A bifunctional ATPase drives tad pilus extension and retraction

Authors

Courtney K. Ellison, Indiana University
Jingbo Kan, CUNY Brooklyn College
Jennifer L. Chlebek, Indiana University
Katherine R. Hummels, Indiana University
Gaёl Panis, University of Geneva
Patrick H. Viollier, University of Geneva
Nicolas Biais, CUNY Brooklyn CollegeFollow
Ankur B. Dalia, Indiana University
Yves V. Brun, Indiana University

Document Type

Article

Publication Date

12-18-2019

Abstract

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.

Comments

This work was originally published in Science Advances, available at DOI: 10.1126/sciadv.aay2591

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