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Volumn 287, Issue 7, 2012, Pages 4426-4433

Mitochondrial disulfide relay: Redox-regulated protein import into the intermembrane space

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSOLS; INTERMEMBRANE SPACE; MATRIX PROTEINS; MITOCHONDRIAL PROTEIN; PERIPLASM; PROTEIN IMPORT; RE-OXIDATION; RESPIRATORY CHAINS; SULFHYDRYL;

EID: 84856853161     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.R111.270678     Document Type: Short Survey
Times cited : (98)

References (100)
  • 1
    • 68749112707 scopus 로고    scopus 로고
    • Importing mitochondrial proteins: Machineries and mechanisms
    • Chacinska, A., Koehler, C. M., Milenkovic, D., Lithgow, T., and Pfanner, N. (2009) Importing mitochondrial proteins: machineries and mechanisms. Cell 138, 628-644
    • (2009) Cell , vol.138 , pp. 628-644
    • Chacinska, A.1    Koehler, C.M.2    Milenkovic, D.3    Lithgow, T.4    Pfanner, N.5
  • 2
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Neupert, W., and Herrmann, J. M. (2007) Translocation of proteins into mitochondria. Annu. Rev. Biochem. 76, 723-749
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 3
    • 77953027874 scopus 로고    scopus 로고
    • Transport of proteins across or into the mitochondrial outer membrane
    • Endo, T., and Yamano, K. (2010) Transport of proteins across or into the mitochondrial outer membrane. Biochim. Biophys. Acta 1803, 706-714
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 706-714
    • Endo, T.1    Yamano, K.2
  • 6
    • 77957060561 scopus 로고    scopus 로고
    • The intermembrane space of mitochondria
    • Herrmann, J. M., and Riemer, J. (2010) The intermembrane space of mitochondria. Antioxid. Redox Signal. 13, 1341-1358
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 1341-1358
    • Herrmann, J.M.1    Riemer, J.2
  • 7
    • 73349091842 scopus 로고    scopus 로고
    • The role of mitochondria in apoptosis
    • Wang, C., and Youle, R. J. (2009) The role of mitochondria in apoptosis. Annu. Rev. Genet. 43, 95-118
    • (2009) Annu. Rev. Genet. , vol.43 , pp. 95-118
    • Wang, C.1    Youle, R.J.2
  • 9
    • 0033568154 scopus 로고    scopus 로고
    • A mutant for the yeast scERV1 gene displays a new defect in mitochondrial morphology and distribution
    • DOI 10.1002/(SICI)1097-0061(19990915)15:12<1171::AID-YEA443>3.0. CO;2-T
    • Becher, D., Kricke, J., Stein, G., and Lisowsky, T. (1999) A mutant for the yeast scERV1 gene displays a new defect in mitochondrial morphology and distribution. Yeast 15, 1171-1181 (Pubitemid 29440630)
    • (1999) Yeast , vol.15 , Issue.12 , pp. 1171-1181
    • Becher, D.1    Kricke, J.2    Stein, G.3    Lisowsky, T.4
  • 10
    • 0034647976 scopus 로고    scopus 로고
    • Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase
    • DOI 10.1016/S0014-5793(00)01767-1, PII S0014579300017671
    • Lee, J., Hofhaus, G., and Lisowsky, T. (2000) Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase. FEBS Lett. 477, 62-66 (Pubitemid 30438858)
    • (2000) FEBS Letters , vol.477 , Issue.1-2 , pp. 62-66
    • Lee, J.-E.1    Hofhaus, G.2    Lisowsky, T.3
