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Different degrees of lever arm rotation control myosin step size
Myosins are actin-based motors that are generally believed to move by amplifying small structural changes in the core motor domain via a lever arm rotation of the light chain binding domain. However, the lack of a quantitative agreement between observed step sizes and the length of the proposed leve...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2003
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172898/ https://www.ncbi.nlm.nih.gov/pubmed/12719468 http://dx.doi.org/10.1083/jcb.200212039 |
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author | Köhler, Danny Ruff, Christine Meyhöfer, Edgar Bähler, Martin |
author_facet | Köhler, Danny Ruff, Christine Meyhöfer, Edgar Bähler, Martin |
author_sort | Köhler, Danny |
collection | PubMed |
description | Myosins are actin-based motors that are generally believed to move by amplifying small structural changes in the core motor domain via a lever arm rotation of the light chain binding domain. However, the lack of a quantitative agreement between observed step sizes and the length of the proposed lever arms from different myosins challenges this view. We analyzed the step size of rat myosin 1d (Myo1d) and surprisingly found that this myosin takes unexpectedly large steps in comparison to other myosins. Engineering the length of the light chain binding domain of rat Myo1d resulted in a linear increase of step size in relation to the putative lever arm length, indicative of a lever arm rotation of the light chain binding domain. The extrapolated pivoting point resided in the same region of the rat Myo1d head domain as in conventional myosins. Therefore, rat Myo1d achieves its larger working stroke by a large calculated ∼90° rotation of the light chain binding domain. These results demonstrate that differences in myosin step sizes are not only controlled by lever arm length, but also by substantial differences in the degree of lever arm rotation. |
format | Text |
id | pubmed-2172898 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2003 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21728982008-05-01 Different degrees of lever arm rotation control myosin step size Köhler, Danny Ruff, Christine Meyhöfer, Edgar Bähler, Martin J Cell Biol Report Myosins are actin-based motors that are generally believed to move by amplifying small structural changes in the core motor domain via a lever arm rotation of the light chain binding domain. However, the lack of a quantitative agreement between observed step sizes and the length of the proposed lever arms from different myosins challenges this view. We analyzed the step size of rat myosin 1d (Myo1d) and surprisingly found that this myosin takes unexpectedly large steps in comparison to other myosins. Engineering the length of the light chain binding domain of rat Myo1d resulted in a linear increase of step size in relation to the putative lever arm length, indicative of a lever arm rotation of the light chain binding domain. The extrapolated pivoting point resided in the same region of the rat Myo1d head domain as in conventional myosins. Therefore, rat Myo1d achieves its larger working stroke by a large calculated ∼90° rotation of the light chain binding domain. These results demonstrate that differences in myosin step sizes are not only controlled by lever arm length, but also by substantial differences in the degree of lever arm rotation. The Rockefeller University Press 2003-04-28 /pmc/articles/PMC2172898/ /pubmed/12719468 http://dx.doi.org/10.1083/jcb.200212039 Text en Copyright © 2003, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Report Köhler, Danny Ruff, Christine Meyhöfer, Edgar Bähler, Martin Different degrees of lever arm rotation control myosin step size |
title | Different degrees of lever arm rotation control myosin step size |
title_full | Different degrees of lever arm rotation control myosin step size |
title_fullStr | Different degrees of lever arm rotation control myosin step size |
title_full_unstemmed | Different degrees of lever arm rotation control myosin step size |
title_short | Different degrees of lever arm rotation control myosin step size |
title_sort | different degrees of lever arm rotation control myosin step size |
topic | Report |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172898/ https://www.ncbi.nlm.nih.gov/pubmed/12719468 http://dx.doi.org/10.1083/jcb.200212039 |
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