Catch bond drives stator mechanosensitivity in the bacterial flagellar motor.
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 turn...
| Main Authors: | , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
National Academy of Sciences
2017
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| _version_ | 1797059055282290688 |
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| author | Nord, A Gachon, E Perez-Carrasco, R Nirody, J Barducci, A Berry, R Pedaci, F |
| author_facet | Nord, A Gachon, E Perez-Carrasco, R Nirody, J Barducci, A Berry, R Pedaci, F |
| author_sort | Nord, A |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-06T19:58:50Z |
| format | Journal article |
| id | oxford-uuid:2692757b-7721-4ecc-9a36-d4a5ea5aee22 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T19:58:50Z |
| publishDate | 2017 |
| publisher | National Academy of Sciences |
| record_format | dspace |
| spelling | oxford-uuid:2692757b-7721-4ecc-9a36-d4a5ea5aee222022-03-26T12:01:50ZCatch bond drives stator mechanosensitivity in the bacterial flagellar motor.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:2692757b-7721-4ecc-9a36-d4a5ea5aee22EnglishSymplectic Elements at OxfordNational Academy of Sciences2017Nord, AGachon, EPerez-Carrasco, RNirody, JBarducci, ABerry, RPedaci, FThe 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. |
| spellingShingle | Nord, A Gachon, E Perez-Carrasco, R Nirody, J Barducci, A Berry, R Pedaci, F Catch bond drives stator mechanosensitivity in the bacterial flagellar motor. |
| title | Catch bond drives stator mechanosensitivity in the bacterial flagellar motor. |
| title_full | Catch bond drives stator mechanosensitivity in the bacterial flagellar motor. |
| title_fullStr | Catch bond drives stator mechanosensitivity in the bacterial flagellar motor. |
| title_full_unstemmed | Catch bond drives stator mechanosensitivity in the bacterial flagellar motor. |
| title_short | Catch bond drives stator mechanosensitivity in the bacterial flagellar motor. |
| title_sort | catch bond drives stator mechanosensitivity in the bacterial flagellar motor |
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