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Volumn 337, Issue 3, 2005, Pages 832-839

hCOX18 and hCOX19: Two human genes involved in cytochrome c oxidase assembly

Author keywords

COX deficiency; COX assembly genes; Cytochrome c oxidase; Metal chaperones; Mitochondria; Oxa1; Respiratory chain

Indexed keywords

CYTOCHROME C OXIDASE; GENE PRODUCT; POLYPEPTIDE; PROTEIN;

EID: 26844566827     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.09.127     Document Type: Article
Times cited : (26)

References (37)
  • 2
    • 0025145542 scopus 로고
    • PET genes of Saccharomyces cerevisiae
    • A. Tzagoloff, and C.L. Dieckmann PET genes of Saccharomyces cerevisiae Microbiol. Rev. 54 1990 211 225
    • (1990) Microbiol. Rev. , vol.54 , pp. 211-225
    • Tzagoloff, A.1    Dieckmann, C.L.2
  • 5
    • 0031044985 scopus 로고    scopus 로고
    • Molecular analysis of cytochrome c oxidase deficiency in Leigh's syndrome
    • P.L. Adams, R.N. Lightowlers, and D.M. Turnbull Molecular analysis of cytochrome c oxidase deficiency in Leigh's syndrome Ann. Neurol. 41 1997 268 270
    • (1997) Ann. Neurol. , vol.41 , pp. 268-270
    • Adams, P.L.1    Lightowlers, R.N.2    Turnbull, D.M.3
  • 6
    • 0031788095 scopus 로고    scopus 로고
    • A systematic mutation screen of 10 nuclear and 25 mitochondrial candidate genes in 21 patients with cytochrome c oxidase (COX) deficiency shows tRNA (Ser) (UCN) mutations in a subgroup with syndromal encephalopathy
    • M. Jaksch, S. Hofmann, S. Kleinle, S. Liechti-Gallati, D.E. Pongratz, J. Muller-Hocker, K.B. Jedele, T. Meitinger, and K.D. Gerbitz A systematic mutation screen of 10 nuclear and 25 mitochondrial candidate genes in 21 patients with cytochrome c oxidase (COX) deficiency shows tRNA (Ser) (UCN) mutations in a subgroup with syndromal encephalopathy J. Med. Genet. 35 1998 895 900
    • (1998) J. Med. Genet. , vol.35 , pp. 895-900
    • Jaksch, M.1    Hofmann, S.2    Kleinle, S.3    Liechti-Gallati, S.4    Pongratz, D.E.5    Muller-Hocker, J.6    Jedele, K.B.7    Meitinger, T.8    Gerbitz, K.D.9
  • 9
    • 0032534869 scopus 로고    scopus 로고
    • Identification and characterization of human cDNAs specific to BCS1, PET112, SCO1, COX15, and COX11, five genes involved in the formation and function of the mitochondrial respiratory chain
    • V. Petruzzella, V. Tiranti, P. Fernandez, P. Ianna, R. Carrozzo, and M. Zeviani Identification and characterization of human cDNAs specific to BCS1, PET112, SCO1, COX15, and COX11, five genes involved in the formation and function of the mitochondrial respiratory chain Genomics 54 1998 494 504
    • (1998) Genomics , vol.54 , pp. 494-504
    • Petruzzella, V.1    Tiranti, V.2    Fernandez, P.3    Ianna, P.4    Carrozzo, R.5    Zeviani, M.6
  • 10
    • 0034685890 scopus 로고    scopus 로고
    • Cloning and characterization of COX18, a Saccharomyces cerevisiae PET gene required for the assembly of cytochrome oxidase
    • R.L. Souza, N.S. Green-Willms, T.D. Fox, A. Tzagoloff, and F.G. Nobrega Cloning and characterization of COX18, a Saccharomyces cerevisiae PET gene required for the assembly of cytochrome oxidase J. Biol. Chem. 275 2000 14898 14902
    • (2000) J. Biol. Chem. , vol.275 , pp. 14898-14902
    • Souza, R.L.1    Green-Willms, N.S.2    Fox, T.D.3    Tzagoloff, A.4    Nobrega, F.G.5
  • 11
    • 0037174842 scopus 로고    scopus 로고
