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dc.contributor.authorFabiani, Florian D
dc.contributor.authorRenault, Thibaud T
dc.contributor.authorPeters, Britta
dc.contributor.authorDietsche, Tobias
dc.contributor.authorGálvez, Eric J C
dc.contributor.authorGuse, Alina
dc.contributor.authorFreier, Karen
dc.contributor.authorCharpentier, Emmanuelle
dc.contributor.authorStrowig, Till
dc.contributor.authorFranz-Wachtel, Mirita
dc.contributor.authorMacek, Boris
dc.contributor.authorWagner, Samuel
dc.contributor.authorHensel, Michael
dc.contributor.authorErhardt, Marc
dc.date.accessioned2017-08-17T10:02:01Z
dc.date.available2017-08-17T10:02:01Z
dc.date.issued2017-08
dc.identifier.citationA flagellum-specific chaperone facilitates assembly of the core type III export apparatus of the bacterial flagellum. 2017, 15 (8):e2002267 PLoS Biol.en
dc.identifier.issn1545-7885
dc.identifier.pmid28771474
dc.identifier.doi10.1371/journal.pbio.2002267
dc.identifier.urihttp://hdl.handle.net/10033/621060
dc.description.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.
dc.language.isoenen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.titleA flagellum-specific chaperone facilitates assembly of the core type III export apparatus of the bacterial flagellum.en
dc.typeArticleen
dc.contributor.departmentHelmholtz Centre for infection research, Inhoffenstr. 7, 38124 Braunschweig, Germany.en
dc.identifier.journalPLoS biologyen
refterms.dateFOA2018-06-13T17:10:51Z
html.description.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.


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