Structural insights into ring-building motif domains involved in bacterial sporulation.

Liu, B; Chan, H; Bauda, E; Contreras-Martel, C; Bellard, L; Villard, A-M; Mas, C; Neumann, E; Fenel, D; Favier, A; Serrano, M; Henriques, AO; Rodrigues, CDA; Morlot, C

Structural insights into ring-building motif domains involved in bacterial sporulation.

Liu, B Chan, H

Bauda, E Contreras-Martel, C Bellard, L Villard, A-M Mas, C Neumann, E Fenel, D Favier, A Serrano, M Henriques, AO Rodrigues, CDA Morlot, C

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Publisher:: Elsevier BV
Publication Type:: Journal Article
Citation:: Journal of structural biology, 2021, 214, (1), pp. 107813
Issue Date:: 2021-11-19

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Field	Value	Language
dc.contributor.author	Liu, B
dc.contributor.author	Chan, H https://orcid.org/0000-0002-5194-0006
dc.contributor.author	Bauda, E
dc.contributor.author	Contreras-Martel, C
dc.contributor.author	Bellard, L
dc.contributor.author	Villard, A-M
dc.contributor.author	Mas, C
dc.contributor.author	Neumann, E
dc.contributor.author	Fenel, D
dc.contributor.author	Favier, A
dc.contributor.author	Serrano, M
dc.contributor.author	Henriques, AO
dc.contributor.author	Rodrigues, CDA
dc.contributor.author	Morlot, C
dc.date.accessioned	2022-01-05T05:17:39Z
dc.date.available	2021-11-15
dc.date.available	2022-01-05T05:17:39Z
dc.date.issued	2021-11-19
dc.identifier.citation	Journal of structural biology, 2021, 214, (1), pp. 107813
dc.identifier.issn	1047-8477
dc.identifier.issn	1095-8657
dc.identifier.uri	http://hdl.handle.net/10453/152705
dc.description.abstract	Components of specialized secretion systems, which span the inner and outer membranes in Gram-negative bacteria, include ring-forming proteins whose oligomerization was proposed to be promoted by domains called RBM for "Ring-Building Motifs". During spore formation in Gram-positive bacteria, a transport system called the SpoIIIA-SpoIIQ complex also assembles in the double membrane that surrounds the forespore following its endocytosis by the mother cell. The presence of RBM domains in some of the SpoIIIA proteins led to the hypothesis that they would assemble into rings connecting the two membranes and form a conduit between the mother cell and forespore. Among them, SpoIIIAG forms homo-oligomeric rings in vitro but the oligomerization of other RBM-containing SpoIIIA proteins, including SpoIIIAH, remains to be demonstrated. In this work, we identified RBM domains in the YhcN/YlaJ family of proteins that are not related to the SpoIIIA-SpoIIQ complex. We solved the crystal structure of YhcN from Bacillus subtilis, which confirmed the presence of a RBM fold, flanked by additional secondary structures. As the protein did not show any oligomerization ability in vitro, we investigated the structural determinants of ring formation in SpoIIIAG, SpoIIIAH and YhcN. We showed that in vitro, the conserved core of RBM domains alone is not sufficient for oligomerization while the β-barrel forming region in SpoIIIAG forms rings on its own. This work suggests that some RBMs might indeed participate in the assembly of homomeric rings but others might have evolved toward other functions.
dc.format	Print-Electronic
dc.language	eng
dc.publisher	Elsevier BV
dc.relation	http://purl.org/au-research/grants/arc/DP190100793
dc.relation.ispartof	Journal of structural biology
dc.relation.isbasedon	10.1016/j.jsb.2021.107813
dc.rights	info:eu-repo/semantics/restrictedAccess
dc.rights	This is an open access article under the CC BY-NC-ND license.
dc.subject	0601 Biochemistry and Cell Biology, 0608 Zoology
dc.subject.classification	Biophysics
dc.title	Structural insights into ring-building motif domains involved in bacterial sporulation.
dc.type	Journal Article
utslib.citation.volume	214
utslib.location.activity	United States
utslib.for	0601 Biochemistry and Cell Biology
utslib.for	0608 Zoology
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	recently_added	*
dc.date.updated	2022-01-05T05:16:54Z
pubs.issue	1
pubs.publication-status	Published
pubs.volume	214
utslib.citation.issue	1

Abstract:

Components of specialized secretion systems, which span the inner and outer membranes in Gram-negative bacteria, include ring-forming proteins whose oligomerization was proposed to be promoted by domains called RBM for "Ring-Building Motifs". During spore formation in Gram-positive bacteria, a transport system called the SpoIIIA-SpoIIQ complex also assembles in the double membrane that surrounds the forespore following its endocytosis by the mother cell. The presence of RBM domains in some of the SpoIIIA proteins led to the hypothesis that they would assemble into rings connecting the two membranes and form a conduit between the mother cell and forespore. Among them, SpoIIIAG forms homo-oligomeric rings in vitro but the oligomerization of other RBM-containing SpoIIIA proteins, including SpoIIIAH, remains to be demonstrated. In this work, we identified RBM domains in the YhcN/YlaJ family of proteins that are not related to the SpoIIIA-SpoIIQ complex. We solved the crystal structure of YhcN from Bacillus subtilis, which confirmed the presence of a RBM fold, flanked by additional secondary structures. As the protein did not show any oligomerization ability in vitro, we investigated the structural determinants of ring formation in SpoIIIAG, SpoIIIAH and YhcN. We showed that in vitro, the conserved core of RBM domains alone is not sufficient for oligomerization while the β-barrel forming region in SpoIIIAG forms rings on its own. This work suggests that some RBMs might indeed participate in the assembly of homomeric rings but others might have evolved toward other functions.

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http://hdl.handle.net/10453/152705