  • 11
    • 0028318596 scopus 로고
    • ERV1 is involved in the cell division cycle and the maintenance of mitochondrial genomes in Saccharomyces cerevisiae
    • Lisowsky, T. (1994) ERV1 is involved in the cell division cycle and the maintenance of mitochondrial genomes in Saccharomyces cerevisiae. Curr. Genet. 26, 15-20
    • (1994) Curr. Genet. , vol.26 , pp. 15-20
    • Lisowsky, T.1
  • 13
    • 9144273327 scopus 로고    scopus 로고
    • Identification of Tim40 that mediates protein sorting to the mitochondrial intermembrane space
    • DOI 10.1074/jbc.M410272200
    • Naoé, M., Ohwa, Y., Ishikawa, D., Ohshima, C., Nishikawa, S., Yamamoto, H., and Endo, T. (2004) Identification of Tim40 that mediates protein sorting to the mitochondrial intermembrane space. J. Biol. Chem. 279, 47815-47821 (Pubitemid 39540931)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.46 , pp. 47815-47821
    • Naoe, M.1    Ohwa, Y.2    Ishikawa, D.3    Ohshima, C.4    Nishikawa, S.-I.5    Yamamoto, H.6    Endo, T.7
  • 14
    • 11144339526 scopus 로고    scopus 로고
    • Mia40, a novel factor for protein import into the intermembrane space of mitochondria is able to bind metal ions
    • DOI 10.1016/j.febslet.2004.11.072, PII S0014579304014681
    • Terziyska, N., Lutz, T., Kozany, C., Mokranjac, D., Mesecke, N., Neupert, W., Herrmann, J. M., and Hell, K. (2005) Mia40, a novel factor for protein import into the intermembrane space of mitochondria, is able to bind metal ions. FEBS Lett. 579, 179-184 (Pubitemid 40023393)
    • (2005) FEBS Letters , vol.579 , Issue.1 , pp. 179-184
    • Terziyska, N.1    Lutz, T.2    Kozany, C.3    Mokranjac, D.4    Mesecke, N.5    Neupert, W.6    Herrmann, J.M.7    Hell, K.8
  • 21
    • 41449101717 scopus 로고    scopus 로고
    • The Erv family of sulfhydryl oxidases
    • Fass, D. (2008) The Erv family of sulfhydryl oxidases. Biochim. Biophys. Acta 1783, 557-566
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 557-566
    • Fass, D.1
  • 22
    • 33646688670 scopus 로고    scopus 로고
    • Multidomain flavin-dependent sulfhydryl oxidases
    • DOI 10.1089/ars.2006.8.300
    • Coppock, D. L., and Thorpe, C. (2006) Multidomain flavin-dependent sulfhydryl oxidases. Antioxid. Redox Signal. 8, 300-311 (Pubitemid 43741301)
    • (2006) Antioxidants and Redox Signaling , vol.8 , Issue.3-4 , pp. 300-311
    • Coppock, D.L.1    Thorpe, C.2
  • 23
    • 0037407929 scopus 로고    scopus 로고
    • The crystal structure of augmenter of liver regeneration: A mammalian FAD-dependent sulfhydryl oxidase
    • DOI 10.1110/ps.0238103
    • Wu, C. K., Dailey, T. A., Dailey, H. A., Wang, B. C., and Rose, J. P. (2003) The crystal structure of augmenter of liver regeneration: a mammalian FAD-dependent sulfhydryl oxidase. Protein Sci. 12, 1109-1118 (Pubitemid 36505444)
    • (2003) Protein Science , vol.12 , Issue.5 , pp. 1109-1118
    • Wu, C.-K.1    Dailey, T.A.2    Dailey, H.A.3    Wang, B.-C.4    Rose, J.P.5
  • 24
    • 0036142325 scopus 로고    scopus 로고
    • A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p
    • DOI 10.1038/nsb740
