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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| Format: | Article |
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Public Library of Science (PLoS)
2017-08-01
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| Series: | PLoS Biology |
| Online Access: | https://journals.plos.org/plosbiology/article/file?id=10.1371/journal.pbio.2002267&type=printable |
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| 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 |
| 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 |
| collection | DOAJ |
| 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. |
| format | Article |
| id | doaj-art-971ccf46c2bb48bc9748a5e4db21f942 |
| institution | DOAJ |
| issn | 1544-9173 1545-7885 |
| language | English |
| publishDate | 2017-08-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Biology |
| spelling | doaj-art-971ccf46c2bb48bc9748a5e4db21f9422025-08-20T03:11:25ZengPublic 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://journals.plos.org/plosbiology/article/file?id=10.1371/journal.pbio.2002267&type=printable |
| 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 |
| title | 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_short | 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 |
| url | https://journals.plos.org/plosbiology/article/file?id=10.1371/journal.pbio.2002267&type=printable |
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