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Papers In Press, published online ahead of print November 13, 2003
J. Biol. Chem, 10.1074/jbc.M311772200
Submitted on October 27, 2003
Revised on November 11, 2003
Accepted on November 13, 2003

Cox17 is functional when tethered to the mitochondrial inner membrane

Andrew B. Maxfield, Daren N. Heaton, and Dennis R. Winge

Department of Biochemistry and Internal Medicine, University of Utah Health Sciences Center, Salt Lake City, UT 84132-2408

Corresponding Author: dennis.winge{at}hsc.utah.edu

Cox17 is an essential protein in the assembly of cytochrome c oxidase within the mitochondrion. Cox17 is implicated in providing copper ions for formation of CuA and CuB sites in the oxidase complex. To address whether Cox17 is functional in shuttling copper ions to the mitochondrion, Cox17 was tethered to the mitochondrial inner membrane by a fusion to the transmembrane domain of the inner membrane protein, Sco2. The copper-binding domain of Sco2 that projects into the intermitochondrial membrane space (IMS) was replaced with Cox17. The Sco2/Cox17 fusion protein containing the mitochondrial import sequence and transmembrane segment of Sco2 is exclusively localized within the mitochondrion. The Sco2/Cox17 protein restores respiratory growth and normal cytochrome oxidase activity in cox17D cells. These studies suggest that Cox17’s function is confined to the mitochondrial intermembrane space. Domain mapping of yeast Cox17 reveals that the carboxyl-terminal segment of the protein has a function within the IMS that is independent of copper ion binding. The essential C-terminal function of Cox17 maps to a candidate amphipathic helix that is important for mitochondrial uptake and retention of the Cox17 protein. This motif can be spatially separated from the N-terminal copper-binding functional motif. Possible roles of the C-terminal motif are discussed.


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