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J. Biol. Chem., Vol. 280, Issue 15, 15348-15355, April 15, 2005

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ATP-independent Control of Vac8 Palmitoylation by a SNARE Subcomplex on Yeast Vacuoles^*

Lars E. P. Dietrich**, Tracy J. LaGrassa**, Jan Rohde, Marina Cristodero¶, Christoph T. A. Meiringer, and Christian Ungermann||

From the Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany

Yeast vacuole fusion requires palmitoylated Vac8. We previously showed that Vac8 acylation occurs early in the fusion reaction, is blocked by antibodies against Sec18 (yeast N-ethylmaleimide-sensitive fusion protein (NSF)), and is mediated by the R-SNARE Ykt6. Here we analyzed the regulation of this reaction on purified vacuoles. We show that Vac8 acylation is restricted to a narrow time window, is independent of ATP hydrolysis by Sec18, and is stimulated by the ion chelator EDTA. Analysis of vacuole protein complexes indicated that Ykt6 is part of a complex distinct from the second R-SNARE, Nyv1. We speculate that during vacuole fusion, Nyv1 is the classical R-SNARE, whereas the Ykt6-containing complex has a novel function in Vac8 palmitoylation.

Received for publication, September 14, 2004 , and in revised form, January 18, 2005.

^* This work was supported by Grant UN 111/2-3 from the Deutsche Forschungsgemeinschaft, by SFB638, the European Molecular Biology Organization Young Investigator Programme, and the Fonds der Chemischen Industrie (to C. U.), by predoctoral fellowships from the Boehringer Ingelheim Fonds (to L. E. P. D.) and the National Science Foundation Graduate Research Fellowship Program, and by a Chica & Heinz Schaller Stiftung/Deutscher Akademischer Austauschdienst University of Heidelberg Molecular and Cellular Biology Programme Fellowship (to T. J. L.). 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.

These authors contributed equally to this work.

^** Present address: California Inst. of Technology, Pasadena, CA 91125.

Present address: German University of Cairo, Al Tagamoa Al Khames, New Cairo City, Egypt.

^¶ Present address: Zentrum für Molekularbiologie Heidelberg, University of Heidelberg, Im Neuenheimer Feld 284, 69120 Heidelberg, Germany.

^|| To whom correspondence should be addressed. Tel.: 49-6221-544180; Fax: 49-6221-544366; E-mail: cu2{at}ix.urz.uni-heidelberg.de.

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