    • Gross, E., Sevier, C. S., Vala, A., Kaiser, C. A., and Fass, D. (2002) A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p. Nat. Struct. Biol. 9, 61-67 (Pubitemid 34049182)
    • (2002) Nature Structural Biology , vol.9 , Issue.1 , pp. 61-67
    • Gross, E.1    Sevier, C.S.2    Vala, A.3    Kaiser, C.A.4    Fass, D.5
  • 25
    • 33747352990 scopus 로고    scopus 로고
    • Gain of function in an ERV/ALR sulfhydryl oxidase by molecular engineering of the shuttle disulfide
    • Vitu, E., Bentzur, M., Lisowsky, T., Kaiser, C. A., and Fass, D. (2006) Gain of function in an ERV/ALR sulfhydryl oxidase by molecular engineering of the shuttle disulfide. J. Mol. Biol. 362, 89-101
    • (2006) J. Mol. Biol. , vol.362 , pp. 89-101
    • Vitu, E.1    Bentzur, M.2    Lisowsky, T.3    Kaiser, C.A.4    Fass, D.5
  • 26
    • 77955265541 scopus 로고    scopus 로고
    • Structure of the human sulfhydryl oxidase augmenter of liver regeneration and characterization of a human mutation causing an autosomal recessive myopathy
    • Daithankar, V. N., Schaefer, S. A., Dong, M., Bahnson, B. J., and Thorpe, C. (2010) Structure of the human sulfhydryl oxidase augmenter of liver regeneration and characterization of a human mutation causing an autosomal recessive myopathy. Biochemistry 49, 6737-6745
    • (2010) Biochemistry , vol.49 , pp. 6737-6745
    • Daithankar, V.N.1    Schaefer, S.A.2    Dong, M.3    Bahnson, B.J.4    Thorpe, C.5
  • 27
    • 0037395242 scopus 로고    scopus 로고
    • The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centre
    • DOI 10.1046/j.1432-1033.2003.03519.x
    • Hofhaus, G., Lee, J. E., Tews, I., Rosenberg, B., and Lisowsky, T. (2003) The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox center. Eur. J. Biochem. 270, 1528-1535 (Pubitemid 36459591)
    • (2003) European Journal of Biochemistry , vol.270 , Issue.7 , pp. 1528-1535
    • Hofhaus, G.1    Lee, J.-E.2    Tews, I.3    Rosenberg, B.4    Lisowsky, T.5
  • 28
    • 70350383669 scopus 로고    scopus 로고
    • Deciphering structural and functional roles of individual disulfide bonds of the mitochondrial sulfhydryl oxidase Erv1p
    • Ang, S. K., and Lu, H. (2009) Deciphering structural and functional roles of individual disulfide bonds of the mitochondrial sulfhydryl oxidase Erv1p. J. Biol. Chem. 284, 28754-28761
    • (2009) J. Biol. Chem. , vol.284 , pp. 28754-28761
    • Ang, S.K.1    Lu, H.2
  • 30
    • 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
  • 31
    • 13444304104 scopus 로고    scopus 로고
    • Augmenter of liver regeneration: A flavin-dependent sulfhydryl oxidase with cytochrome c reductase activity
    • DOI 10.1021/bi0479555
    • Farrell, S. R., and Thorpe, C. (2005) Augmenter of liver regeneration: a flavin-dependent sulfhydryl oxidase with cytochrome c reductase activity. Biochemistry 44, 1532-1541 (Pubitemid 40204396)
    • (2005) Biochemistry , vol.44 , Issue.5 , pp. 1532-1541
    • Farrell, S.R.1    Thorpe, C.2
  • 32
    • 35948991049 scopus 로고    scopus 로고
    • The disulfide relay system of mitochondria is connected to the respiratory chain
    • DOI 10.1083/jcb.200707123
