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Originally published In Press as doi:10.1074/jbc.M007563200 on October 24, 2000

J. Biol. Chem., Vol. 276, Issue 8, 5952-5958, February 23, 2001
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The C-terminal Tail of UNC-60B (Actin Depolymerizing Factor/Cofilin) Is Critical for Maintaining Its Stable Association with F-actin and Is Implicated in the Second Actin-binding Site*,

Shoichiro OnoDagger §, Amy McGough, Brian J. Pope||, Vincent T. Tolbert**, Alice BuiDagger , Jan PohlDagger Dagger , Guy M. BenianDagger , Kim M. Gernert§§, and Alan G. Weeds||

From the Dagger  Department of Pathology, Emory University, Atlanta, Georgia 30322, the  Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, || Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 2QH, United Kingdom, ** Frederick Douglas High School, Atlanta, Georgia 30030, the Dagger Dagger  Microchemical Facility, Winship Cancer Institute, Emory University, Atlanta, Georgia 30322, and §§ BIMCORE, Molecular Graphics, Emory University, Atlanta, Georgia 30322

Actin depolymerizing factor (ADF)/cofilin changes the twist of actin filaments by binding two longitudinally associated actin subunits. In the absence of an atomic model of the ADF/cofilin-F-actin complex, we have identified residues in ADF/cofilin that are essential for filament binding. Here, we have characterized the C-terminal tail of UNC-60B (a nematode ADF/cofilin isoform) as a novel determinant for its association with F-actin. Removal of the C-terminal isoleucine (Ile152) by carboxypeptidase A or truncation by mutagenesis eliminated F-actin binding activity but strongly enhanced actin depolymerizing activity. Replacement of Ile152 by Ala had a similar but less marked effect; F-actin binding was weakened and depolymerizing activity slightly enhanced. Truncation of both Arg151 and Ile152 or replacement of Arg151 with Ala also abolished F-actin binding and enhanced depolymerizing activity. Loss of F-actin binding in these mutants was accompanied by loss or greatly decreased severing activity. All of the variants of UNC-60B interacted with G-actin in an indistinguishable manner from wild type. Cryoelectron microscopy showed that UNC-60B changed the twist of F-actin to a similar extent to vertebrate ADF/cofilins. Helical reconstruction and structural modeling of UNC-60B-F-actin complex reveal how the C terminus of UNC-60B might be involved in one of the two actin-binding sites.

* This work was supported by the American Heart Association Southeast Affiliate Grant 9960146V (to S. O.), the National Science Foundation Grant MCB-9728762 (to G. M. B.), and National Institutes of Health Grant GM59677 (to A. M.).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.

The on-line version of this article (available at http://www.jbc.org) contains coordinates and structures. To view these PDB files, you may use Rasmol software (http://www.rasmol.org).

§ To whom correspondence should be addressed: Dept. of Pathology, Emory University, 1639 Pierce Dr., Woodruff Memorial Bldg., Rm. 7109C, Atlanta, GA 30322. Tel.: 404-727-3916; Fax: 404-727-8540; E-mail: ono@bimcore.emory.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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