Robustness in an Ultrasensitive Motor

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 molecu...

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Main Authors: Guangzhe Liu, Antai Tao, Rongjing Zhang, Junhua Yuan
Format: Article
Language:English
Published: American Society for Microbiology 2020-03-01
Series:mBio
Subjects:
Online Access:https://doi.org/10.1128/mBio.03050-19
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spelling doaj-1233fd7d6461433ba08b63067bce2c902021-07-02T12:45:43ZengAmerican Society for MicrobiologymBio2150-75112020-03-01112e03050-1910.1128/mBio.03050-19Robustness in an Ultrasensitive MotorGuangzhe LiuAntai TaoRongjing ZhangJunhua YuanThe 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.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.https://doi.org/10.1128/mBio.03050-19sensitivitymolecular motoradaptive remodelingflagellar motor
collection DOAJ
language English
format Article
sources DOAJ
author Guangzhe Liu
Antai Tao
Rongjing Zhang
Junhua Yuan
spellingShingle Guangzhe Liu
Antai Tao
Rongjing Zhang
Junhua Yuan
Robustness in an Ultrasensitive Motor
mBio
sensitivity
molecular motor
adaptive remodeling
flagellar motor
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
series mBio
issn 2150-7511
publishDate 2020-03-01
description 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.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.
topic sensitivity
molecular motor
adaptive remodeling
flagellar motor
url https://doi.org/10.1128/mBio.03050-19
work_keys_str_mv AT guangzheliu robustnessinanultrasensitivemotor
AT antaitao robustnessinanultrasensitivemotor
AT rongjingzhang robustnessinanultrasensitivemotor
AT junhuayuan robustnessinanultrasensitivemotor
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