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Volumn 289, Issue 14, 2014, Pages 9852-9864

The mitochondrial intermembrane space oxireductase mia40 funnels the oxidative folding pathway of the cytochrome c oxidase assembly protein cox19

Author keywords

[No Author keywords available]

Indexed keywords

COVALENT BONDS; ETHANOL; PROTEINS; REACTION INTERMEDIATES;

EID: 84898060500     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.553479     Document Type: Article
Times cited : (16)

References (32)
  • 1
    • 66749163678 scopus 로고    scopus 로고
    • Disulfide formation in the ER and mitochondria: Two solutions to a common process
    • Riemer, J., Bulleid, N., and Herrmann, J. M. (2009) Disulfide formation in the ER and mitochondria: two solutions to a common process. Science 234, 1284-1287
    • (2009) Science , vol.234 , pp. 1284-1287
    • Riemer, J.1    Bulleid, N.2    Herrmann, J.M.3
  • 2
    • 70349451660 scopus 로고    scopus 로고
    • Multiple pathways for mitochondrial protein traffic
    • Endo, T., and Yamano, K. (2009) Multiple pathways for mitochondrial protein traffic. Biol. Chem. 390, 723-730
    • (2009) Biol. Chem. , vol.390 , pp. 723-730
    • Endo, T.1    Yamano, K.2
  • 3
    • 70449652177 scopus 로고    scopus 로고
    • Disulphide bond formation in the inter-membrane space of mitochondria
    • Deponte, M., and Hell, K. (2009) Disulphide bond formation in the inter-membrane space of mitochondria. J. Biochem. 146, 599-608
    • (2009) J. Biochem. , vol.146 , pp. 599-608
    • Deponte, M.1    Hell, K.2
  • 4
    • 79851512523 scopus 로고    scopus 로고
    • Oxidation-driven protein import into mitochondria: Insights and blind spots
    • Riemer, J., Fischer, M., and Herrmann, J. M. (2011) Oxidation-driven protein import into mitochondria: Insights and blind spots. Biochim. Biophys. Acta 1808, 981-989
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 981-989
    • Riemer, J.1    Fischer, M.2    Herrmann, J.M.3
  • 8
    • 21244445718 scopus 로고    scopus 로고
    • A disulfide relay system in the intermem-brane space of mitochondria that mediates protein import
    • Mesecke, N., Terziyska, N., Kozany, C., Baumann, F., Neupert, W., Hell, K., and Herrmann, J. M. (2005) A disulfide relay system in the intermem-brane space of mitochondria that mediates protein import. Cell 121, 1059-1069
    • (2005) Cell , vol.121 , pp. 1059-1069
    • Mesecke, N.1    Terziyska, N.2    Kozany, C.3    Baumann, F.4    Neupert, W.5    Hell, K.6    Herrmann, J.M.7
  • 9
    • 41449099521 scopus 로고    scopus 로고
    • The Erv1-Mia40 disulfide relay system in the intermem-brane space of mitochondria
    • Hell, K. (2008) The Erv1-Mia40 disulfide relay system in the intermem-brane space of mitochondria. Biochim. Biophys. Acta 1783, 601-609
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 601-609
    • Hell, K.1
  • 10
    • 34249849560 scopus 로고    scopus 로고
    • Characterization of the cytochrome c oxidase assembly factor Cox19 of Saccharomyces cerevisiae
    • Rigby, K., Zhang, L., Cobine, P. A., George, G. N., and Winge, D. R. (2007) Characterization of the cytochrome c oxidase assembly factor Cox19 of Saccharomyces cerevisiae. J. Biol. Chem. 282, 10233-10242
    • (2007) J. Biol. Chem. , vol.282 , pp. 10233-10242
    • Rigby, K.1    Zhang, L.2    Cobine, P.A.3    George, G.N.4    Winge, D.R.5
  • 12
    • 77149120128 scopus 로고    scopus 로고
    • Mitochondrial disulfide bond formation is driven by intersubunit electron transfer in Erv1 and proofread by glutathione
    • Bien, M., Longen, S., Wagener, N., Chwalla, I., Herrmann, J. M., and Riemer, J. (2010) Mitochondrial disulfide bond formation is driven by intersubunit electron transfer in Erv1 and proofread by glutathione. Mol. Cell 37, 516-528
    • (2010) Mol. Cell , vol.37 , pp. 516-528
    • Bien, M.1    Longen, S.2    Wagener, N.3    Chwalla, I.4    Herrmann, J.M.5    Riemer, J.6
  • 15
    • 0034992645 scopus 로고    scopus 로고
    • A method for efficient isotopic labelling of recombinant proteins
    • Marley, J., Lu, M., and Bracken, C. (2001) A method for efficient isotopic labelling of recombinant proteins. J. Biomol. NMR 20, 71-75
