A change in actin conformation associated with filament instability after P <sub>i</sub> release
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- Lisa D. Belmont
- Department of Molecular and Cellular Biology, University of California, Berkeley, CA 94720-3202; and Department of Cell Biology and Neuroanatomy, University of Minnesota Medical School, Minneapolis, MN 55455
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- Albina Orlova
- Department of Molecular and Cellular Biology, University of California, Berkeley, CA 94720-3202; and Department of Cell Biology and Neuroanatomy, University of Minnesota Medical School, Minneapolis, MN 55455
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- David G. Drubin
- Department of Molecular and Cellular Biology, University of California, Berkeley, CA 94720-3202; and Department of Cell Biology and Neuroanatomy, University of Minnesota Medical School, Minneapolis, MN 55455
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- Edward H. Egelman
- Department of Molecular and Cellular Biology, University of California, Berkeley, CA 94720-3202; and Department of Cell Biology and Neuroanatomy, University of Minnesota Medical School, Minneapolis, MN 55455
書誌事項
- 公開日
- 1999-01-05
- DOI
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- 10.1073/pnas.96.1.29
- 公開者
- Proceedings of the National Academy of Sciences
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説明
<jats:p> The ability of actin to both polymerize into filaments and to depolymerize permits the rapid rearrangements of actin structures that are essential for actin’s function in most cellular processes. Filament polarity and dynamic properties are conferred by the hydrolysis of ATP on actin filaments. Release of inorganic phosphate (P <jats:sub>i</jats:sub> ) from filaments after ATP hydrolysis promotes depolymerization. We identify a yeast actin mutation, Val-159 to Asn, which uncouples P <jats:sub>i</jats:sub> release from the conformational change that results in filament destabilization. Three-dimensional reconstructions of electron micrographs reveal a conformational difference between ADP-P <jats:sub>i</jats:sub> filaments and ADP filaments and show that ADP V159N filaments resemble ADP-P <jats:sub>i</jats:sub> wild-type filaments. Crystal structures of mammalian β-actin in which the nucleotide binding cleft is in the “open” and “closed” states can be used to model actin filaments in the ADP and ADP-P <jats:sub>i</jats:sub> conformations, respectively. We propose that these two conformations of G-actin may be related to two functional states of F-actin. </jats:p>
収録刊行物
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 96 (1), 29-34, 1999-01-05
Proceedings of the National Academy of Sciences