Purification, Characterization, and Localization of Yeast Cox17p, a Mitochondrial Copper Shuttle

Beers, John; Glerum, D. Moira; Tzagoloff, Alexander

doi:10.1074/jbc.272.52.33191

Cited by 212 publications

(180 citation statements)

References 25 publications

Supporting

Mentioning

168

Contrasting

Unclassified

Order By: Relevance

“…Residual copper binding was observed in Sco1 recovered from wild-type yeast containing chromosomally encoded Cox17. This residual copper metallation of Sco1 arises from the low, endogenous levels of Cox17 within the cytoplasm (8). Copper metallation of Sco1 was nearly abolished when purified from cells containing Cox17 tethered to the mitochondrial inner membrane.…”

Section: Discussionmentioning

confidence: 92%

“…Cox17 is a soluble protein that localizes within the IMS and also within the cytoplasm (8). The dual localization of Cox17 suggested that it served as a copper ion shuttle to the mitochondrion.…”

mentioning

confidence: 99%

“…Sco1 was first implicated in the copper delivery pathway to CcO by the observation that the respiratory-deficient phenotype of a cox17-1 strain was suppressed by overexpression of SCO1 (7). Sco1 is an integral inner membrane (IM) protein that is tethered to the IM by a single transmembrane helix and contains a globular domain, projecting into the intermembrane space (IMS) (8,9). Null sco1 cells, like cox17⌬ cells, are respiratory-deficient and have diminished CcO activity.…”

mentioning

confidence: 99%

See 2 more Smart Citations

Specific Copper Transfer from the Cox17 Metallochaperone to Both Sco1 and Cox11 in the Assembly of Yeast Cytochrome c Oxidase

Horng

Cobine

Maxfield³

et al. 2004

Journal of Biological Chemistry

278

218

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 92%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Specific Copper Transfer from the Cox17 Metallochaperone to Both Sco1 and Cox11 in the Assembly of Yeast Cytochrome c Oxidase

Horng

Cobine

Maxfield³

et al. 2004

Journal of Biological Chemistry

278

218

View full text Add to dashboard Cite

“…The major C-terminal portion of Sco1p including a CXXXCmotif, which resembles the copper binding site of Cox2p, and H 239 protrudes into the mt intermembrane space (Krummeck, 1992;Beers et al, 1997). Both cysteine residues of the CXXXC-motif, C 148 and C 152 , as well as H 239 have been shown to be essential for Sco1p function Lode et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

Molecular characterization of Saccharomyces cerevisiae Sco2p reveals a high degree of redundancy with Sco1p

Lode¹,

Paret²,

Rödel³

2002

Yeast

View full text Add to dashboard Cite

The Saccharomyces cerevisiae gene SCO1 has been shown to play an essential role in the transfer of copper to the Cu A -centre of the mitochondrial cytochrome c oxidase subunit Cox2p. By contrast, the function of Sco2p, the gene product of the highly homologous SCO2 gene, remains to be elucidated. Deletion of the SCO2 gene does not affect growth on a variety of carbon sources, including glycerol, lactate and ethanol. We report here, that Sco2p is anchored in the mitochondrial membrane by a single transmembrane segment and displays a similar tripartite structure as Sco1p. Most parts of Sco1p can be replaced by the homologous parts of Sco2p without loss of function. A short stretch of 13 amino acids, immediately adjacent to the transmembrane region, is crucial for Sco1p function and cannot be replaced by its Sco2p counterpart. We propose that this region is relevant for the correct spatial orientation of the C-terminal part of the protein. Immunoprecipitation and in vitro binding assays show that Sco2p interacts with the C-terminal portion of Cox2p. This interaction is neither dependent on bound copper ions nor on the presence of Sco1p. Furthermore we report on in vitro binding assays which show that Sco2p can form homomeric complexes, but also heteromeric complexes with Sco1p. Our data suggest that Sco2p is involved in the transfer of copper to Cox2p, but that this activity is insufficient for oxidative growth and not able to substitute for Sco1p activity.

show abstract

“…Cox17 is found in both the cytosol and mitochondria. It was originally thought that Cox 17 binds copper in the cytosol, translocates into mitochondria and delivers copper to Cox1 and Cox2 [48][49][50]. However, further studies in yeast showed that in Cox 17 deficient cells, CcO activity can be fully restored by mitochondrial restricted expression of Cox17 [51].…”

Section: Copper Metabolism In Eukaryotic Cellsmentioning

confidence: 99%

XIAP: Cell death regulation meets copper homeostasis

Mufti

Burstein

Duckett

2007

Archives of Biochemistry and Biophysics

View full text Add to dashboard Cite

Purification, Characterization, and Localization of Yeast Cox17p, a Mitochondrial Copper Shuttle

Cited by 212 publications

References 25 publications

Specific Copper Transfer from the Cox17 Metallochaperone to Both Sco1 and Cox11 in the Assembly of Yeast Cytochrome c Oxidase

Specific Copper Transfer from the Cox17 Metallochaperone to Both Sco1 and Cox11 in the Assembly of Yeast Cytochrome c Oxidase

Molecular characterization of Saccharomyces cerevisiae Sco2p reveals a high degree of redundancy with Sco1p

XIAP: Cell death regulation meets copper homeostasis

Contact Info

Product

Resources

About