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Originally published In Press as doi:10.1074/jbc.M203360200 on June 4, 2002

J. Biol. Chem., Vol. 277, Issue 32, 28774-28779, August 9, 2002
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Tropomyosin and Gelsolin Cooperate in Controlling the Microfilament System*

Maria Nyåkern-MeazzaDagger , Kartik Narayan§, Clarence E. Schutt§, and Uno LindbergDagger

From the Dagger  Department of Cell Biology, The Wenner-Gren Institute, Stockholm University, SE-10691 Stockholm, Sweden and § Henry Hoyt Laboratory, Department of Chemistry, Princeton University, Princeton, New Jersey 08544

Tropomyosin has been shown to cause annealing of gelsolin-capped actin filaments. Here we show that tropomyosin is highly efficient in transforming even the smallest gelsolin-actin complexes into long actin filaments. At low concentrations of tropomyosin, the effect of tropomyosin depends on the length of the actin oligomer, and the cooperative nature of the process is a direct indication that tropomyosin induces a conformational change in the gelsolin-actin complexes, altering the structure at the actin (+) end such that capping by gelsolin is abolished. At increased concentrations of tropomyosin, heterodimers, trimers, and tetramers are converted to actin filaments. In addition, evidence is presented demonstrating that gelsolin, once removed from the (+) end of the actin, can reassociate with the newly formed tropomyosin-decorated actin filaments. Interestingly, the binding of gelsolin to the tropomyosin-actin filament complexes saturates at 2 gelsolin molecules per 14 actin and 2 tropomyosins, i.e. two gelsolins per tropomyosin-regulatory unit along the filament. These observations support the view that both tropomyosin and gelsolin are likely to have important functions in addition to those proposed earlier.

* This work was supported by the Swedish Foundation for International Cooperation in Research and Higher Education (STINT), the Swedish Cancer Society, the Swedish Natural Science Research Council (NFR) (to U. L.) and National Institutes of Health Grant GM44038 (to C. E. S.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 46-8-164101; Fax: 46-8-159837; E-mail: uno@cellbio.su.se.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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