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Minimum requirements for the actin-like treadmilling motor system

Actin is one of the most abundant proteins in eukaryote cells, which forms a double stranded filament. The actin filament is not only a main component of the cytoskeleton, but also acts as a motor protein which moves toward one specific end, the barbed end, driven by polymerization at the barbed end...

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Detalles Bibliográficos
Autor principal: Narita, Akihiro
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Landes Bioscience 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3384570/
https://www.ncbi.nlm.nih.gov/pubmed/22754609
http://dx.doi.org/10.4161/bioa.18115
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author Narita, Akihiro
author_facet Narita, Akihiro
author_sort Narita, Akihiro
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description Actin is one of the most abundant proteins in eukaryote cells, which forms a double stranded filament. The actin filament is not only a main component of the cytoskeleton, but also acts as a motor protein which moves toward one specific end, the barbed end, driven by polymerization at the barbed end and depolymerization at the other end, the pointed end, without any associated proteins. This motor activity is referred to as “treadmilling” and it represents the simplest motor system known, consisting of only one 42 kDa protein, actin. Here we report the minimum requirements of the actin-like motor system elucidated by computer simulations: (1) Nucleotide binding and ATPase activity in the filament; (2) Polarity in the rates of polymerization and depolymerization between the two ends; and (3) The dependence of the subunit-subunit interactions on the bound nucleotide. These requirements are simple and this knowledge should facilitate the development of artificial molecular motor systems in the future.
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spelling pubmed-33845702012-06-29 Minimum requirements for the actin-like treadmilling motor system Narita, Akihiro Bioarchitecture Perspective Actin is one of the most abundant proteins in eukaryote cells, which forms a double stranded filament. The actin filament is not only a main component of the cytoskeleton, but also acts as a motor protein which moves toward one specific end, the barbed end, driven by polymerization at the barbed end and depolymerization at the other end, the pointed end, without any associated proteins. This motor activity is referred to as “treadmilling” and it represents the simplest motor system known, consisting of only one 42 kDa protein, actin. Here we report the minimum requirements of the actin-like motor system elucidated by computer simulations: (1) Nucleotide binding and ATPase activity in the filament; (2) Polarity in the rates of polymerization and depolymerization between the two ends; and (3) The dependence of the subunit-subunit interactions on the bound nucleotide. These requirements are simple and this knowledge should facilitate the development of artificial molecular motor systems in the future. Landes Bioscience 2011-09-01 /pmc/articles/PMC3384570/ /pubmed/22754609 http://dx.doi.org/10.4161/bioa.18115 Text en Copyright © 2011 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.
spellingShingle Perspective
Narita, Akihiro
Minimum requirements for the actin-like treadmilling motor system
title Minimum requirements for the actin-like treadmilling motor system
title_full Minimum requirements for the actin-like treadmilling motor system
title_fullStr Minimum requirements for the actin-like treadmilling motor system
title_full_unstemmed Minimum requirements for the actin-like treadmilling motor system
title_short Minimum requirements for the actin-like treadmilling motor system
title_sort minimum requirements for the actin-like treadmilling motor system
topic Perspective
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3384570/
https://www.ncbi.nlm.nih.gov/pubmed/22754609
http://dx.doi.org/10.4161/bioa.18115
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