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Published 26 September 2005. doi:10.1083/jcb.200507048
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 170, Number 7, 1091-1099
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Article

The vacuolar DHHC-CRD protein Pfa3p is a protein acyltransferase for Vac8p



Jessica E. Smotrys, Marissa J. Schoenfish, Monica A. Stutz, and Maurine E. Linder

Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110

Correspondence to M.E. Linder: mlinder{at}cellbiology.wustl.edu

Palmitoylation of the vacuolar membrane protein Vac8p is essential for vacuole fusion in yeast (Veit, M., R. Laage, L. Dietrich, L. Wang, and C. Ungermann. 2001. EMBO J. 20:3145–3155; Wang, Y.X., E.J. Kauffman, J.E. Duex, and L.S. Weisman. 2001. J. Biol. Chem. 276:35133–35140). Proteins that contain an Asp-His-His-Cys (DHHC)–cysteine rich domain (CRD) are emerging as a family of protein acyltransferases, and are therefore candidates for mediators of Vac8p palmitoylation. Here we demonstrate that the DHHC-CRD proteins Pfa3p (protein fatty acyltransferase 3, encoded by YNL326c) and Swf1p are important for vacuole fusion. Cells lacking Pfa3p had fragmented vacuoles when stressed, and cells lacking both Pfa3p and Swf1p had fragmented vacuoles under normal growth conditions. Pfa3p promoted Vac8p membrane association and palmitoylation in vivo and partially purified Pfa3p palmitoylated Vac8p in vitro, establishing Vac8p as a substrate for palmitoylation by Pfa3p. Vac8p is the first N-myristoylated, palmitoylated protein identified as a substrate for a DHHC-CRD protein.

J.E. Smotrys and M.J. Schoenfish contributed equally to this work.

Abbreviations used in this paper: DHHC-CRD, Asp-His-His-Cys cysteine-rich domain; LB, lysis buffer; myr-Vac8p, N-myristoylated Vac8p; NF, nonfluorescent media; palm-CoA, palmitoyl-CoenzymeA; PAT, protein acyltransferase; PFA, protein fatty acyltransferase; WT, wild type.


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