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Temperature effect on the chemomechanical regulation of substeps within the power stroke of a single Myosin II

Myosin IIs in the skeletal muscle are highly efficient nanoscale machines evolved in nature. Understanding how they function can not only bring insights into various biological processes but also provide guidelines to engineer synthetic nanoscale motors working in the vicinity of thermal noise. Thou...

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Detalles Bibliográficos
Autores principales: Dong, Chenling, Chen, Bin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4726395/
https://www.ncbi.nlm.nih.gov/pubmed/26786569
http://dx.doi.org/10.1038/srep19506
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author Dong, Chenling
Chen, Bin
author_facet Dong, Chenling
Chen, Bin
author_sort Dong, Chenling
collection PubMed
description Myosin IIs in the skeletal muscle are highly efficient nanoscale machines evolved in nature. Understanding how they function can not only bring insights into various biological processes but also provide guidelines to engineer synthetic nanoscale motors working in the vicinity of thermal noise. Though it was clearly demonstrated that the behavior of a skeletal muscle fiber, or that of a single myosin was strongly affected by the temperature, how exactly the temperature affects the kinetics of a single myosin is not fully understood. By adapting the newly developed transitional state model, which successfully explained the intriguing motor force regulation during skeletal muscle contraction, here we systematically explain how exactly the power stroke of a single myosin proceeds, with the consideration of the chemomechanical regulation of sub-steps within the stroke. The adapted theory is then utilized to investigate the temperature effect on various aspects of the power stroke. Our analysis suggests that, though swing rates, the isometric force, and the maximal stroke size all strongly vary with the temperature, the temperature can have a very small effect on the releasable elastic energy within the power stroke.
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spelling pubmed-47263952016-01-27 Temperature effect on the chemomechanical regulation of substeps within the power stroke of a single Myosin II Dong, Chenling Chen, Bin Sci Rep Article Myosin IIs in the skeletal muscle are highly efficient nanoscale machines evolved in nature. Understanding how they function can not only bring insights into various biological processes but also provide guidelines to engineer synthetic nanoscale motors working in the vicinity of thermal noise. Though it was clearly demonstrated that the behavior of a skeletal muscle fiber, or that of a single myosin was strongly affected by the temperature, how exactly the temperature affects the kinetics of a single myosin is not fully understood. By adapting the newly developed transitional state model, which successfully explained the intriguing motor force regulation during skeletal muscle contraction, here we systematically explain how exactly the power stroke of a single myosin proceeds, with the consideration of the chemomechanical regulation of sub-steps within the stroke. The adapted theory is then utilized to investigate the temperature effect on various aspects of the power stroke. Our analysis suggests that, though swing rates, the isometric force, and the maximal stroke size all strongly vary with the temperature, the temperature can have a very small effect on the releasable elastic energy within the power stroke. Nature Publishing Group 2016-01-20 /pmc/articles/PMC4726395/ /pubmed/26786569 http://dx.doi.org/10.1038/srep19506 Text en Copyright © 2016, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Dong, Chenling
Chen, Bin
Temperature effect on the chemomechanical regulation of substeps within the power stroke of a single Myosin II
title Temperature effect on the chemomechanical regulation of substeps within the power stroke of a single Myosin II
title_full Temperature effect on the chemomechanical regulation of substeps within the power stroke of a single Myosin II
title_fullStr Temperature effect on the chemomechanical regulation of substeps within the power stroke of a single Myosin II
title_full_unstemmed Temperature effect on the chemomechanical regulation of substeps within the power stroke of a single Myosin II
title_short Temperature effect on the chemomechanical regulation of substeps within the power stroke of a single Myosin II
title_sort temperature effect on the chemomechanical regulation of substeps within the power stroke of a single myosin ii
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4726395/
https://www.ncbi.nlm.nih.gov/pubmed/26786569
http://dx.doi.org/10.1038/srep19506
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