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J Biol Chem, Vol. 273, Issue 33, 20894-20902, August 14, 1998

Kinetic Analysis of the Interaction of Actin-depolymerizing Factor (ADF)/Cofilin with G- and F-Actins
COMPARISON OF PLANT AND HUMAN ADFs AND EFFECT OF PHOSPHORYLATION

Fariza RessadDagger , Dominique DidryDagger , Gui-Xian Xia§, Yan Hong§, Nam-Hai Chua, Dominique PantaloniDagger , and Marie-France CarlierDagger

From the Dagger  Dynamique du Cytosquelette, Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, 91198 Gif-sur-Yvette, France, the § Laboratory of Plant Cell Biology, Institute of Molecular Agrobiology, National University of Singapore, Singapore 118240, and the  Laboratory of Plant Molecular Biology, Rockefeller University, New York, New York 10021

The thermodynamics and kinetics of actin interaction with Arabidopsis thaliana actin-depolymerizing factor (ADF)1, human ADF, and S6D mutant ADF1 protein mimicking phosphorylated (inactive) ADF are examined comparatively. ADFs interact with ADP·G-actin in rapid equilibrium (k+ = 155 µM-1·s-1 and k- = 16 s-1 at 4 °C under physiological ionic conditions). The kinetics of interaction of plant and human ADFs with F-actin are slower and exhibit kinetic cooperativity, consistent with a scheme in which the initial binding of ADF to two adjacent subunits of the filament nucleates a structural change that propagates along the filament, allowing faster binding of ADF in a "zipper" mode. ADF binds in a non-cooperative faster process to gelsolin-capped filaments or to subtilisin-cleaved F-actin, which are structurally different from standard filaments (Orlova, A., Prochniewicz, E., and Egelman, E. H. (1995) J. Mol. Biol. 245, 598-607). In contrast, the binding of phalloidin to F-actin cooperatively inhibits its interaction with ADF. The ADF-facilitated nucleation of ADP·actin self-assembly indicates that ADF stabilizes lateral interactions in the filament. Plant and human ADFs cause only partial depolymerization of F-actin at pH 8, consistent with identical functions in enhancing F-actin dynamics. Phosphorylation does not affect ADF activity per se, but decreases its affinity for actin by 20-fold.


Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.



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