A flagellum-specific chaperone facilitates assembly of the core type III export apparatus of the bacterial flagellum.
Many 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 cytoplasm...
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doaj-971ccf46c2bb48bc9748a5e4db21f9422021-07-02T16:28:50ZengPublic Library of Science (PLoS)PLoS Biology1544-91731545-78852017-08-01158e200226710.1371/journal.pbio.2002267A flagellum-specific chaperone facilitates assembly of the core type III export apparatus of the bacterial flagellum.Florian D FabianiThibaud T RenaultBritta PetersTobias DietscheEric J C GálvezAlina GuseKaren FreierEmmanuelle CharpentierTill StrowigMirita Franz-WachtelBoris MacekSamuel WagnerMichael HenselMarc ErhardtMany 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.https://doi.org/10.1371/journal.pbio.2002267 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Florian D Fabiani Thibaud T Renault Britta Peters Tobias Dietsche Eric J C Gálvez Alina Guse Karen Freier Emmanuelle Charpentier Till Strowig Mirita Franz-Wachtel Boris Macek Samuel Wagner Michael Hensel Marc Erhardt |
spellingShingle |
Florian D Fabiani Thibaud T Renault Britta Peters Tobias Dietsche Eric J C Gálvez Alina Guse Karen Freier Emmanuelle Charpentier Till Strowig Mirita Franz-Wachtel Boris Macek Samuel Wagner Michael Hensel Marc Erhardt A flagellum-specific chaperone facilitates assembly of the core type III export apparatus of the bacterial flagellum. PLoS Biology |
author_facet |
Florian D Fabiani Thibaud T Renault Britta Peters Tobias Dietsche Eric J C Gálvez Alina Guse Karen Freier Emmanuelle Charpentier Till Strowig Mirita Franz-Wachtel Boris Macek Samuel Wagner Michael Hensel Marc Erhardt |
author_sort |
Florian D Fabiani |
title |
A flagellum-specific chaperone facilitates assembly of the core type III export apparatus of the bacterial flagellum. |
title_short |
A flagellum-specific chaperone facilitates assembly of the core type III export apparatus of the bacterial flagellum. |
title_full |
A flagellum-specific chaperone facilitates assembly of the core type III export apparatus of the bacterial flagellum. |
title_fullStr |
A flagellum-specific chaperone facilitates assembly of the core type III export apparatus of the bacterial flagellum. |
title_full_unstemmed |
A flagellum-specific chaperone facilitates assembly of the core type III export apparatus of the bacterial flagellum. |
title_sort |
flagellum-specific chaperone facilitates assembly of the core type iii export apparatus of the bacterial flagellum. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS Biology |
issn |
1544-9173 1545-7885 |
publishDate |
2017-08-01 |
description |
Many 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. |
url |
https://doi.org/10.1371/journal.pbio.2002267 |
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