    • (2001) J. Biomol. NMR , vol.20 , pp. 71-75
    • Marley, J.1    Lu, M.2    Bracken, C.3
  • 16
    • 41649118619 scopus 로고    scopus 로고
    • Oxidative folding competes with mitochon-drial import of the small Tim proteins
    • Morgan, B., and Lu, H. (2008) Oxidative folding competes with mitochon-drial import of the small Tim proteins. Biochem. J. 411, 115-122
    • (2008) Biochem. J. , vol.411 , pp. 115-122
    • Morgan, B.1    Lu, H.2
  • 17
    • 33747375875 scopus 로고    scopus 로고
    • Characterizing the tick carboxypeptidase inhibitor: Molecular basis for its two-domain nature
    • Arolas, J. L., Bronsoms, S., Ventura, S., Aviles, F. X., and Calvete, J. J. (2006) Characterizing the tick carboxypeptidase inhibitor: molecular basis for its two-domain nature. J. Biol. Chem. 281, 22906-22916
    • (2006) J. Biol. Chem. , vol.281 , pp. 22906-22916
    • Arolas, J.L.1    Bronsoms, S.2    Ventura, S.3    Aviles, F.X.4    Calvete, J.J.5
  • 20
    • 41849150019 scopus 로고    scopus 로고
    • Intrinsically Disordered Proteins Display No Preference for Chaperone Binding in Vivo
    • Harrison, P., Hegyi, H., and Tompa, P. (2008) Intrinsically Disordered Proteins Display No Preference for Chaperone Binding In Vivo. PLoS Comput. Biol. 4, e1000017
    • (2008) PLoS Comput. Biol. , vol.4
    • Harrison, P.1    Hegyi, H.2    Tompa, P.3
  • 21
    • 0037154980 scopus 로고    scopus 로고
    • Protein Folding and Unfolding at Atomic Resolution
    • Fersht, A. R., and Daggett, V. (2002) Protein Folding and Unfolding at Atomic Resolution. Cell 108, 573-582
    • (2002) Cell , vol.108 , pp. 573-582
    • Fersht, A.R.1    Daggett, V.2
  • 23
    • 33646350007 scopus 로고    scopus 로고
    • Folding of small disulfide-rich proteins: Clarifying the puzzle
    • Arolas, J. L., Aviles, F. X., Chang, J.-Y., and Ventura, S. (2006) Folding of small disulfide-rich proteins: clarifying the puzzle. Trends Biochem. Sci. 31, 292-301
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 292-301
    • Arolas, J.L.1    Aviles, F.X.2    Chang, J.-Y.3    Ventura, S.4
  • 24
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart, D. S., Sykes, B. D., and Richards, F. M. (1992) The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31, 1647-1651
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 27
    • 84866091394 scopus 로고    scopus 로고
    • Role of Twin Cys-Xaa9-Cys Motif Cysteines in Mi-tochondrial Import of the Cytochrome c Oxidase Biogenesis Factor Cmc1
    • Bourens, M., Dabir, D. V., Tienson, H. L., Sorokina, I., Koehler, C. M., and Barrientos, A. (2012) Role of Twin Cys-Xaa9-Cys Motif Cysteines in Mi-tochondrial Import of the Cytochrome c Oxidase Biogenesis Factor Cmc1. J. Biol. Chem. 287, 31258-31269
    • (2012) J. Biol. Chem. , vol.287 , pp. 31258-31269
    • Bourens, M.1    Dabir, D.V.2    Tienson, H.L.3    Sorokina, I.4    Koehler, C.M.5    Barrientos, A.6
  • 28
    • 34547896606 scopus 로고    scopus 로고
    • Oxidative folding of small Tims is mediated by site-specific docking onto Mia40 in the mitochondrial inter-membrane space
    • Sideris, D. P., and Tokatlidis, K. (2007) Oxidative folding of small Tims is mediated by site-specific docking onto Mia40 in the mitochondrial inter-membrane space. Mol. Microbiol. 65, 1360-1373
    • (2007) Mol. Microbiol. , vol.65 , pp. 1360-1373
    • Sideris, D.P.1    Tokatlidis, K.2
  • 30
    • 34547929482 scopus 로고    scopus 로고
    • Biogenesis of the Essential Tim9 Tim10 Chap-erone ComplexofMitochondria: Site-specific recognitionofcysteines residues by the intermembrane space receptor Mia40
    • Milenkovic, D., Gabriel, K., Guiard, B., Schulze-Specking, A., Pfanner, N., and Chacinska, A. (2007) Biogenesis of the Essential Tim9 Tim10 Chap-erone ComplexofMitochondria: site-specific recognitionofcysteines residues by the intermembrane space receptor Mia40. J. Biol. Chem. 282, 22472-22480
    • (2007) J. Biol. Chem. , vol.282 , pp. 22472-22480
    • Milenkovic, D.1    Gabriel, K.2    Guiard, B.3    Schulze-Specking, A.4    Pfanner, N.5    Chacinska, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.