    • Characterization of COX19, a widely distributed gene required for expression of mitochondrial cytochrome oxidase
    • M.P. Nobrega, S.C. Bandeira, J. Beers, and A. Tzagoloff Characterization of COX19, a widely distributed gene required for expression of mitochondrial cytochrome oxidase J. Biol. Chem. 277 2002 40206 40211
    • (2002) J. Biol. Chem. , vol.277 , pp. 40206-40211
    • Nobrega, M.P.1    Bandeira, S.C.2    Beers, J.3    Tzagoloff, A.4
  • 12
    • 0027236280 scopus 로고
    • Information resources at the National Center for Biotechnology Information
    • R.M. Woodsmall, and D.A. Benson Information resources at the National Center for Biotechnology Information Bull. Med. Libr. Assoc. 81 1993 282 284
    • (1993) Bull. Med. Libr. Assoc. , vol.81 , pp. 282-284
    • Woodsmall, R.M.1    Benson, D.A.2
  • 13
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • F. Corpet Multiple sequence alignment with hierarchical clustering Nucleic Acids Res. 16 1988 10881 10890
    • (1988) Nucleic Acids Res. , vol.16 , pp. 10881-10890
    • Corpet, F.1
  • 14
    • 2942589051 scopus 로고    scopus 로고
    • Predotar: A tool for rapidly screening proteomes for N-terminal targeting sequences
    • I. Small, N. Peeters, F. Legeai, and C. Lurin Predotar: a tool for rapidly screening proteomes for N-terminal targeting sequences Proteomics 4 2004 1581 1590
    • (2004) Proteomics , vol.4 , pp. 1581-1590
    • Small, I.1    Peeters, N.2    Legeai, F.3    Lurin, C.4
  • 15
    • 0032972509 scopus 로고    scopus 로고
    • PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization
    • K. Nakai, and P. Horton PSORT: a program for detecting sorting signals in proteins and predicting their subcellular localization Trends Biochem. Sci. 24 1999 34 36
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 34-36
    • Nakai, K.1    Horton, P.2
  • 16
    • 0029915525 scopus 로고    scopus 로고
    • Computational method to predict mitochondrially imported proteins and their targeting sequences
    • M.G. Claros, and P. Vincens Computational method to predict mitochondrially imported proteins and their targeting sequences Eur. J. Biochem. 241 1996 779 786
    • (1996) Eur. J. Biochem. , vol.241 , pp. 779-786
    • Claros, M.G.1    Vincens, P.2
  • 17
    • 18144423143 scopus 로고    scopus 로고
    • Membrane topology mapping of vitamin k epoxide reductase by in vitro translation/cotranslocation
    • J.K. Tie, C. Nicchitta, G. von Heijne, and D.W. Stafford Membrane topology mapping of vitamin k epoxide reductase by in vitro translation/ cotranslocation J. Biol. Chem. 280 2005 16410 16416
    • (2005) J. Biol. Chem. , vol.280 , pp. 16410-16416
    • Tie, J.K.1    Nicchitta, C.2    Von Heijne, G.3    Stafford, D.W.4
  • 18
    • 0032822836 scopus 로고    scopus 로고
    • GeneBuilder: Interactive in silico prediction of gene structure
    • L. Milanesi, D. D'Angelo, and I.B. Rogozin GeneBuilder: interactive in silico prediction of gene structure Bioinformatics 15 1999 612 621
    • (1999) Bioinformatics , vol.15 , pp. 612-621
    • Milanesi, L.1    D'Angelo, D.2    Rogozin, I.B.3
  • 20
    • 0034523499 scopus 로고    scopus 로고
    • MaskerAid: A performance enhancement to RepeatMasker
    • J.A. Bedell, I. Korf, and W. Gish MaskerAid: a performance enhancement to RepeatMasker Bioinformatics 16 2000 1040 1041
