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.
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2 April 2001
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April 02 2001
Actin Depolymerizing Factor Stabilizes an Existing State of F-Actin and Can Change the Tilt of F-Actin Subunits
Vitold E. Galkin,
Vitold E. Galkin
aDepartment of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908
bDepartment of Cell Cultures, Institute of Cytology RAS, St. Petersburg, Russia
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Albina Orlova,
Albina Orlova
aDepartment of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908
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Natalya Lukoyanova,
Natalya Lukoyanova
aDepartment of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908
cInstitute of Theoretical and Experimental Biophysics RAS, Puschino, Russia
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Willy Wriggers,
Willy Wriggers
dDepartment of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037
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Edward H. Egelman
Edward H. Egelman
aDepartment of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908
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Vitold E. Galkin
aDepartment of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908
bDepartment of Cell Cultures, Institute of Cytology RAS, St. Petersburg, Russia
Albina Orlova
aDepartment of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908
Natalya Lukoyanova
aDepartment of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908
cInstitute of Theoretical and Experimental Biophysics RAS, Puschino, Russia
Willy Wriggers
dDepartment of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037
Edward H. Egelman
aDepartment of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908
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.
Received:
December 08 2000
Revision Requested:
February 01 2001
Accepted:
February 05 2001
Online ISSN: 1540-8140
Print ISSN: 0021-9525
© 2001 The Rockefeller University Press
2001
The Rockefeller University Press
J Cell Biol (2001) 153 (1): 75–86.
Article history
Received:
December 08 2000
Revision Requested:
February 01 2001
Accepted:
February 05 2001
Connected Content
Citation
Vitold E. Galkin, Albina Orlova, Natalya Lukoyanova, Willy Wriggers, Edward H. Egelman; Actin Depolymerizing Factor Stabilizes an Existing State of F-Actin and Can Change the Tilt of F-Actin Subunits. J Cell Biol 2 April 2001; 153 (1): 75–86. doi: https://doi.org/10.1083/jcb.153.1.75
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