Cargando…
The type IV pilus protein PilU functions as a PilT-dependent retraction ATPase
Type IV pili are dynamic cell surface appendages found throughout the bacteria. The ability of these structures to undergo repetitive cycles of extension and retraction underpins their crucial roles in adhesion, motility and natural competence for transformation. In the best-studied systems a dedica...
Autores principales: | , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6762196/ https://www.ncbi.nlm.nih.gov/pubmed/31525185 http://dx.doi.org/10.1371/journal.pgen.1008393 |
_version_ | 1783454164793163776 |
---|---|
author | Adams, David W. Pereira, Jorge M. Stoudmann, Candice Stutzmann, Sandrine Blokesch, Melanie |
author_facet | Adams, David W. Pereira, Jorge M. Stoudmann, Candice Stutzmann, Sandrine Blokesch, Melanie |
author_sort | Adams, David W. |
collection | PubMed |
description | Type IV pili are dynamic cell surface appendages found throughout the bacteria. The ability of these structures to undergo repetitive cycles of extension and retraction underpins their crucial roles in adhesion, motility and natural competence for transformation. In the best-studied systems a dedicated retraction ATPase PilT powers pilus retraction. Curiously, a second presumed retraction ATPase PilU is often encoded immediately downstream of pilT. However, despite the presence of two potential retraction ATPases, pilT deletions lead to a total loss of pilus function, raising the question of why PilU fails to take over. Here, using the DNA-uptake pilus and mannose-sensitive haemagglutinin (MSHA) pilus of Vibrio cholerae as model systems, we show that inactivated PilT variants, defective for either ATP-binding or hydrolysis, have unexpected intermediate phenotypes that are PilU-dependent. In addition to demonstrating that PilU can function as a bona fide retraction ATPase, we go on to make the surprising discovery that PilU functions exclusively in a PilT-dependent manner and identify a naturally occurring pandemic V. cholerae PilT variant that renders PilU essential for pilus function. Finally, we show that Pseudomonas aeruginosa PilU also functions as a PilT-dependent retraction ATPase, providing evidence that the functional coupling between PilT and PilU could be a widespread mechanism for optimal pilus retraction. |
format | Online Article Text |
id | pubmed-6762196 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-67621962019-10-11 The type IV pilus protein PilU functions as a PilT-dependent retraction ATPase Adams, David W. Pereira, Jorge M. Stoudmann, Candice Stutzmann, Sandrine Blokesch, Melanie PLoS Genet Research Article Type IV pili are dynamic cell surface appendages found throughout the bacteria. The ability of these structures to undergo repetitive cycles of extension and retraction underpins their crucial roles in adhesion, motility and natural competence for transformation. In the best-studied systems a dedicated retraction ATPase PilT powers pilus retraction. Curiously, a second presumed retraction ATPase PilU is often encoded immediately downstream of pilT. However, despite the presence of two potential retraction ATPases, pilT deletions lead to a total loss of pilus function, raising the question of why PilU fails to take over. Here, using the DNA-uptake pilus and mannose-sensitive haemagglutinin (MSHA) pilus of Vibrio cholerae as model systems, we show that inactivated PilT variants, defective for either ATP-binding or hydrolysis, have unexpected intermediate phenotypes that are PilU-dependent. In addition to demonstrating that PilU can function as a bona fide retraction ATPase, we go on to make the surprising discovery that PilU functions exclusively in a PilT-dependent manner and identify a naturally occurring pandemic V. cholerae PilT variant that renders PilU essential for pilus function. Finally, we show that Pseudomonas aeruginosa PilU also functions as a PilT-dependent retraction ATPase, providing evidence that the functional coupling between PilT and PilU could be a widespread mechanism for optimal pilus retraction. Public Library of Science 2019-09-16 /pmc/articles/PMC6762196/ /pubmed/31525185 http://dx.doi.org/10.1371/journal.pgen.1008393 Text en © 2019 Adams 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 Adams, David W. Pereira, Jorge M. Stoudmann, Candice Stutzmann, Sandrine Blokesch, Melanie The type IV pilus protein PilU functions as a PilT-dependent retraction ATPase |
title | The type IV pilus protein PilU functions as a PilT-dependent retraction ATPase |
title_full | The type IV pilus protein PilU functions as a PilT-dependent retraction ATPase |
title_fullStr | The type IV pilus protein PilU functions as a PilT-dependent retraction ATPase |
title_full_unstemmed | The type IV pilus protein PilU functions as a PilT-dependent retraction ATPase |
title_short | The type IV pilus protein PilU functions as a PilT-dependent retraction ATPase |
title_sort | type iv pilus protein pilu functions as a pilt-dependent retraction atpase |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6762196/ https://www.ncbi.nlm.nih.gov/pubmed/31525185 http://dx.doi.org/10.1371/journal.pgen.1008393 |
work_keys_str_mv | AT adamsdavidw thetypeivpilusproteinpilufunctionsasapiltdependentretractionatpase AT pereirajorgem thetypeivpilusproteinpilufunctionsasapiltdependentretractionatpase AT stoudmanncandice thetypeivpilusproteinpilufunctionsasapiltdependentretractionatpase AT stutzmannsandrine thetypeivpilusproteinpilufunctionsasapiltdependentretractionatpase AT blokeschmelanie thetypeivpilusproteinpilufunctionsasapiltdependentretractionatpase AT adamsdavidw typeivpilusproteinpilufunctionsasapiltdependentretractionatpase AT pereirajorgem typeivpilusproteinpilufunctionsasapiltdependentretractionatpase AT stoudmanncandice typeivpilusproteinpilufunctionsasapiltdependentretractionatpase AT stutzmannsandrine typeivpilusproteinpilufunctionsasapiltdependentretractionatpase AT blokeschmelanie typeivpilusproteinpilufunctionsasapiltdependentretractionatpase |