    • (2000) Bioinformatics , vol.16 , pp. 1040-1041
    • Bedell, J.A.1    Korf, I.2    Gish, W.3
  • 21
    • 0035853721 scopus 로고    scopus 로고
    • The mitochondrial permeability transition, release of cytochrome c and cell death. Correlation with the duration of pore openings in situ
    • V. Petronilli, D. Penzo, L. Scorrano, P. Bernardi, and F. Di Lisa The mitochondrial permeability transition, release of cytochrome c and cell death. Correlation with the duration of pore openings in situ J. Biol. Chem. 276 2001 12030 12034
    • (2001) J. Biol. Chem. , vol.276 , pp. 12030-12034
    • Petronilli, V.1    Penzo, D.2    Scorrano, L.3    Bernardi, P.4    Di Lisa, F.5
  • 23
    • 16844375031 scopus 로고    scopus 로고
    • Evolution of mitochondrial oxa proteins from bacterial YidC. Inherited and acquired functions of a conserved protein insertion machinery
    • M. Preuss, M. Ott, S. Funes, J. Luirink, and J.M. Herrmann Evolution of mitochondrial oxa proteins from bacterial YidC. Inherited and acquired functions of a conserved protein insertion machinery J. Biol. Chem. 280 2005 13004 13011
    • (2005) J. Biol. Chem. , vol.280 , pp. 13004-13011
    • Preuss, M.1    Ott, M.2    Funes, S.3    Luirink, J.4    Herrmann, J.M.5
  • 24
    • 0030908894 scopus 로고    scopus 로고
    • Insertion into the mitochondrial inner membrane of a polytopic protein, the nuclear-encoded Oxa1p
    • J.M. Herrmann, W. Neupert, and R.A. Stuart Insertion into the mitochondrial inner membrane of a polytopic protein, the nuclear-encoded Oxa1p EMBO J. 16 1997 2217 2226
    • (1997) EMBO J. , vol.16 , pp. 2217-2226
    • Herrmann, J.M.1    Neupert, W.2    Stuart, R.A.3
  • 25
    • 15844421373 scopus 로고    scopus 로고
    • Characterization of COX17, a yeast gene involved in copper metabolism and assembly of cytochrome oxidase
    • D.M. Glerum, A. Shtanko, and A. Tzagoloff Characterization of COX17, a yeast gene involved in copper metabolism and assembly of cytochrome oxidase J. Biol. Chem. 271 1996 14504 14509
    • (1996) J. Biol. Chem. , vol.271 , pp. 14504-14509
    • Glerum, D.M.1    Shtanko, A.2    Tzagoloff, A.3
  • 27
    • 0347157958 scopus 로고    scopus 로고
    • The Alb3/Oxa1/YidC protein family: Membrane-localized chaperones facilitating membrane protein insertion?
    • A. Kuhn, R. Stuart, R. Henry, and R.E. Dalbey The Alb3/Oxa1/YidC protein family: membrane-localized chaperones facilitating membrane protein insertion? Trends Cell Biol. 13 2003 510 516
    • (2003) Trends Cell Biol. , vol.13 , pp. 510-516
    • Kuhn, A.1    Stuart, R.2    Henry, R.3    Dalbey, R.E.4
  • 28
    • 0348136787 scopus 로고    scopus 로고
    • Yeast Oxa1 interacts with mitochondrial ribosomes: The importance of the C-terminal region of Oxa1
    • L. Jia, M. Dienhart, M. Schramp, M. McCauley, K. Hell, and R.A. Stuart Yeast Oxa1 interacts with mitochondrial ribosomes: the importance of the C-terminal region of Oxa1 EMBO J. 22 2003 6438 6447
    • (2003) EMBO J. , vol.22 , pp. 6438-6447
    • Jia, L.1    Dienhart, M.2    Schramp, M.3    McCauley, M.4    Hell, K.5    Stuart, R.A.6
  • 29
    • 0345732691 scopus 로고    scopus 로고
    • Ribosome binding to the Oxa1 complex facilitates co-translational protein insertion in mitochondria
    • G. Szyrach, M. Ott, N. Bonnefoy, W. Neupert, and J.M. Herrmann Ribosome binding to the Oxa1 complex facilitates co-translational protein insertion in mitochondria EMBO J. 22 2003 6448 6457