    • Bihlmaier, K., Mesecke, N., Terziyska, N., Bien, M., Hell, K., and Herrmann, J. M. (2007) The disulfide relay system of mitochondria is connected to the respiratory chain. J. Cell Biol. 179, 389-395 (Pubitemid 350074784)
    • (2007) Journal of Cell Biology , vol.179 , Issue.3 , pp. 389-395
    • Bihlmaier, K.1    Mesecke, N.2    Terziyska, N.3    Bien, M.4    Hell, K.5    Herrmann, J.M.6
  • 33
    • 36549033797 scopus 로고    scopus 로고
    • A role for cytochrome c and cytochrome c peroxidase in electron shuttling from Erv1
    • DOI 10.1038/sj.emboj.7601909, PII 7601909
    • Dabir, D. V., Leverich, E. P., Kim, S. K., Tsai, F. D., Hirasawa, M., Knaff, D. B., and Koehler, C. M. (2007) A role for cytochrome c and cytochrome c peroxidase in electron shuttling from Erv1. EMBO J. 26, 4801-4811 (Pubitemid 350191306)
    • (2007) EMBO Journal , vol.26 , Issue.23 , pp. 4801-4811
    • Dabir, D.V.1    Leverich, E.P.2    Kim, S.-K.3    Tsai, F.D.4    Hirasawa, M.5    Knaff, D.B.6    Koehler, C.M.7
  • 34
    • 27144438677 scopus 로고    scopus 로고
    • Erv1 mediates the Mia40-dependent protein import pathway and provides a functional link to the respiratory chain by shuttling electrons to cytochrome c
    • DOI 10.1016/j.jmb.2005.08.049, PII S002228360501003X
    • Allen, S., Balabanidou, V., Sideris, D. P., Lisowsky, T., and Tokatlidis, K. (2005) Erv1 mediates the Mia40-dependent protein import pathway and provides a functional link to the respiratory chain by shuttling electrons to cytochrome c. J. Mol. Biol. 353, 937-944 (Pubitemid 41503262)
    • (2005) Journal of Molecular Biology , vol.353 , Issue.5 , pp. 937-944
    • Allen, S.1    Balabanidou, V.2    Sideris, D.P.3    Lisowsky, T.4    Tokatlidis, K.5
  • 36
    • 55549107466 scopus 로고    scopus 로고
    • The zinc-binding protein Hot13 promotes oxidation of the mitochondrial import receptor Mia40
    • Mesecke, N., Bihlmaier, K., Grumbt, B., Longen, S., Terziyska, N., Hell, K., and Herrmann, J. M. (2008) The zinc-binding protein Hot13 promotes oxidation of the mitochondrial import receptor Mia40. EMBO Rep. 9, 1107-1113
    • (2008) EMBO Rep. , vol.9 , pp. 1107-1113
    • Mesecke, N.1    Bihlmaier, K.2    Grumbt, B.3    Longen, S.4    Terziyska, N.5    Hell, K.6    Herrmann, J.M.7
  • 37
    • 65449141380 scopus 로고    scopus 로고
    • Zinc can play chaperone- like and inhibitor roles during import of mitochondrial small Tim proteins
    • Morgan, B., Ang, S. K., Yan, G., and Lu, H. (2009) Zinc can play chaperone- like and inhibitor roles during import of mitochondrial small Tim proteins. J. Biol. Chem. 284, 6818-6825
    • (2009) J. Biol. Chem. , vol.284 , pp. 6818-6825
    • Morgan, B.1    Ang, S.K.2    Yan, G.3    Lu, H.4
  • 38
    • 0036200898 scopus 로고    scopus 로고
    • Genome-wide analysis of mRNAs targeted to yeast mitochondria
    • DOI 10.1093/embo-reports/kvf025
    • Marc, P., Margeot, A., Devaux, F., Blugeon, C., Corral-Debrinski, M., and Jacq, C. (2002) Genome-wide analysis of mRNAs targeted to yeast mitochondria. EMBO Rep. 3, 159-164 (Pubitemid 34213494)
    • (2002) EMBO Reports , vol.3 , Issue.2 , pp. 159-164
