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

doi:10.1083/jcb.153.1.75

Published online 2 April 2001. doi:10.1083/jcb.153.1.75

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© The Rockefeller University Press, 0021-9525/2001/4/75/ $5.00
The Journal of Cell Biology, Volume 153, Number 1, April 2, 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. Galkin^a,b, Albina Orlova^a, Natalya Lukoyanova^a,c, Willy Wriggers^d, and Edward H. Egelman^a
^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

Correspondence to: Edward H. Egelman, Department of Biochemistry and Molecular Genetics, Box 800733, University of Virginia Health Sciences Center, Charlottesville, VA 22908-0733. Tel:(804) 924-8210 Fax:(804) 924-5069 E-mail:egelman{at}virginia.edu.

Proteins in the actin depolymerizing factor (ADF)/cofilin familyare essential for rapid F-actin turnover, and most depolymerizeactin in a pH-dependent manner. Complexes of human and plantADF with F-actin at different pH were examined using electronmicroscopy and a novel method of image analysis for helicalfilaments. Although ADF changes the mean twist of actin, weshow that it does this by stabilizing a preexisting F-actinangular conformation. In addition, ADF induces a large ( $~$ 12°)tilt of actin subunits at high pH where filaments are readilydisrupted. A second ADF molecule binds to a site on the oppositeside of F-actin from that of the previously described ADF bindingsite, and this second site is only largely occupied at highpH. All of these states display a high degree of cooperativitythat appears to be an integral part of F-actin.

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

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