COX17 explained

Cytochrome c oxidase copper chaperone is a protein that in humans is encoded by the COX17 gene.^{[1] [2]}

Function

Cytochrome c oxidase (COX), the terminal component of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. This component is a heteromeric complex consisting of 3 catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes. The mitochondrially-encoded subunits function in electron transfer, and the nuclear-encoded subunits may function in the regulation and assembly of the complex. This nuclear gene encodes a protein which is not a structural subunit, but may be involved in the recruitment of copper to mitochondria for incorporation into the COX apoenzyme. This protein shares 92% amino acid sequence identity with mouse and rat Cox17 proteins. This gene is no longer considered to be a candidate gene for COX deficiency. A pseudogene COX17P has been found on chromosome 13.^[2]

Further reading

• Punter FA, Adams DL, Glerum DM . Characterization and localization of human COX17, a gene involved in mitochondrial copper transport. . Hum. Genet. . 107 . 1 . 69–74 . 2000 . 10982038 . 10.1007/s004390050013 .
• Horvath R . Characterization of human SCO1 and COX17 genes in mitochondrial cytochrome-c-oxidase deficiency . Biochem. Biophys. Res. Commun. . 276 . 2 . 530–3 . 2000 . 11027508 . 10.1006/bbrc.2000.3495 . vanc. Lochmüller H . Stucka R . 3 . Yao . J . Shoubridge . EA . Kim . SH . Gerbitz . KD . Jaksch . M .
• Kako K . The expression of Cox17p in rodent tissues and cells . Eur. J. Biochem. . 267 . 22 . 6699–707 . 2000 . 11054125 . 10.1046/j.1432-1327.2000.01771.x . vanc. Tsumori K . Ohmasa Y . 3 . Takahashi . Yoshinori . Munekata . Eisuke . free.
• Heaton DN, George GN, Garrison G, Winge DR . The mitochondrial copper metallochaperone Cox17 exists as an oligomeric, polycopper complex . Biochemistry . 40 . 3 . 743–51 . 2001 . 11170391 . 10.1021/bi002315x .
• Strausberg RL . Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences . Proc. Natl. Acad. Sci. U.S.A. . 99 . 26 . 16899–903 . 2003 . 12477932 . 10.1073/pnas.242603899 . 139241 . vanc. Feingold EA . Grouse LH . 3 . Derge . JG . Klausner . RD . Collins . FS . Wagner . L . Shenmen . CM . Schuler . GD . 2002PNAS...9916899M . free .
• Suzuki C . Identification of COX17 as a therapeutic target for non-small cell lung cancer . Cancer Res. . 63 . 21 . 7038–41 . 2004 . 14612491 . vanc. Daigo Y . Kikuchi T . 3 . Katagiri . T . Nakamura . Y .
• Ota T . Complete sequencing and characterization of 21,243 full-length human cDNAs . Nat. Genet. . 36 . 1 . 40–5 . 2004 . 14702039 . 10.1038/ng1285 . vanc. Suzuki Y . Nishikawa T . 3 . Otsuki . Tetsuji . Sugiyama . Tomoyasu . Irie . Ryotaro . Wakamatsu . Ai . Hayashi . Koji . Sato . Hiroyuki . free .
• Gerhard DS . The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) . Genome Res. . 14 . 10B . 2121–7 . 2004 . 15489334 . 10.1101/gr.2596504 . 528928 . vanc. Wagner L . Feingold EA . 3 . Shenmen . CM . Grouse . LH . Schuler . G . Klein . SL . Old . S . Rasooly . R .
• Kako K . A selective requirement for copper-dependent activation of cytochrome c oxidase by Cox17p . Biochem. Biophys. Res. Commun. . 324 . 4 . 1379–85 . 2005 . 15504366 . 10.1016/j.bbrc.2004.09.211 . vanc. Takehara A . Arai H . 3 . Onodera . T . Takahashi . Y . Hanagata . H . Ogra . Y . Takagi . H . Kodama . H .
• Arnesano F . Folding studies of Cox17 reveal an important interplay of cysteine oxidation and copper binding . Structure . 13 . 5 . 713–22 . 2005 . 15893662 . 10.1016/j.str.2005.02.015 . vanc. Balatri E . Banci L . 3 . Bertini . Ivano . Winge . Dennis R. . free .
• Stelzl U . A human protein-protein interaction network: a resource for annotating the proteome . Cell . 122 . 6 . 957–68 . 2005 . 16169070 . 10.1016/j.cell.2005.08.029 . vanc. Worm U . Lalowski M . 3 . Haenig . Christian . Brembeck . Felix H. . Goehler . Heike . Stroedicke . Martin . Zenkner . Martina . Schoenherr . Anke . 11858/00-001M-0000-0010-8592-0 . 8235923 . free .
• Rual JF . Towards a proteome-scale map of the human protein-protein interaction network . Nature . 437 . 7062 . 1173–8 . 2005 . 16189514 . 10.1038/nature04209 . vanc. Venkatesan K . Hao T . 3 . Hirozane-Kishikawa . Tomoko . Dricot . Amélie . Li . Ning . Berriz . Gabriel F. . Gibbons . Francis D. . Dreze . Matija . 2005Natur.437.1173R . 4427026 .
• Cobine PA . The P174L mutation in human Sco1 severely compromises Cox17-dependent metallation but does not impair copper binding . J. Biol. Chem. . 281 . 18 . 12270–6 . 2006 . 16520371 . 10.1074/jbc.M600496200 . vanc. Pierrel F . Leary SC . 3 . Sasarman . F . Horng . YC . Shoubridge . EA . Winge . DR . 12826240 . free .
• Ma J . Identifying leukocyte gene expression patterns associated with plasma lipid levels in human subjects . Atherosclerosis . 191 . 1 . 63–72 . 2007 . 16806233 . 10.1016/j.atherosclerosis.2006.05.032 . vanc. Dempsey AA . Stamatiou D . 3 . Marshall . K . Liew . C .
• Voronova A . Cox17, a copper chaperone for cytochrome c oxidase: expression, purification, and formation of mixed disulphide adducts with thiol reagents . Protein Expr. Purif. . 53 . 1 . 138–44 . 2007 . 17208454 . 10.1016/j.pep.2006.11.014 . vanc. Kazantseva J . Tuuling M . 3 . Sokolova . Niina . Sillard . Rannar . Palumaa . Peep .
• Voronova A . Oxidative switches in functioning of mammalian copper chaperone Cox17 . Biochem. J. . 408 . 1 . 139–48 . 2007 . 17672825 . 10.1042/BJ20070804 . 2049083 . vanc. Meyer-Klaucke W . Meyer T . 3 . Rompel . Annette . Krebs . Bernt . Kazantseva . Jekaterina . Sillard . Rannar . Palumaa . Peep .

Notes and References

1. Amaravadi R, Glerum DM, Tzagoloff A . Isolation of a cDNA encoding the human homolog of COX17, a yeast gene essential for mitochondrial copper recruitment . Hum Genet . 99 . 3 . 329–33 . Mar 1997 . 9050918 . 10.1007/s004390050367 . 30340147 .
2. Web site: Entrez Gene: COX17 COX17 cytochrome c oxidase assembly homolog (S. cerevisiae).