    • Marc, P.1    Margeot, A.2    Devaux, F.3    Blugeon, C.4    Corral-Debrinski, M.5    Jacq, C.6
  • 40
    • 79151471434 scopus 로고    scopus 로고
    • PUF proteins: Repression, activation, and mRNA localization
    • Quenault, T., Lithgow, T., and Traven, A. (2011) PUF proteins: repression, activation, and mRNA localization. Trends Cell Biol. 21, 104-112
    • (2011) Trends Cell Biol. , vol.21 , pp. 104-112
    • Quenault, T.1    Lithgow, T.2    Traven, A.3
  • 42
    • 33846446777 scopus 로고    scopus 로고
    • Puf3p, a Pumilio family RNA binding protein, localizes to mitochondria and regulates mitochondrial biogenesis and motility in budding yeast
    • DOI 10.1083/jcb.200606054
    • García-Rodríguez, L. J., Gay, A. C., and Pon, L. A. (2007) Puf3p, a Pumilio family RNA-binding protein, localizes to mitochondria and regulates mitochondrial biogenesis and motility in budding yeast. J. Cell Biol. 176, 197-207 (Pubitemid 46143260)
    • (2007) Journal of Cell Biology , vol.176 , Issue.2 , pp. 197-207
    • Garcia-Rodriguez, L.J.1    Gay, A.C.2    Pon, L.A.3
  • 43
    • 2442584610 scopus 로고    scopus 로고
    • Functional TIM10 Chaperone Assembly Is Redox-regulated in Vivo
    • DOI 10.1074/jbc.M313045200
    • Lu, H., Allen, S., Wardleworth, L., Savory, P., and Tokatlidis, K. (2004) Functional TIM10 chaperone assembly is redox-regulated in vivo. J. Biol. Chem. 279, 18952-18958 (Pubitemid 38623324)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.18 , pp. 18952-18958
    • Lu, H.1    Allen, S.2    Wardleworth, L.3    Savory, P.4    Tokatlidis, K.5
  • 44
    • 0043239359 scopus 로고    scopus 로고
    • Import of small Tim proteins into the mitochondrial intermembrane space
    • DOI 10.1093/emboj/cdg421
    • Lutz, T., Neupert, W., and Herrmann, J. M. (2003) Import of small Tim proteins into the mitochondrial intermembrane space. EMBO J. 22, 4400-4408 (Pubitemid 37087194)
    • (2003) EMBO Journal , vol.22 , Issue.17 , pp. 4400-4408
    • Lutz, T.1    Neupert, W.2    Herrmann, J.M.3
  • 45
    • 41649118619 scopus 로고    scopus 로고
    • Oxidative folding competes with mitochondrial import of the small Tim proteins
    • DOI 10.1042/BJ20071476
    • Morgan, B., and Lu, H. (2008) Oxidative folding competes with mitochondrial import of the small Tim proteins. Biochem. J. 411, 115-122 (Pubitemid 351482353)
    • (2008) Biochemical Journal , vol.411 , Issue.1 , pp. 115-122
    • Morgan, B.1    Lu, H.2
  • 46
    • 21244445718 scopus 로고    scopus 로고
    • A disulfide relay system in the intermembrane space of mitochondria that mediates protein import
    • DOI 10.1016/j.cell.2005.04.011, PII S0092867405003570
    • Mesecke, N., Terziyska, N., Kozany, C., Baumann, F., Neupert, W., Hell, K., and Herrmann, J. M. (2005) A disulfide relay system in the intermembrane space of mitochondria that mediates protein import. Cell 121, 1059-1069 (Pubitemid 40884396)
    • (2005) Cell , vol.121 , Issue.7 , 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
  • 47
    • 0036499987 scopus 로고    scopus 로고
    • The Tim9p-Tim10p complex binds to the transmembrane domains of the ADP/ATP carrier
    • DOI 10.1093/emboj/21.5.942
