The Library
Structural insights into ring-building motif domains involved in bacterial sporulation
Tools
Tools
Tools
Liu, Bowen, Chan, Helena, Bauda, Elda, Contreras-Martel, Carlos, Bellard, Laure, Villard, Anne-Marie, Mas, Caroline, Neumann, Emmanuelle, Fenel, Daphna, Favier, Adrien, Serrano, Monica, Henriques, Adriano O., Rodrigues, Christopher D.A. and Morlot, Cecile (2022) Structural insights into ring-building motif domains involved in bacterial sporulation. Journal of Structural Biology, 214 (1). 107813. doi:10.1016/j.jsb.2021.107813 ISSN 1047-8477.
|
PDF
1-s2.0-S1047847721001180-main.pdf - Published Version - Requires a PDF viewer. Available under License Creative Commons Attribution Non-commercial No Derivatives 4.0. Download (5Mb) | Preview |
Official URL: http://dx.doi.org/10.1016/j.jsb.2021.107813
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.
| Item Type: | Journal Article | |||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Subjects: | Q Science > QK Botany Q Science > QP Physiology Q Science > QR Microbiology |
|||||||||||||||||||||
| Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | |||||||||||||||||||||
| Library of Congress Subject Headings (LCSH): | Gram-negative bacteria, Bacterial spores, Germination , Bacillus subtilis , Membrane proteins | |||||||||||||||||||||
| Journal or Publication Title: | Journal of Structural Biology | |||||||||||||||||||||
| Publisher: | Elsevier | |||||||||||||||||||||
| ISSN: | 1047-8477 | |||||||||||||||||||||
| Official Date: | March 2022 | |||||||||||||||||||||
| Dates: |
|
|||||||||||||||||||||
| Volume: | 214 | |||||||||||||||||||||
| Number: | 1 | |||||||||||||||||||||
| Article Number: | 107813 | |||||||||||||||||||||
| DOI: | 10.1016/j.jsb.2021.107813 | |||||||||||||||||||||
| Status: | Peer Reviewed | |||||||||||||||||||||
| Publication Status: | Published | |||||||||||||||||||||
| Access rights to Published version: | Open Access (Creative Commons) | |||||||||||||||||||||
| Date of first compliant deposit: | 20 January 2022 | |||||||||||||||||||||
| Date of first compliant Open Access: | 21 January 2022 | |||||||||||||||||||||
| RIOXX Funder/Project Grant: |
|
Request changes or add full text files to a record
Repository staff actions (login required)
 |
View Item |
Downloads
Downloads per month over past year
