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J. Biol. Chem., Vol. 279, Issue 19, 20002-20008, May 7, 2004

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Unique Features of Plant Mitochondrial Sulfhydryl Oxidase^*

Alexander Levitan, Avihai Danon, Holds the Judith and Martin Freedman Career Developmental Chair, and Thomas Lisowsky¶||

From the Department of Plant Sciences, Weizmann Institute of Science, Rehovot, 76100, Israel and the ^¶Botanisches Institut, Heinrich-Heine-Universität Düsseldorf, Universitätsstrasse 1, 40225 Düsseldorf, Germany

The yeast and human mitochondrial sulfhydryl oxidases of the Erv1/Alr family have been shown to be essential for the biogenesis of mitochondria and the cytosolic iron sulfur cluster assembly. In this study we identified a likely candidate for the first mitochondrial flavin-linked sulfhydryl oxidase of the Erv1-type from a photosynthetic organism. The central core of the plant enzyme (AtErv1) exhibits all of the characteristic features of the Erv1/Alr protein family, including a redox-active YPCXXC motif, noncovalently bound FAD, and sulfhydryl oxidase activity. Transient expression of fusion proteins of AtErv1 and the green fluorescence protein in plant protoplasts showed that the plant enzyme preferentially localizes to the mitochondria. Yet AtErv1 has several unique features, such as the presence of a CXXXXC motif in its carboxyl-terminal domain and the absence of an amino-terminally localized cysteine pair common to yeast and human Erv1/Alr proteins. In addition, the dimerization of AtErv1 is not mediated by its amino terminus but by its unique CXXXXC motif. In vitro assays with purified protein and artificial substrates demonstrate a preference of AtErv1 for dithiols with a defined space between the thiol groups, suggesting a thioredoxin-like substrate.

Received for publication, November 25, 2003 , and in revised form, February 11, 2004.

^* 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.

^|| Supported by SFB (sonderforschungsbereich) 575 and by funds from the European Commission via MitEURO Program Grant QLG1-CT-2001-00966.

Supported by Grant 651/00 from the Israel Science Foundation and a grant from the Minerva Foundation. To whom correspondence should be addressed. Tel.: 972-8934-2382; Fax: 972-8934-4181; E-mail: Avihai.Danon{at}weizmann.ac.il.

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