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Originally published In Press as doi:10.1074/jbc.M909502199 on March 15, 2000

J. Biol. Chem., Vol. 275, Issue 21, 15955-15961, May 26, 2000
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Isa1p Is a Component of the Mitochondrial Machinery for Maturation of Cellular Iron-Sulfur Proteins and Requires Conserved Cysteine Residues for Function*

Anita Kaut, Heike Lange, Kerstin Diekert, Gyula KispalDagger , and Roland Lill§

From the Institut für Zytobiologie und Zytopathologie der Philipps-Universität Marburg, Robert-Koch-Strasse 5, 35033 Marburg, Germany

In eukaryotes, mitochondria execute a central task in the assembly of cellular iron-sulfur (Fe/S) proteins. The organelles synthesize their own set of Fe/S proteins, and they initiate the generation of extramitochondrial Fe/S proteins. In the present study, we identify the mitochondrial matrix protein Isa1p of Saccharomyces cerevisiae as a new member of the Fe/S cluster biosynthesis machinery. Isa1p belongs to a family of homologous proteins present in prokaryotes and eukaryotes. Deletion of the ISA1 gene results in the loss of mitochondrial DNA precluding the use of the Delta isa1 strain for functional analysis. Cells in which Isa1p was depleted by regulated gene expression maintained the mitochondrial DNA, yet the cells displayed retarded growth on nonfermentable carbon sources. This finding indicates the importance of Isa1p for mitochondrial function. Deficiency of Isa1p caused a defect in mitochondrial Fe/S protein assembly. Moreover, Isa1p was required for maturation of cytosolic Fe/S proteins. Two cysteine residues in a conserved sequence motif characterizing the Isa1p protein family were found to be essential for Isa1p function in the biogenesis of both intra- and extramitochondrial Fe/S proteins. Our findings suggest a function for Isa1p in the binding of iron or an intermediate of Fe/S cluster assembly.

* This work was supported by grants from the Sonderforschungsbereich 286 of the Deutsche Forschungsgemeinschaft, the Volkswagen-Stiftung, the Fonds der Chemischen Industrie, and the Alexander von Humboldt-Stiftung and by Hungarian Funds OKTA Grants T6378, T020079, and T022581.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Present address: Inst. of Biochemistry, University Medical School of Pecs, Szigeti 12, 7624 Pecs, Hungary.

§ To whom correspondence should be addressed. Tel.: 49-6421-286-6449; Fax: 49-6421-286-6414; E-mail: Lill@mailer.uni-marburg.de.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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