    • Curran, S. P., Leuenberger, D., Oppliger, W., and Koehler, C. M. (2002) The Tim9p-Tim10p complex binds to the transmembrane domains of the ADP/ATP carrier. EMBO J. 21, 942-953 (Pubitemid 34206167)
    • (2002) EMBO Journal , vol.21 , Issue.5 , pp. 942-953
    • Curran, S.P.1    Leuenberger, D.2    Oppliger, W.3    Koehler, C.M.4
  • 49
    • 77957053865 scopus 로고    scopus 로고
    • The N-terminal shuttle domain of Erv1 determines the affinity for Mia40 and mediates electron transfer to the catalytic Erv1 core in yeast mitochondria
    • Lionaki, E., Aivaliotis, M., Pozidis, C., and Tokatlidis, K. (2010) The N-terminal shuttle domain of Erv1 determines the affinity for Mia40 and mediates electron transfer to the catalytic Erv1 core in yeast mitochondria. Antioxid. Redox Signal. 13, 1327-1339
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 1327-1339
    • Lionaki, E.1    Aivaliotis, M.2    Pozidis, C.3    Tokatlidis, K.4
  • 51
    • 26844501423 scopus 로고    scopus 로고
    • Zinc binding stabilizes mitochondrial Tim10 in a reduced and import-competent state kinetically
    • DOI 10.1016/j.jmb.2005.09.002, PII S0022283605010557
    • Lu, H., and Woodburn, J. (2005) Zinc binding stabilizes mitochondrial Tim10 in a reduced and import-competent state kinetically. J. Mol. Biol. 353, 897-910 (Pubitemid 41457390)
    • (2005) Journal of Molecular Biology , vol.353 , Issue.4 , pp. 897-910
    • Lu, H.1    Woodburn, J.2
  • 56
    • 18944396823 scopus 로고    scopus 로고
    • Folding studies of Cox17 reveal an important interplay of cysteine oxidation and copper binding
    • DOI 10.1016/j.str.2005.02.015, PII S096921260500119X
    • Arnesano, F., Balatri, E., Banci, L., Bertini, I., and Winge, D. R. (2005) Folding studies of Cox17 reveal an important interplay of cysteine oxidation and copper binding. Structure 13, 713-722 (Pubitemid 40704660)
    • (2005) Structure , vol.13 , Issue.5 , pp. 713-722
    • Arnesano, F.1    Balatri, E.2    Banci, L.3    Bertini, I.4    Winge, D.R.5
  • 58
    • 29544436323 scopus 로고    scopus 로고
    • Crystal structure of the mitochondrial chaperone TIM9-10 reveals a six-bladed α-propeller
    • DOI 10.1016/j.molcel.2005.11.010, PII S1097276505017703
    • Webb, C. T., Gorman, M. A., Lazarou, M., Ryan, M. T., and Gulbis, J. M. (2006) Crystal structure of the mitochondrial chaperone TIM9-10 reveals a six-bladed α-propeller. Mol. Cell 21, 123-133 (Pubitemid 43017854)
    • (2006) Molecular Cell , vol.21 , Issue.1 , pp. 123-133
    • Webb, C.T.1    Gorman, M.A.2    Lazarou, M.3    Ryan, M.T.4    Gulbis, J.M.5
  • 60
    • 33845630817 scopus 로고    scopus 로고
    • Novel Mitochondrial Intermembrane Space Proteins as Substrates of the MIA Import Pathway
    • DOI 10.1016/j.jmb.2006.10.038, PII S0022283606014173
    • Gabriel, K., Milenkovic, D., Chacinska, A., Müller, J., Guiard, B., Pfanner, N., and Meisinger, C. (2007) Novel mitochondrial intermembrane space proteins as substrates of the MIA import pathway. J. Mol. Biol. 365, 612-620 (Pubitemid 44960363)
    • (2007) Journal of Molecular Biology , vol.365 , Issue.3 , pp. 612-620
