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Originally published In Press as doi:10.1074/jbc.M209893200 on November 22, 2002

J. Biol. Chem., Vol. 278, Issue 6, 3770-3775, February 7, 2003
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COX16 Encodes a Novel Protein Required for the Assembly of Cytochrome Oxidase in Saccharomyces cerevisiae*

Christopher G. CarlsonDagger §, Antoni Barrientos||, Alexander Tzagoloff, and D. Moira GlerumDagger **

From the Dagger  Department of Medical Genetics, University of Alberta, Edmonton, Alberta T6G 2H7, Canada and the  Department of Biological Sciences, Columbia University, New York, New York 10027

We have characterized Cox16p, a new cytochrome oxidase (COX) assembly factor. This protein is encoded by COX16, corresponding to the previously uncharacterized open reading frame YJL003w of the yeast genome. COX16 was identified in studies of COX-deficient mutants previously assigned to complementation group G22 of a collection of yeast pet mutants. To determine its location, Cox16p was tagged with a Myc epitope at the C terminus. The fusion protein, when expressed from a low-copy plasmid, complements the mutant and is detected solely in mitochondria. Cox16p-myc is an integral component of the mitochondrial inner membrane, with its C terminus exposed to the intermembrane space. Cox16 homologues are found in both the human and murine genomes, although human COX16 does not complement the yeast mutant. Cox16p does not appear to be involved in maturation of subunit 2, copper recruitment, or heme A biosynthesis. Cox16p is thus a new protein in the growing family of eukaryotic COX assembly factors for which there are as yet no specific functions known. Like other recently described nuclear gene products involved in expression of cytochrome oxidase, COX16 is a candidate for screening in inherited human COX deficiencies.

* This work was supported by grants from the Canadian Institutes of Health Research (CIHR) (to D. M. G.) and by research Grant GM50187 from the National Institutes of Health (to A. T.)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.

§ Recipient of a Natural Sciences and Engineering Research Council PGS'A' Studentship.

|| Supported by Grant MDACU01991001 from the Muscular Dystrophy Association.

** CIHR New Investigator and an Alberta Heritage Foundation for Medical Research Scholar. To whom correspondence should be addressed: Dept. of Medical Genetics, University of Alberta, 8-33 Medical Sciences Bldg., Edmonton, AB T6G 2H7, Canada. Tel.: 780-492-4563; Fax: 780-492-1998; E-mail: moira.glerum@ualberta.ca.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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