Journal article
Catch bond drives stator mechanosensitivity in the bacterial flagellar motor.
- Abstract:
- The bacterial flagellar motor (BFM) is the rotary motor that rotates each bacterial flagellum, powering the swimming and swarming of many motile bacteria. The torque is provided by stator units, ion motive force-powered ion channels known to assemble and disassemble dynamically in the BFM. This turnover is mechanosensitive, with the number of engaged units dependent on the viscous load experienced by the motor through the flagellum. However, the molecular mechanism driving BFM mechanosensitivity is unknown. Here, we directly measure the kinetics of arrival and departure of the stator units in individual motors via analysis of high-resolution recordings of motor speed, while dynamically varying the load on the motor via external magnetic torque. The kinetic rates obtained, robust with respect to the details of the applied adsorption model, indicate that the lifetime of an assembled stator unit increases when a higher force is applied to its anchoring point in the cell wall. This provides strong evidence that a catch bond (a bond strengthened instead of weakened by force) drives mechanosensitivity of the flagellar motor complex. These results add the BFM to a short, but growing, list of systems demonstrating catch bonds, suggesting that this "molecular strategy" is a widespread mechanism to sense and respond to mechanical stress. We propose that force-enhanced stator adhesion allows the cell to adapt to a heterogeneous environmental viscosity and may ultimately play a role in surface-sensing during swarming and biofilm formation.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Preview, Version of record, pdf, 1.5MB, Terms of use)
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- Publisher copy:
- 10.1073/pnas.1716002114
Authors
- Publisher:
- National Academy of Sciences
- Journal:
- Proceedings of the National Academy of Sciences More from this journal
- Volume:
- 114
- Issue:
- 49
- Pages:
- 12952-12957
- Publication date:
- 2017-11-01
- Acceptance date:
- 2017-10-27
- DOI:
- EISSN:
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1091-6490
- ISSN:
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0027-8424
- Pmid:
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29183968
- Language:
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English
- Keywords:
- Pubs id:
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pubs:811247
- UUID:
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uuid:2692757b-7721-4ecc-9a36-d4a5ea5aee22
- Local pid:
-
pubs:811247
- Source identifiers:
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811247
- Deposit date:
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2018-03-26
Terms of use
- Copyright holder:
- Berry et al
- Copyright date:
- 2017
- Notes:
- Copyright © 2017 the Author(s). Published by PNAS. This open access article is distributed under Creative Commons Attribution-NonCommercial-NoDerivatives License 4.0 (CC BY-NC-ND).
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