ATP and ADP actin states§

Authors

  • Dmitri S. Kudryashov,

    Corresponding author
    1. Department of Chemistry and Biochemistry, the Ohio State University, Columbus, OH 43210
    • Department of Chemistry and Biochemistry, the Ohio State University, Columbus, OH 43210
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  • Emil Reisler

    1. Department of Chemistry and Biochemistry and Molecular Biology Institute, University of California at Los Angeles (UCLA), Los Angeles, CA 90095
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  • Dedication: We dedicate this review to the memory of Henryk (Heini) Eisenberg, a truly outstanding scientist, with exceptional ability to develop and apply rigorous thermodynamic and physical approaches to the analysis of biological macromolecules and their interactions. One of us (E.R.) was fortunate to have been introduced as his graduate student to the fascinating world of self-assembly of biomolecules, specifically glutamic dehydrogenase. Heini's own interest in the dynamic equilibria states of this enzyme and their regulation by nucleotides was stimulated during his sabbatical at NIH and the collaboration with Gordon M. Tomkins. With his creative mastery of thermodynamics and light scattering theories and the ability to model and predict the link between the measured parameters and the arrangement of the enzyme's subunits, Heini was ahead of his time in mapping protein substructures in the absence of crystallography data.

  • Heini was an ideal mentor; inspiring, supportive, offering ideas, opening new vistas on how to solve challenging problems, and yet encouraging full independence and self-reliance of his students and postdoctoral fellows. He created an environment of intellectual ambition and curiosity and true excitement about learning how biomolecules function. The informal and supportive environment included also his family—his wife Nutzi and children Shai and Danny—as well as his students and postdocs families. Heini's support and friendship were a gift and asset that has accompanied me (E.R.) in all the years after I left his group. His legacy is in the outstanding publications and the scientists whose careers he helped to launch.

  • §

    This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

Abstract

This minireview is dedicated to the memory of Henryk Eisenberg and honors his major contributions to many areas of biophysics and to the analysis of macromolecular states and interactions in particular. This work reviews the ATP and ADP states of a ubiquitous protein, actins, and considers the present evidence for and against unique, nucleotide-dependent conformations of this protein. The effects of ATP and ADP on specific structural elements of actins, its loops and clefts, as revealed by mutational, crosslinking, spectroscopic, and EPR methods are discussed. It is concluded that the existing evidence points to dynamic equilibria of these structural elements among various conformational states in both ATP- and ADP-actins, with the nucleotides impacting the equilibria distributions. © 2012 Wiley Periodicals, Inc. Biopolymers 99: 245–256, 2013.

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