    • Gabriel, K.1    Milenkovic, D.2    Chacinska, A.3    Muller, J.4    Guiard, B.5    Pfanner, N.6    Meisinger, C.7
  • 61
    • 7544219638 scopus 로고    scopus 로고
    • New developments in mitochondrial assembly
    • Koehler, C. M. (2004) New developments in mitochondrial assembly. Annu. Rev. Cell Dev. Biol. 20, 309-335
    • (2004) Annu. Rev. Cell Dev. Biol. , vol.20 , pp. 309-335
    • Koehler, C.M.1
  • 63
    • 1842478040 scopus 로고    scopus 로고
    • The Tim8-Tim13 Complex of Neurospora crassa Functions in the Assembly of Proteins into Both Mitochondrial Membranes
    • DOI 10.1074/jbc.M313037200
    • Hoppins, S. C., and Nargang, F. E. (2004) The Tim8-Tim13 complex of Neurospora crassa functions in the assembly of proteins into both mitochondrial membranes. J. Biol. Chem. 279, 12396-12405 (Pubitemid 38445807)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.13 , pp. 12396-12405
    • Hoppins, S.C.1    Nargang, F.E.2
  • 65
    • 0032568029 scopus 로고    scopus 로고
    • Carrier protein import into mitochondria mediated by the intermembrane proteins Tim10/Mrs11 and Tim12/Mrs5
    • DOI 10.1038/36136
    • Sirrenberg, C., Endres, M., Fölsch, H., Stuart, R. A., Neupert, W., and Brunner, M. (1998) Carrier protein import into mitochondria mediated by the intermembrane proteins Tim10/Mrs11 and Tim12/Mrs5. Nature 391, 912-915 (Pubitemid 28157671)
    • (1998) Nature , vol.391 , Issue.6670 , pp. 912-915
    • Sirrenberg, C.1    Endres, M.2    Folsch, H.3    Stuart, R.A.4    Neupert, W.5    Brunner, M.6
  • 66
    • 0037119946 scopus 로고    scopus 로고
    • The role of the Tim8p-Tim13p complex in a conserved import pathway for mitochondrial polytopic inner membrane proteins
    • Curran, S. P., Leuenberger, D., Schmidt, E., and Koehler, C. M. (2002) The role of the Tim8p-Tim13p complex in a conserved import pathway for mitochondrial polytopic inner membrane proteins. J. Cell Biol. 158, 1017-1027
    • (2002) J. Cell Biol. , vol.158 , pp. 1017-1027
    • Curran, S.P.1    Leuenberger, D.2    Schmidt, E.3    Koehler, C.M.4
  • 67
    • 51349138652 scopus 로고    scopus 로고
    • The Tim8-Tim13 complex has multiple substrate-binding sites and binds cooperatively to Tim23
    • Beverly, K. N., Sawaya, M. R., Schmid, E., and Koehler, C. M. (2008) The Tim8-Tim13 complex has multiple substrate-binding sites and binds cooperatively to Tim23. J. Mol. Biol. 382, 1144-1156
    • (2008) J. Mol. Biol. , vol.382 , pp. 1144-1156
    • Beverly, K.N.1    Sawaya, M.R.2    Schmid, E.3    Koehler, C.M.4
  • 68
    • 0036501592 scopus 로고    scopus 로고
    • Human deafness dystonia syndrome is caused by a defect in assembly of the DDP1/TIMM8a-TIMM13 complex
    • Roesch, K., Curran, S. P., Tranebjaerg, L., and Koehler, C. M. (2002) Human deafness dystonia syndrome is caused by a defect in assembly of the DDP1/TIMM8a-TIMM13 complex. Hum. Mol. Genet. 11, 477-486 (Pubitemid 34257484)
    • (2002) Human Molecular Genetics , vol.11 , Issue.5 , pp. 477-486
    • Roesch, K.1    Curran, S.P.2    Tranebjaerg, L.3    Koehler, C.M.4
  • 69
    • 0037189583 scopus 로고    scopus 로고
