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J. Biol. Chem., Vol. 278, Issue 42, 41213-41220, October 17, 2003

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Candida tropicalis Expresses Two Mitochondrial 2-Enoyl Thioester Reductases That Are Able to Form Both Homodimers and Heterodimers^*

Juha M. Torkko, Kari T. Koivuranta, Alexander J. Kastaniotis, Tomi T. Airenne, Tuomo Glumoff, Mika Ilves¶, Andreas Hartig||, Aner Gurvitz||, and J. Kalervo Hiltunen**

From the Biocenter Oulu, Department of Biochemistry and the ^¶Department of Physiology, FIN-90014 University of Oulu, Finland, VTT Biotechnology, P.O.Box 1500, FIN-02044 VTT, Finland, and the ^||Max F. Perutz Laboratories, University Departments at the Vienna Biocenter, Department of Biochemistry and Molecular Cell Biology, University of Vienna, Dr. Bohr-Gasse 9, A-1030 Vienna, Austria

Here we report on the cloning of a Candida tropicalis gene, ETR2, that is closely related to ETR1. Both genes encode enzymatically active 2-enoyl thioester reductases involved in mitochondrial synthesis of fatty acids (fatty acid synthesis type II) and respiratory competence. The 5'- and 3'-flanking (coding) regions of ETR2 and ETR1 are about 90% (97%) identical, indicating that the genes have evolved via gene duplication. The gene products differ in three amino acid residues: Ile⁶⁷ (Val), Ala⁹² (Thr), and Lys²⁵¹ (Arg) in Etr2p (Etr1p). Quantitative PCR analysis and reverse transcriptase-PCR indicated that both genes were expressed about equally in fermenting and ETR1 predominantly respiring yeast cells. Like the situation with ETR1, expression of ETR2 in respiration-deficient Saccharomyces cerevisiae mutant cells devoid of Ybr026p/Etr1p was able to restore growth on glycerol. Triclosan that is used as an antibacterial agent against fatty acid synthesis type II 2-enoyl thioester reductases inhibited growth of FabI overexpressing mutant yeast cells but was not able to inhibit respiratory growth of the ETR2- or ETR1-complemented mutant yeast cells. Resolving of crystal structures obtained via Etr2p and Etr1p co-crystallization indicated that all possible dimer variants occur in the same asymmetric unit, suggesting that similar dimer formation also takes place in vivo.

Received for publication, July 16, 2003

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) U94996.

The atomic coordinates and structure factors (code IN96) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by the European Community Access to Research Infrastructure action of the Improving Human Potential Program and by grants from the Sigrid Jusélius Foundation and the Academy of Finland. 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.

^** To whom correspondence should be addressed: Dept. of Biochemistry and Biocenter Oulu, P.O. Box 3000, University of Oulu, Oulu FIN-90014, Finland. Tel.: 358-8-553-1150; Fax: 358-8-553-1141; E-mail: Kalervo.Hiltunen{at}oulu.fi.

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