A bifunctional ATPase drives tad pilus extension and retraction.
- Ellison CK Department of Biology, Indiana University, 1001 E. 3rd Street, Bloomington, IN 47405, USA.
- Kan J Biology Department, CUNY Brooklyn College, 2900 Bedford Avenue, Brooklyn, NY 11210, USA.
- Chlebek JL Department of Biology, Indiana University, 1001 E. 3rd Street, Bloomington, IN 47405, USA.
- Hummels KR Department of Biology, Indiana University, 1001 E. 3rd Street, Bloomington, IN 47405, USA.
- Panis G Department of Microbiology and Molecular Medicine, Faculty of Medicine, University of Geneva, Geneva, Switzerland.
- Viollier PH Department of Microbiology and Molecular Medicine, Faculty of Medicine, University of Geneva, Geneva, Switzerland.
- Biais N Biology Department, CUNY Brooklyn College, 2900 Bedford Avenue, Brooklyn, NY 11210, USA.
- Dalia AB Department of Biology, Indiana University, 1001 E. 3rd Street, Bloomington, IN 47405, USA.
- Brun YV Department of Biology, Indiana University, 1001 E. 3rd Street, Bloomington, IN 47405, USA.
- 2020-01-04
Published in:
- Science advances. - 2019
Adenosine Triphosphatases
Adenosine Triphosphate
Catalytic Domain
Caulobacter crescentus
Caulobacteraceae
Fimbriae Proteins
Fimbriae, Bacterial
Hydrolysis
Molecular Motor Proteins
Phylogeny
English
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.
- Language
-
- English
- Open access status
- gold
- Identifiers
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- DOI 10.1126/sciadv.aay2591
- PMID 31897429
- Persistent URL
- https://folia.unifr.ch/global/documents/138310
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