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Mutagenesis reveals a specific role for Cox17p in copper transport to cytochrome oxidase.

Abstract
The provision of copper to cytochrome oxidase is one of the requisite steps in the assembly of the holoenzyme. Several proteins are involved in this process including Cox17p, Sco1p, and Cox11p. Cox17p, an 8-kDa protein, is the only molecule thought to be involved in shuttling copper from the cytoplasm into mitochondria. Given the small size of Cox17p, we have taken a random and site-directed mutagenesis approach to studying structure-function relationships in Cox17p. Mutations have been generated in 70% of the Cox17p amino acid residues, with only a small subset leading to a detectable respiration-deficient phenotype. We have characterized the respiration-deficient cox17 mutants and found in addition to the expected cytochrome oxidase deficiency, a specific lack of Cox2p and the presence of a misassembled cytochrome oxidase in a subset of mutants. These results suggest that Cox17p is involved upstream of Sco1p in delivering copper specifically to subunit 2 of cytochrome oxidase and predict the existence of a subunit 1-specific copper chaperone.
AuthorsFiona A Punter, D Moira Glerum
JournalThe Journal of biological chemistry (J Biol Chem) Vol. 278 Issue 33 Pg. 30875-80 (Aug 15 2003) ISSN: 0021-9258 [Print] United States
PMID12788943 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • COX17 protein, S cerevisiae
  • Cation Transport Proteins
  • Molecular Chaperones
  • Saccharomyces cerevisiae Proteins
  • Copper
  • Electron Transport Complex IV
Topics
  • Amino Acid Sequence
  • Cation Transport Proteins (genetics, metabolism)
  • Copper (metabolism)
  • Electron Transport Complex IV (metabolism)
  • Mitochondria (metabolism)
  • Molecular Chaperones
  • Mutagenesis, Site-Directed
  • Phenotype
  • Saccharomyces cerevisiae Proteins
  • Yeasts (genetics, metabolism)

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