    • (2003) EMBO J. , vol.22 , pp. 6448-6457
    • Szyrach, G.1    Ott, M.2    Bonnefoy, N.3    Neupert, W.4    Herrmann, J.M.5
  • 30
    • 0032515148 scopus 로고    scopus 로고
    • Membrane topology of the 60-kDa Oxa1p homologue from Escherichia coli
    • A. Saaf, M. Monne, J.W. de Gier, and G. von Heijne Membrane topology of the 60-kDa Oxa1p homologue from Escherichia coli J. Biol. Chem. 273 1998 30415 30418
    • (1998) J. Biol. Chem. , vol.273 , pp. 30415-30418
    • Saaf, A.1    Monne, M.2    De Gier, J.W.3    Von Heijne, G.4
  • 31
    • 0024442722 scopus 로고
    • Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues
    • G. von Heijne Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues Nature 341 1989 456 458
    • (1989) Nature , vol.341 , pp. 456-458
    • Von Heijne, G.1
  • 32
    • 0025059797 scopus 로고
    • The role of charged amino acids in the localization of secreted and membrane proteins
    • D. Boyd, and J. Beckwith The role of charged amino acids in the localization of secreted and membrane proteins Cell 62 1990 1031 1033
    • (1990) Cell , vol.62 , pp. 1031-1033
    • Boyd, D.1    Beckwith, J.2
  • 33
    • 0036223216 scopus 로고    scopus 로고
    • Cox18p is required for export of the mitochondrially encoded Saccharomyces cerevisiae Cox2p C-tail and interacts with Pnt1p and Mss2p in the inner membrane
    • S.A. Saracco, and T.D. Fox Cox18p is required for export of the mitochondrially encoded Saccharomyces cerevisiae Cox2p C-tail and interacts with Pnt1p and Mss2p in the inner membrane Mol. Biol. Cell 13 2002 1122 1131
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1122-1131
    • Saracco, S.A.1    Fox, T.D.2
  • 34
    • 1542677273 scopus 로고    scopus 로고
    • Initiation of transcription of the MUC3A human intestinal mucin from a TATA-less promoter and comparison with the MUC3B amino terminus
    • J.R. Gum Jr., J.W. Hicks, S.C. Crawley, C.M. Dahl, S.C. Yang, A.M. Roberton, and Y.S. Kim Initiation of transcription of the MUC3A human intestinal mucin from a TATA-less promoter and comparison with the MUC3B amino terminus J. Biol. Chem. 278 2003 49600 49609
    • (2003) J. Biol. Chem. , vol.278 , pp. 49600-49609
    • Gum Jr., J.R.1    Hicks, J.W.2    Crawley, S.C.3    Dahl, C.M.4    Yang, S.C.5    Roberton, A.M.6    Kim, Y.S.7
  • 36
    • 3843110146 scopus 로고    scopus 로고
    • COX23, a homologue of COX17, is required for cytochrome oxidase assembly
    • M.H. Barros, A. Johnson, and A. Tzagoloff COX23, a homologue of COX17, is required for cytochrome oxidase assembly J. Biol. Chem. 279 2004 31943 31947
    • (2004) J. Biol. Chem. , vol.279 , pp. 31943-31947
    • Barros, M.H.1    Johnson, A.2    Tzagoloff, A.3
  • 37
    • 4143074731 scopus 로고    scopus 로고
    • Specific copper transfer from the Cox17 metallochaperone to both Sco1 and Cox11 in the assembly of yeast cytochrome c oxidase
    • Y.C. Horng, P.A. Cobine, A.B. Maxfield, H.S. Carr, and D.R. Winge Specific copper transfer from the Cox17 metallochaperone to both Sco1 and Cox11 in the assembly of yeast cytochrome c oxidase J. Biol. Chem. 279 2004 35334 35340
    • (2004) J. Biol. Chem. , vol.279 , pp. 35334-35340
    • Horng, Y.C.1    Cobine, P.A.2    Maxfield, A.B.3    Carr, H.S.4    Winge, D.R.5


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