Unique features of plant mitochondrial sulfhydryl oxidase

doi:10.1074/jbc.M312877200

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Papers In Press, published online ahead of print March 2, 2004
J. Biol. Chem, 10.1074/jbc.M312877200
Submitted on November 25, 2003
Revised on March 2, 2004
Accepted on March 2, 2004

Unique features of plant mitochondrial sulfhydryl oxidase

Alexander Levitan, Avihai Danon, and Thomas Lisowsky

Department of Plant Sciences, Weizmann Institute of Science, Rehovot, Rehevot 76100

Corresponding Author: avihai.danon{at}weizmann.ac.il

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 being 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 characteristic features of the Erv1/Alr protein family, including a redox-active YPCXXC motif, non-covalently 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 carboxy-terminal domain and the absence of an amino-terminal 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.

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