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Relaxation time asymmetry in stator dynamics of the bacterial flagellar motor

View ORCID ProfileRuben Perez-Carrasco, María-José Franco-Oñate, Jean-Charles Walter, Jérôme Dorignac, Fred Geniet, John Palmeri, Andrea Parmeggiani, Nils-Ole Walliser, View ORCID ProfileAshley L Nord
doi: https://doi.org/10.1101/2021.07.05.451114
Ruben Perez-Carrasco
aDepartment of Life Sciences, Imperial College London, London, SW7 2BU UK
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María-José Franco-Oñate
bLaboratoire Charles Coulomb (L2C), Univ. Montpellier, CNRS, Montpellier, France
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Jean-Charles Walter
bLaboratoire Charles Coulomb (L2C), Univ. Montpellier, CNRS, Montpellier, France
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Jérôme Dorignac
bLaboratoire Charles Coulomb (L2C), Univ. Montpellier, CNRS, Montpellier, France
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Fred Geniet
bLaboratoire Charles Coulomb (L2C), Univ. Montpellier, CNRS, Montpellier, France
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John Palmeri
bLaboratoire Charles Coulomb (L2C), Univ. Montpellier, CNRS, Montpellier, France
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Andrea Parmeggiani
bLaboratoire Charles Coulomb (L2C), Univ. Montpellier, CNRS, Montpellier, France
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Nils-Ole Walliser
bLaboratoire Charles Coulomb (L2C), Univ. Montpellier, CNRS, Montpellier, France
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Ashley L Nord
cCentre de Biologie Structurale U. Montpellier, CNRS, INSERM, Montpellier, 34090 France
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  • ORCID record for Ashley L Nord
  • For correspondence: ashley.nord@cbs.cnrs.fr
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Abstract

The bacterial flagellar motor (BFM) is the membrane-embedded rotary molecular motor which turns the flagellum that provides thrust to many bacterial species. This large multimeric complex, composed of a few dozen constituent proteins, has emerged as a hallmark of dynamic subunit exchange. The stator units are inner-membrane ion channels which dynamically bind and unbind to the peptidoglycan at the rotor periphery, consuming the ion motive force (IMF) and applying torque to the rotor when bound. The dynamic exchange is known to be a function of the viscous load on the flagellum, allowing the bacterium to dynamically adapt to its local viscous environment, but the molecular mechanisms of exchange and mechanosensitivity remain to be revealed. Here, by actively perturbing the steady-state stator stoichiometry of individual motors, we reveal a stoichiometry-dependent asymmetry in stator remodeling kinetics. We interrogate the potential effect of next-neighbor interactions and local stator unit depletion and find that neither can explain the observed asymmetry. We then simulate and fit two mechanistically diverse models which recapitulate the asymmetry, finding stator assembly dynamics to be particularly well described by a two-state catch-bond mechanism.

Competing Interest Statement

The authors have declared no competing interest.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC 4.0 International license.
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Posted July 06, 2021.
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Relaxation time asymmetry in stator dynamics of the bacterial flagellar motor
Ruben Perez-Carrasco, María-José Franco-Oñate, Jean-Charles Walter, Jérôme Dorignac, Fred Geniet, John Palmeri, Andrea Parmeggiani, Nils-Ole Walliser, Ashley L Nord
bioRxiv 2021.07.05.451114; doi: https://doi.org/10.1101/2021.07.05.451114
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Relaxation time asymmetry in stator dynamics of the bacterial flagellar motor
Ruben Perez-Carrasco, María-José Franco-Oñate, Jean-Charles Walter, Jérôme Dorignac, Fred Geniet, John Palmeri, Andrea Parmeggiani, Nils-Ole Walliser, Ashley L Nord
bioRxiv 2021.07.05.451114; doi: https://doi.org/10.1101/2021.07.05.451114

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