Evolution of mechanical cooperativity among myosin II motors

Myosin II is a biomolecular machine that is responsible for muscle contraction. Myosin II motors act cooperatively: during muscle contraction, multiple motors bind to a single actin filament and pull it against an external load, like people pulling on a rope in a tug-of-war. We model the dynamics of...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2021-05, Vol.118 (20), p.1-6
Main Authors: Wagoner, Jason A., Dill, Ken A.
Format: Article
Language:English
Subjects:
Actin
Actomyosin
Adaptation
Biological Sciences
Cooperativity
Ecological adaptation
Evolution
Filaments
Motors
Muscle contraction
Muscles
Muscular function
Myosin
Physical Sciences
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Summary:Myosin II is a biomolecular machine that is responsible for muscle contraction. Myosin II motors act cooperatively: during muscle contraction, multiple motors bind to a single actin filament and pull it against an external load, like people pulling on a rope in a tug-of-war. We model the dynamics of actomyosin filaments in order to study the evolution of motor–motor cooperativity. We find that filament backsliding—the distance an actin slides backward when a motor at the end of its cycle releases—is central to the speed and efficiency of muscle contraction. Our model predicts that this backsliding has been reduced through evolutionary adaptations to the motor’s binding propensity, the strength of the motor’s power stroke, and the force dependence of the motor’s release from actin. These properties optimize the collective action of myosin II motors, which is not a simple sum of individual motor actions. The model also shows that these evolutionary variables can explain the speed–efficiency trade-off observed across different muscle tissues. This is an example of how evolution can tune the microscopic properties of individual proteins in order to optimize complex biological functions.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.2101871118