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J. Biol. Chem., Vol. 280, Issue 3, 1854-1863, January 21, 2005

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A Role for Pet100p in the Assembly of Yeast Cytochrome c Oxidase

INTERACTION WITH A SUBASSEMBLY THAT ACCUMULATES IN A pet100 MUTANT^*

Cynthia Church, Bradley Goehring, Daniel Forsha, Philip Wazny, and Robert O. Poyton

From the Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, Colorado 80309-0347

The biogenesis of multimeric protein complexes of the inner mitochondrial membrane in yeast requires a number of nuclear-coded ancillary proteins. One of these, Pet100p, is required for cytochrome c oxidase. Previous studies have shown that Pet100p is not required for the synthesis, processing, or targeting of cytochrome c oxidase subunits to the mitochondrion nor for heme A biosynthesis. Here, we report that Pet100p does not affect the localization of cytochrome c oxidase subunit polypeptides to the inner mitochondrial membrane but instead functions after they have arrived at the inner membrane. We have also localized Pet100p to the inner mitochondrial membrane in wild type cells, where it is present in a subassembly (Complex A) with cytochrome c oxidase subunits VII, VIIa, and VIII. Pet100p does not interact with the same subunits after they have been assembled into the holoenzyme. In addition, we have identified two subassemblies that are present in pet100 null mutant cells: one subassembly (Complex A') is composed of subunits VII, VIIa, and VIII but not Pet100p, and another subassembly (Complex B) is composed of subunits Va and VI. Because pet100 null mutant cells lack assembled cytochrome c oxidase but accumulate Complexes A' and B it appears likely that these subassemblies of cytochrome c oxidase subunits are intermediates along an assembly pathway for holocytochrome c oxidase and that Pet100p functions in this pathway to facilitate the interaction(s) between Complex A' and other cytochrome c oxidase subassemblies and subunits.

Received for publication, September 17, 2004 , and in revised form, October 21, 2004.

^* This work supported by National Institutes of Health Grant GM30228 (to R. O. P.). 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.

Present address: Metropolitan State College of Denver, Dept. of Biology, Campus Box 53, P. O. Box 173362, Denver, CO 80217-3362.

To whom correspondence should be addressed. Tel.: 303-492-3823; Fax: 303-492-7744; E-mail: Poyton{at}spot.Colorado.EDU.

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