A flagellum-specific chaperone facilitates assembly of the core type III export apparatus of the bacterial flagellum.
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
AuthorsFabiani, Florian D
Renault, Thibaud T
Gálvez, Eric J C
MetadataShow full item record
AbstractMany bacteria move using a complex, self-assembling nanomachine, the bacterial flagellum. Biosynthesis of the flagellum depends on a flagellar-specific type III secretion system (T3SS), a protein export machine homologous to the export machinery of the virulence-associated injectisome. Six cytoplasmic (FliH/I/J/G/M/N) and seven integral-membrane proteins (FlhA/B FliF/O/P/Q/R) form the flagellar basal body and are involved in the transport of flagellar building blocks across the inner membrane in a proton motive force-dependent manner. However, how the large, multi-component transmembrane export gate complex assembles in a coordinated manner remains enigmatic. Specific for most flagellar T3SSs is the presence of FliO, a small bitopic membrane protein with a large cytoplasmic domain. The function of FliO is unknown, but homologs of FliO are found in >80% of all flagellated bacteria. Here, we demonstrate that FliO protects FliP from proteolytic degradation and promotes the formation of a stable FliP-FliR complex required for the assembly of a functional core export apparatus. We further reveal the subcellular localization of FliO by super-resolution microscopy and show that FliO is not part of the assembled flagellar basal body. In summary, our results suggest that FliO functions as a novel, flagellar T3SS-specific chaperone, which facilitates quality control and productive assembly of the core T3SS export machinery.
CitationA flagellum-specific chaperone facilitates assembly of the core type III export apparatus of the bacterial flagellum. 2017, 15 (8):e2002267 PLoS Biol.
AffiliationHelmholtz Centre for infection research, Inhoffenstr. 7, 38124 Braunschweig, Germany.
The following license files are associated with this item:
- Creative Commons
Except where otherwise noted, this item's license is described as http://creativecommons.org/licenses/by-nc-sa/4.0/
- Assembly and stoichiometry of the core structure of the bacterial flagellar type III export gate complex.
- Authors: Fukumura T, Makino F, Dietsche T, Kinoshita M, Kato T, Wagner S, Namba K, Imada K, Minamino T
- Issue date: 2017 Aug
- Assembly and stoichiometry of FliF and FlhA in Salmonella flagellar basal body.
- Authors: Morimoto YV, Ito M, Hiraoka KD, Che YS, Bai F, Kami-Ike N, Namba K, Minamino T
- Issue date: 2014 Mar
- Protein export through the bacterial flagellar type III export pathway.
- Authors: Minamino T
- Issue date: 2014 Aug
- <i>In Vitro</i> Reconstitution of Functional Type III Protein Export and Insights into Flagellar Assembly.
- Authors: Terashima H, Kawamoto A, Tatsumi C, Namba K, Minamino T, Imada K
- Issue date: 2018 Jun 26
- Assembling flagella in Salmonella mutant strains producing a type III export apparatus without FliO.
- Authors: Barker CS, Meshcheryakova IV, Inoue T, Samatey FA
- Issue date: 2014 Dec