 490	en_US
dc.identifier.issn	1047-8477	en_US
dc.identifier.uri	http://hdl.handle.net/10453/129382
dc.description.abstract	© 2018 Elsevier Inc. The Gram-positive bacterium Bacillus subtilis responds to starvation by entering a morphological differentiation process leading to the formation of a highly resistant spore. Early in the sporulation process, the cell asymmetrically divides into a large compartment (the mother cell) and a smaller one (the forespore), which will maturate into a resistant spore. Proper development of the forespore requires the assembly of a multiprotein complex called the SpoIIIA-SpoIIQ complex or “A-Q complex”. This complex involves the forespore protein SpoIIQ and eight mother cell proteins (SpoIIIAA to SpoIIIAH), many of which share structural similarities with components of specialized secretion systems and flagella found in Gram-negative bacteria. The assembly of the A-Q complex across the two membranes that separate the mother cell and forespore was recently shown to require GerM. GerM is a lipoprotein composed of two GerMN domains, a family of domains with unknown function. Here, we report X-ray crystallographic structures of the first GerMN domain of GerM at 1.0 Å resolution, and of the soluble domain of GerM (the tandem of GerMN domains) at 2.1 Å resolution. These structures reveal that GerMN domains can adopt distinct conformations and that the core of these domains display structural similarities with ring-building motifs found in components of specialized secretion system and in SpoIIIA proteins. This work provides an additional piece towards the structural characterization of the A-Q complex.	en_US
dc.relation.ispartof	Journal of Structural Biology	en_US
dc.relation.isbasedon	10.1016/j.jsb.2018.09.010	en_US
dc.subject.classification	Biophysics	en_US
dc.subject.mesh	Flagella	en_US
dc.subject.mesh	Bacillus subtilis	en_US
dc.subject.mesh	Spores, Bacterial	en_US
dc.subject.mesh	Hydrolases	en_US
dc.subject.mesh	Lipoproteins	en_US
dc.subject.mesh	Bacterial Proteins	en_US
dc.subject.mesh	Crystallography, X-Ray	en_US
dc.subject.mesh	Amino Acid Sequence	en_US
dc.subject.mesh	Protein Conformation	en_US
dc.subject.mesh	Sequence Homology, Amino Acid	en_US
dc.subject.mesh	Models, Molecular	en_US
dc.subject.mesh	Protein Domains	en_US
dc.title	Structural characterization of the sporulation protein GerM from Bacillus subtilis	en_US
dc.type	Journal Article
utslib.citation.volume	3	en_US
utslib.citation.volume	204	en_US
utslib.for	0601 Biochemistry and Cell Biology	en_US
utslib.for	0608 Zoology	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	204	en_US

Abstract:

© 2018 Elsevier Inc. The Gram-positive bacterium Bacillus subtilis responds to starvation by entering a morphological differentiation process leading to the formation of a highly resistant spore. Early in the sporulation process, the cell asymmetrically divides into a large compartment (the mother cell) and a smaller one (the forespore), which will maturate into a resistant spore. Proper development of the forespore requires the assembly of a multiprotein complex called the SpoIIIA-SpoIIQ complex or “A-Q complex”. This complex involves the forespore protein SpoIIQ and eight mother cell proteins (SpoIIIAA to SpoIIIAH), many of which share structural similarities with components of specialized secretion systems and flagella found in Gram-negative bacteria. The assembly of the A-Q complex across the two membranes that separate the mother cell and forespore was recently shown to require GerM. GerM is a lipoprotein composed of two GerMN domains, a family of domains with unknown function. Here, we report X-ray crystallographic structures of the first GerMN domain of GerM at 1.0 Å resolution, and of the soluble domain of GerM (the tandem of GerMN domains) at 2.1 Å resolution. These structures reveal that GerMN domains can adopt distinct conformations and that the core of these domains display structural similarities with ring-building motifs found in components of specialized secretion system and in SpoIIIA proteins. This work provides an additional piece towards the structural characterization of the A-Q complex.

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http://hdl.handle.net/10453/129382