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A Historical Perspective of Actin Assembly and Its Interactions

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Molecular Interactions of Actin

Part of the book series: Results and Problems in Cell Differentiation ((RESULTS,volume 32))

Abstract

Actin was discovered by F. B. Straub more than 50 years ago as one of the main components of muscle proteins and as a partner of myosin for superprecipitation coupled with the hydrolysis of ATP (Straub 1942). When extracted from dried muscle powder into water, actin was in the state of dispersed monomers, named G-actin, and transformed to fibrous polymers, named F-actin, in a solution of neutral salts. With removal of salts, F-actin returned to G-actin. Later, he noticed that this G-F transformation was coupled with the hydrolysis of ATP bound to G-actin; ADP produced were kept bound to F-actin (Straub and Feuer 1950). The reverse transformation from F to G was not associated with rephosphorylation of bound ADP; G-actin released ADP and bound new ATP in solution.

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Authors and Affiliations

  1. Aichi Institute of Technology, Yagusa, Toyota, 470-0392, Japan

    Fumio Oosawa

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  1. Fumio Oosawa
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Editors and Affiliations

  1. Department of Anatomy and Histology, Institute for Biomedical Research, University of Sydney, 2006, Sydney, Australia

    Cristobal G. dos Remedios

  2. Department of Biochemistry, University of Minnesota, 55455, Minneapolis, MN, USA

    David D. Thomas

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© 2001 Springer-Verlag Berlin Heidelberg

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Oosawa, F. (2001). A Historical Perspective of Actin Assembly and Its Interactions. In: dos Remedios, C.G., Thomas, D.D. (eds) Molecular Interactions of Actin. Results and Problems in Cell Differentiation, vol 32. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-46560-7_2

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  • DOI: https://doi.org/10.1007/978-3-540-46560-7_2

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-53675-5

  • Online ISBN: 978-3-540-46560-7

  • eBook Packages: Springer Book Archive

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