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Distribution and evolution of stable single α-helices (SAH domains) in myosin motor proteins

Stable single-alpha helices (SAHs) are versatile structural elements in many prokaryotic and eukaryotic proteins acting as semi-flexible linkers and constant force springs. This way SAH-domains function as part of the lever of many different myosins. Canonical myosin levers consist of one or several...

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Detalles Bibliográficos
Autores principales: Simm, Dominic, Hatje, Klas, Kollmar, Martin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5378345/
https://www.ncbi.nlm.nih.gov/pubmed/28369123
http://dx.doi.org/10.1371/journal.pone.0174639
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author Simm, Dominic
Hatje, Klas
Kollmar, Martin
author_facet Simm, Dominic
Hatje, Klas
Kollmar, Martin
author_sort Simm, Dominic
collection PubMed
description Stable single-alpha helices (SAHs) are versatile structural elements in many prokaryotic and eukaryotic proteins acting as semi-flexible linkers and constant force springs. This way SAH-domains function as part of the lever of many different myosins. Canonical myosin levers consist of one or several IQ-motifs to which light chains such as calmodulin bind. SAH-domains provide flexibility in length and stiffness to the myosin levers, and may be particularly suited for myosins working in crowded cellular environments. Although the function of the SAH-domains in human class-6 and class-10 myosins has well been characterised, the distribution of the SAH-domain in all myosin subfamilies and across the eukaryotic tree of life remained elusive. Here, we analysed the largest available myosin sequence dataset consisting of 7919 manually annotated myosin sequences from 938 species representing all major eukaryotic branches using the SAH-prediction algorithm of Waggawagga, a recently developed tool for the identification of SAH-domains. With this approach we identified SAH-domains in more than one third of the supposed 79 myosin subfamilies. Depending on the myosin class, the presence of SAH-domains can range from a few to almost all class members indicating complex patterns of independent and taxon-specific SAH-domain gain and loss.
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spelling pubmed-53783452017-04-07 Distribution and evolution of stable single α-helices (SAH domains) in myosin motor proteins Simm, Dominic Hatje, Klas Kollmar, Martin PLoS One Research Article Stable single-alpha helices (SAHs) are versatile structural elements in many prokaryotic and eukaryotic proteins acting as semi-flexible linkers and constant force springs. This way SAH-domains function as part of the lever of many different myosins. Canonical myosin levers consist of one or several IQ-motifs to which light chains such as calmodulin bind. SAH-domains provide flexibility in length and stiffness to the myosin levers, and may be particularly suited for myosins working in crowded cellular environments. Although the function of the SAH-domains in human class-6 and class-10 myosins has well been characterised, the distribution of the SAH-domain in all myosin subfamilies and across the eukaryotic tree of life remained elusive. Here, we analysed the largest available myosin sequence dataset consisting of 7919 manually annotated myosin sequences from 938 species representing all major eukaryotic branches using the SAH-prediction algorithm of Waggawagga, a recently developed tool for the identification of SAH-domains. With this approach we identified SAH-domains in more than one third of the supposed 79 myosin subfamilies. Depending on the myosin class, the presence of SAH-domains can range from a few to almost all class members indicating complex patterns of independent and taxon-specific SAH-domain gain and loss. Public Library of Science 2017-04-03 /pmc/articles/PMC5378345/ /pubmed/28369123 http://dx.doi.org/10.1371/journal.pone.0174639 Text en © 2017 Simm et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Simm, Dominic
Hatje, Klas
Kollmar, Martin
Distribution and evolution of stable single α-helices (SAH domains) in myosin motor proteins
title Distribution and evolution of stable single α-helices (SAH domains) in myosin motor proteins
title_full Distribution and evolution of stable single α-helices (SAH domains) in myosin motor proteins
title_fullStr Distribution and evolution of stable single α-helices (SAH domains) in myosin motor proteins
title_full_unstemmed Distribution and evolution of stable single α-helices (SAH domains) in myosin motor proteins
title_short Distribution and evolution of stable single α-helices (SAH domains) in myosin motor proteins
title_sort distribution and evolution of stable single α-helices (sah domains) in myosin motor proteins
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5378345/
https://www.ncbi.nlm.nih.gov/pubmed/28369123
http://dx.doi.org/10.1371/journal.pone.0174639
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