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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...
Autores principales: | , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5542435/ https://www.ncbi.nlm.nih.gov/pubmed/28771474 http://dx.doi.org/10.1371/journal.pbio.2002267 |
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author | Fabiani, Florian D. Renault, Thibaud T. Peters, Britta Dietsche, Tobias Gálvez, Eric J. C. Guse, Alina Freier, Karen Charpentier, Emmanuelle Strowig, Till Franz-Wachtel, Mirita Macek, Boris Wagner, Samuel Hensel, Michael Erhardt, Marc |
author_facet | Fabiani, Florian D. Renault, Thibaud T. Peters, Britta Dietsche, Tobias Gálvez, Eric J. C. Guse, Alina Freier, Karen Charpentier, Emmanuelle Strowig, Till Franz-Wachtel, Mirita Macek, Boris Wagner, Samuel Hensel, Michael Erhardt, Marc |
author_sort | Fabiani, Florian D. |
collection | PubMed |
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 | Online Article Text |
id | pubmed-5542435 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-55424352017-08-12 A flagellum-specific chaperone facilitates assembly of the core type III export apparatus of the bacterial flagellum Fabiani, Florian D. Renault, Thibaud T. Peters, Britta Dietsche, Tobias Gálvez, Eric J. C. Guse, Alina Freier, Karen Charpentier, Emmanuelle Strowig, Till Franz-Wachtel, Mirita Macek, Boris Wagner, Samuel Hensel, Michael Erhardt, Marc PLoS Biol Research Article 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. Public Library of Science 2017-08-03 /pmc/articles/PMC5542435/ /pubmed/28771474 http://dx.doi.org/10.1371/journal.pbio.2002267 Text en © 2017 Fabiani et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Fabiani, Florian D. Renault, Thibaud T. Peters, Britta Dietsche, Tobias Gálvez, Eric J. C. Guse, Alina Freier, Karen Charpentier, Emmanuelle Strowig, Till Franz-Wachtel, Mirita Macek, Boris Wagner, Samuel Hensel, Michael Erhardt, Marc A flagellum-specific chaperone facilitates assembly of the core type III export apparatus of the bacterial flagellum |
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 |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5542435/ https://www.ncbi.nlm.nih.gov/pubmed/28771474 http://dx.doi.org/10.1371/journal.pbio.2002267 |
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