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Published online 2 April 2001. doi:10.1083/jcb.153.1.75
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© The Rockefeller University Press, 0021-9525/2001//75 $5.00
The Journal of Cell Biology, Volume 153, Number 1, , 2001 75-86

Original Article

Actin Depolymerizing Factor Stabilizes an Existing State of F-Actin and Can Change the Tilt of F-Actin Subunits



Vitold E. Galkina,b, Albina Orlovaa, Natalya Lukoyanovaa,c, Willy Wriggersd, and Edward H. Egelmana

a Department of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908
b Department of Cell Cultures, Institute of Cytology RAS, St. Petersburg, Russia
c Institute of Theoretical and Experimental Biophysics RAS, Puschino, Russia
d Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037
Department of Biochemistry and Molecular Genetics, Box 800733, University of Virginia Health Sciences Center, Charlottesville, VA 22908-0733.(804) 924-5069(804) 924-8210

egelman{at}virginia.edu

Proteins in the actin depolymerizing factor (ADF)/cofilin family are essential for rapid F-actin turnover, and most depolymerize actin in a pH-dependent manner. Complexes of human and plant ADF with F-actin at different pH were examined using electron microscopy and a novel method of image analysis for helical filaments. Although ADF changes the mean twist of actin, we show that it does this by stabilizing a preexisting F-actin angular conformation. In addition, ADF induces a large (~12°) tilt of actin subunits at high pH where filaments are readily disrupted. A second ADF molecule binds to a site on the opposite side of F-actin from that of the previously described ADF binding site, and this second site is only largely occupied at high pH. All of these states display a high degree of cooperativity that appears to be an integral part of F-actin.

Key Words: actin • ADF • cooperativity • electron microscopy • image processing

© 2001 The Rockefeller University Press

Abbreviations used in this paper: ADF, actin depolymerizing factor; h-ADF, human ADF; IHRSR, iterative helical real space reconstruction; p-ADF, plant A. thaliana ADF1.


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