Robustness in an Ultrasensitive Motor

ABSTRACT In Escherichia coli, the chemotaxis response regulator CheY-P binds to FliM, a component of the switch complex at the base of the bacterial flagellar motor, to modulate the direction of motor rotation. The bacterial flagellar motor is ultrasensitive to the concentration of unbound CheY-P in...

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Autores principales:	Guangzhe Liu, Antai Tao, Rongjing Zhang, Junhua Yuan
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2020
Materias:	sensitivity molecular motor adaptive remodeling flagellar motor Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/febd3b8aae524c74a9c4448b42d61ee9
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spelling	oai:doaj.org-article:febd3b8aae524c74a9c4448b42d61ee92021-11-15T15:57:02ZRobustness in an Ultrasensitive Motor10.1128/mBio.03050-192150-7511https://doaj.org/article/febd3b8aae524c74a9c4448b42d61ee92020-04-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.03050-19https://doaj.org/toc/2150-7511ABSTRACT In Escherichia coli, the chemotaxis response regulator CheY-P binds to FliM, a component of the switch complex at the base of the bacterial flagellar motor, to modulate the direction of motor rotation. The bacterial flagellar motor is ultrasensitive to the concentration of unbound CheY-P in the cytoplasm. CheY-P binds to FliM molecules both in the cytoplasm and on the motor. As the concentration of FliM unavoidably varies from cell to cell, leading to a variation of unbound CheY-P concentration in the cytoplasm, this raises the question whether the flagellar motor is robust against this variation, that is, whether the rotational bias of the motor is more or less constant as the concentration of FliM varies. Here, we showed that the motor is robust against variations of the concentration of FliM. We identified adaptive remodeling of the motor as the mechanism for this robustness. As the level of FliM molecules changes, resulting in different amounts of the unbound CheY-P molecules, the motor adaptively changes the composition of its switch complex to compensate for this effect. IMPORTANCE The bacterial flagellar motor is an ultrasensitive motor. Its output, the probability of the motor turning clockwise, depends sensitively on the occupancy of the protein FliM (a component on the switch complex of the motor) by the input CheY-P molecules. With a limited cellular pool of CheY-P molecules, cell-to-cell variation of the FliM level would lead to large unwanted variation of the motor output if not compensated. Here, we showed that the motor output is robust against the variation of FliM level and identified the adaptive remodeling of the motor switch complex as the mechanism for this robustness.Guangzhe LiuAntai TaoRongjing ZhangJunhua YuanAmerican Society for Microbiologyarticlesensitivitymolecular motoradaptive remodelingflagellar motorMicrobiologyQR1-502ENmBio, Vol 11, Iss 2 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	sensitivity molecular motor adaptive remodeling flagellar motor Microbiology QR1-502
spellingShingle	sensitivity molecular motor adaptive remodeling flagellar motor Microbiology QR1-502 Guangzhe Liu Antai Tao Rongjing Zhang Junhua Yuan Robustness in an Ultrasensitive Motor
description	ABSTRACT In Escherichia coli, the chemotaxis response regulator CheY-P binds to FliM, a component of the switch complex at the base of the bacterial flagellar motor, to modulate the direction of motor rotation. The bacterial flagellar motor is ultrasensitive to the concentration of unbound CheY-P in the cytoplasm. CheY-P binds to FliM molecules both in the cytoplasm and on the motor. As the concentration of FliM unavoidably varies from cell to cell, leading to a variation of unbound CheY-P concentration in the cytoplasm, this raises the question whether the flagellar motor is robust against this variation, that is, whether the rotational bias of the motor is more or less constant as the concentration of FliM varies. Here, we showed that the motor is robust against variations of the concentration of FliM. We identified adaptive remodeling of the motor as the mechanism for this robustness. As the level of FliM molecules changes, resulting in different amounts of the unbound CheY-P molecules, the motor adaptively changes the composition of its switch complex to compensate for this effect. IMPORTANCE The bacterial flagellar motor is an ultrasensitive motor. Its output, the probability of the motor turning clockwise, depends sensitively on the occupancy of the protein FliM (a component on the switch complex of the motor) by the input CheY-P molecules. With a limited cellular pool of CheY-P molecules, cell-to-cell variation of the FliM level would lead to large unwanted variation of the motor output if not compensated. Here, we showed that the motor output is robust against the variation of FliM level and identified the adaptive remodeling of the motor switch complex as the mechanism for this robustness.
format	article
author	Guangzhe Liu Antai Tao Rongjing Zhang Junhua Yuan
author_facet	Guangzhe Liu Antai Tao Rongjing Zhang Junhua Yuan
author_sort	Guangzhe Liu
title	Robustness in an Ultrasensitive Motor
title_short	Robustness in an Ultrasensitive Motor
title_full	Robustness in an Ultrasensitive Motor
title_fullStr	Robustness in an Ultrasensitive Motor
title_full_unstemmed	Robustness in an Ultrasensitive Motor
title_sort	robustness in an ultrasensitive motor
publisher	American Society for Microbiology
publishDate	2020
url	https://doaj.org/article/febd3b8aae524c74a9c4448b42d61ee9
work_keys_str_mv	AT guangzheliu robustnessinanultrasensitivemotor AT antaitao robustnessinanultrasensitivemotor AT rongjingzhang robustnessinanultrasensitivemotor AT junhuayuan robustnessinanultrasensitivemotor
_version_	1718427068338798592

Robustness in an Ultrasensitive Motor

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