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Molecular and Cellular Biology, January 2001, p. 109-125, Vol. 21, No. 1
0270-7306/01/$04.00+0 DOI: 10.1128/MCB.21.1.109-125.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Tsc13p Is Required for Fatty Acid Elongation and Localizes to a Novel Structure at the Nuclear-Vacuolar Interface in Saccharomyces cerevisiae

Sepp D. Kohlwein,1 Sandra Eder,1 Chan-Seok Oh,2 Charles E. Martin,2 Ken Gable,3 Dagmar Bacikova,3 and Teresa Dunn3,*

SFB Biomembrane Research Center, Department of Biochemistry, Technical University Graz, A8010 Graz, Austria1; Division of Life Sciences, Bureau of Biological Research, Rutgers University, Piscataway, New Jersey 08854-80822; and Department of Biochemistry, Uniformed Services University of the Health Sciences, Bethesda, Maryland 208143

Received 8 August 2000/Returned for modification 13 September 2000/Accepted 3 October 2000

The TSC13/YDL015c gene was identified in a screen for suppressors of the calcium sensitivity of csg2Delta mutants that are defective in sphingolipid synthesis. The fatty acid moiety of sphingolipids in Saccharomyces cerevisiae is a very long chain fatty acid (VLCFA) that is synthesized by a microsomal enzyme system that lengthens the palmitate produced by cytosolic fatty acid synthase by two carbon units in each cycle of elongation. The TSC13 gene encodes a protein required for elongation, possibly the enoyl reductase that catalyzes the last step in each cycle of elongation. The tsc13 mutant accumulates high levels of long-chain bases as well as ceramides that harbor fatty acids with chain lengths shorter than 26 carbons. These phenotypes are exacerbated by the deletion of either the ELO2 or ELO3 gene, both of which have previously been shown to be required for VLCFA synthesis. Compromising the synthesis of malonyl coenzyme A (malonyl-CoA) by inactivating acetyl-CoA carboxylase in a tsc13 mutant is lethal, further supporting a role of Tsc13p in VLCFA synthesis. Tsc13p coimmunoprecipitates with Elo2p and Elo3p, suggesting that the elongating proteins are organized in a complex. Tsc13p localizes to the endoplasmic reticulum and is highly enriched in a novel structure marking nuclear-vacuolar junctions.

* Corresponding author. Mailing address: Department of Biochemistry, Uniformed Services University of the Health Sciences, 4301 Jones Bridge Road, Bethesda, MD 20814. Phone: (301) 295-3592. Fax: (301) 295-3512. E-mail: tdunn{at}usuhs.mil.

Molecular and Cellular Biology, January 2001, p. 109-125, Vol. 21, No. 1
0270-7306/01/$04.00+0 DOI: 10.1128/MCB.21.1.109-125.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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