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J. Biol. Chem., Vol. 282, Issue 46, 33769-33775, November 16, 2007

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Direct Binding of the Dynamin-like GTPase, Dnm1, to Mitochondrial Dynamics Protein Fis1 Is Negatively Regulated by the Fis1 N-terminal Arm^*

Robert C. Wells, Lora K. Picton, Sarah C. P. Williams¹, Frederick J. Tan², and R. Blake Hill³

From the Departments of Biology and Chemistry, The Johns Hopkins University, Baltimore, Maryland 21218

Recruitment of a dynamin-like GTPase (Drp1/Dlp1/Dnm1) to membranes requires the mitochondrial dynamics protein Fis1. Mdv1 has been proposed to act as an adaptor between Fis1 and Dnm1 in Saccharomyces cerevisiae. We show that S. cerevisiae Fis1 binds directly to Dnm1 and to Mdv1. Two Fis1 regions have been previously implicated in Mdv1 recruitment: an N-terminal "arm" and a concave surface formed by evolutionarily conserved residues in the tetratricopeptide repeat domain. Perturbing either Fis1 region does not affect Mdv1 binding, but both regions influence Dnm1 binding. Fis1 lacking its N-terminal arm binds tightly to Dnm1, and binding is abolished by mutations to the Fis1 concave surface. The Fis1-Dnm1 interaction decreases more than 100-fold in the presence of the Fis1 arm, suggesting that the arm acts in an autoinhibitory manner to restrict access to the Dnm1 binding site on Fis1. Our data indicate that the concave surface of the Fis1 tetratricopeptide repeat-like domain is evolutionarily conserved to bind the dynamin-like GTPase Dnm1 and not Mdv1 as previously predicted.

Received for publication, January 29, 2007 , and in revised form, September 17, 2007.

^* This work was supported by National Institutes of Health Grant RO1GM067180 and Training Grant 2T32GM007231 (to R. C. W., L. K. P., and F. J. T.) and American Cancer Society Award IRG-58-005-41. The costs of publication of this article were defrayed in part by the payment of page charges. This 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 supplemental Figs. 1-4.

¹ Supported in part by the Howard Hughes Medical Institute summer undergraduate research fellowship program.

² Supported in part by a Department of Defense NDSEG fellowship, and a Millipore Foundation Dimitri V. d'Arbeloff award.

³ To whom correspondence should be addressed: Dept. of Biology, Mudd Hall, The Johns Hopkins University, 3400 N. Charles St., Baltimore, MD 21218. Tel.: 410-516-6783; Fax: 702-441-2490; E-mail: hill{at}jhu.edu.

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