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A bifunctional ATPase drives tad pilus extension and retraction
A widespread class of prokaryotic motors powered by secretion motor adenosine triphosphatases (ATPases) drives the dynamic extension and retraction of extracellular fibers, such as type IV pili (T4P). Among these, the tight adherence (tad) pili are critical for surface sensing and biofilm formation....
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Association for the Advancement of Science
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6920026/ https://www.ncbi.nlm.nih.gov/pubmed/31897429 http://dx.doi.org/10.1126/sciadv.aay2591 |
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author | Ellison, Courtney K. Kan, Jingbo Chlebek, Jennifer L. Hummels, Katherine R. Panis, Gaёl Viollier, Patrick H. Biais, Nicolas Dalia, Ankur B. Brun, Yves V. |
author_facet | Ellison, Courtney K. Kan, Jingbo Chlebek, Jennifer L. Hummels, Katherine R. Panis, Gaёl Viollier, Patrick H. Biais, Nicolas Dalia, Ankur B. Brun, Yves V. |
author_sort | Ellison, Courtney K. |
collection | PubMed |
description | A widespread class of prokaryotic motors powered by secretion motor adenosine triphosphatases (ATPases) drives the dynamic extension and retraction of extracellular fibers, such as type IV pili (T4P). Among these, the tight adherence (tad) pili are critical for surface sensing and biofilm formation. As for most other motors belonging to this class, how tad pili retract despite lacking a dedicated retraction motor ATPase has remained a mystery. Here, we find that a bifunctional pilus motor ATPase, CpaF, drives both activities through adenosine 5′-triphosphate (ATP) hydrolysis. We show that mutations within CpaF result in a correlated reduction in the rates of extension and retraction that directly scales with decreased ATP hydrolysis and retraction force. Thus, a single motor ATPase drives the bidirectional processes of pilus fiber extension and retraction. |
format | Online Article Text |
id | pubmed-6920026 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | American Association for the Advancement of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-69200262020-01-02 A bifunctional ATPase drives tad pilus extension and retraction Ellison, Courtney K. Kan, Jingbo Chlebek, Jennifer L. Hummels, Katherine R. Panis, Gaёl Viollier, Patrick H. Biais, Nicolas Dalia, Ankur B. Brun, Yves V. Sci Adv Research Articles A widespread class of prokaryotic motors powered by secretion motor adenosine triphosphatases (ATPases) drives the dynamic extension and retraction of extracellular fibers, such as type IV pili (T4P). Among these, the tight adherence (tad) pili are critical for surface sensing and biofilm formation. As for most other motors belonging to this class, how tad pili retract despite lacking a dedicated retraction motor ATPase has remained a mystery. Here, we find that a bifunctional pilus motor ATPase, CpaF, drives both activities through adenosine 5′-triphosphate (ATP) hydrolysis. We show that mutations within CpaF result in a correlated reduction in the rates of extension and retraction that directly scales with decreased ATP hydrolysis and retraction force. Thus, a single motor ATPase drives the bidirectional processes of pilus fiber extension and retraction. American Association for the Advancement of Science 2019-12-18 /pmc/articles/PMC6920026/ /pubmed/31897429 http://dx.doi.org/10.1126/sciadv.aay2591 Text en Copyright © 2019 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC). http://creativecommons.org/licenses/by-nc/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial license (http://creativecommons.org/licenses/by-nc/4.0/) , which permits use, distribution, and reproduction in any medium, so long as the resultant use is not for commercial advantage and provided the original work is properly cited. |
spellingShingle | Research Articles Ellison, Courtney K. Kan, Jingbo Chlebek, Jennifer L. Hummels, Katherine R. Panis, Gaёl Viollier, Patrick H. Biais, Nicolas Dalia, Ankur B. Brun, Yves V. A bifunctional ATPase drives tad pilus extension and retraction |
title | A bifunctional ATPase drives tad pilus extension and retraction |
title_full | A bifunctional ATPase drives tad pilus extension and retraction |
title_fullStr | A bifunctional ATPase drives tad pilus extension and retraction |
title_full_unstemmed | A bifunctional ATPase drives tad pilus extension and retraction |
title_short | A bifunctional ATPase drives tad pilus extension and retraction |
title_sort | bifunctional atpase drives tad pilus extension and retraction |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6920026/ https://www.ncbi.nlm.nih.gov/pubmed/31897429 http://dx.doi.org/10.1126/sciadv.aay2591 |
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