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DOI10.1073/pnas.1716002114
Catch bond drives stator mechanosensitivity in the bacterial flagellar motor
Nord A.L.; Gachon E.; Perez-Carrasco R.; Nirody J.A.; Barducci A.; Berry R.M.; Pedaci F.
发表日期2017
ISSN0027-8424
起始页码12952
结束页码12957
卷号114期号:49
英文摘要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. © 2017, National Academy of Sciences. All rights reserved.
英文关键词Bacterial flagellar motor; Catch bond; Escherichia coli; Mechanosensitivity; Molecular motor
语种英语
scopus关键词adsorption; Article; bacterial cell wall; bacterial flagellum; bacterial kinetics; force; mechanical stress; nonhuman; priority journal; stoichiometry; torque; biomechanics; chemistry; Escherichia coli; flagellum; kinetics; molecular model; Escherichia coli protein; molecular motor; Biomechanical Phenomena; Escherichia coli; Escherichia coli Proteins; Flagella; Kinetics; Models, Molecular; Molecular Motor Proteins
来源期刊Proceedings of the National Academy of Sciences of the United States of America
文献类型期刊论文
条目标识符http://gcip.llas.ac.cn/handle/2XKMVOVA/160570
作者单位Nord, A.L., Centre de Biochimie Structurale (CBS), INSERM, CNRS, Université de Montpellier, Montpellier, 34090, France; Gachon, E., Centre de Biochimie Structurale (CBS), INSERM, CNRS, Université de Montpellier, Montpellier, 34090, France; Perez-Carrasco, R., Department of Mathematics, University College London, London, WC1E 6BT, United Kingdom; Nirody, J.A., Biophysics Graduate Group, University of California, Berkeley, CA 94720, United States; Barducci, A., Centre de Biochimie Structurale (CBS), INSERM, CNRS, Université de Montpellier, Montpellier, 34090, France; Berry, R.M., Department of Physics, Clarendon Laboratory, University of Oxford, Oxford, OX1 2JD, United Kingdom; Pedaci, F., Centre de Biochimie Structurale (CBS), INSERM, CNRS, Université de Montpellier, Montpellier, 34090, France
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Nord A.L.,Gachon E.,Perez-Carrasco R.,et al. Catch bond drives stator mechanosensitivity in the bacterial flagellar motor[J],2017,114(49).
APA Nord A.L..,Gachon E..,Perez-Carrasco R..,Nirody J.A..,Barducci A..,...&Pedaci F..(2017).Catch bond drives stator mechanosensitivity in the bacterial flagellar motor.Proceedings of the National Academy of Sciences of the United States of America,114(49).
MLA Nord A.L.,et al."Catch bond drives stator mechanosensitivity in the bacterial flagellar motor".Proceedings of the National Academy of Sciences of the United States of America 114.49(2017).
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