    • The C66W mutation in the deafness dystonia peptide 1 (DDP1) affects the formation of functional DDP1·TIM13 complexes in the mitochondrial intermembrane space
    • DOI 10.1074/jbc.M201154200
    • Hofmann, S., Rothbauer, U., Mühlenbein, N., Neupert, W., Gerbitz, K. D., Brunner, M., and Bauer, M. F. (2002) The C66W mutation in the deafness dystonia peptide 1 (DDP1) affects the formation of functional DDP1·TIM13 complexes in the mitochondrial intermembrane space. J. Biol. Chem. 277, 23287-23293 (Pubitemid 34952157)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.26 , pp. 23287-23293
    • Hofmann, S.1    Rothbauer, U.2    Muhlenbein, N.3    Neupert, W.4    Gerbitz, K.-D.5    Brunner, M.6    Bauer, M.F.7
  • 70
    • 0038518286 scopus 로고    scopus 로고
    • Assembly of cytochrome c oxidase within the mitochondrion
    • Carr, H. S., and Winge, D. R. (2003) Assembly of cytochrome c oxidase within the mitochondrion. Acc. Chem. Res. 36, 309-316
    • (2003) Acc. Chem. Res. , vol.36 , pp. 309-316
    • Carr, H.S.1    Winge, D.R.2
  • 71
    • 15844421373 scopus 로고    scopus 로고
    • Characterization of COX17, a yeast gene involved in copper metabolism and assembly of cytochrome oxidase
    • DOI 10.1074/jbc.271.24.14504
    • Glerum, D. M., Shtanko, A., and Tzagoloff, A. (1996) Characterization of COX17, a yeast gene involved in copper metabolism and assembly of cytochrome oxidase. J. Biol. Chem. 271, 14504-14509 (Pubitemid 26190352)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.24 , pp. 14504-14509
    • Moira, G.D.1    Shtanko, A.2    Tzagoloff, A.3
  • 72
    • 3843110146 scopus 로고    scopus 로고
    • COX23, a homologue of COX17, is required for cytochrome oxidase assembly
    • DOI 10.1074/jbc.M405014200
    • Barros, M. H., Johnson, A., and Tzagoloff, A. (2004) COX23, a homologue of COX17, is required for cytochrome oxidase assembly. J. Biol. Chem. 279, 31943-31947 (Pubitemid 39037868)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.30 , pp. 31943-31947
    • Barros, M.H.1    Johnson, A.2    Tzagoloff, A.3
  • 73
    • 0037174842 scopus 로고    scopus 로고
    • Characterization of COX19, a widely distributed gene required for expression of mitochondrial cytochrome oxidase
    • DOI 10.1074/jbc.M207348200
    • Nobrega, M. P., Bandeira, S. C., Beers, J., and Tzagoloff, A. (2002) Characterization of COX19, a widely distributed gene required for expression of mitochondrial cytochrome oxidase. J. Biol. Chem. 277, 40206-40211 (Pubitemid 35215590)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.43 , pp. 40206-40211
    • Nobrega, M.P.1    Bandeira, S.C.B.2    Beers, J.3    Tzagoloff, A.4
  • 74
    • 46149126408 scopus 로고    scopus 로고
    • 9C protein involved in cytochrome c oxidase biogenesis
    • DOI 10.1128/MCB.01920-07
    • Horn, D., Al-Ali, H., and Barrientos, A. (2008) Cmc1p is a conserved mitochondrial twin CX9C protein involved in cytochrome c oxidase biogenesis. Mol. Cell. Biol. 28, 4354-4364 (Pubitemid 351904957)
    • (2008) Molecular and Cellular Biology , vol.28 , Issue.13 , pp. 4354-4364
    • Horn, D.1    Al-Ali, H.2    Barrientos, A.3
  • 76
    • 77956391459 scopus 로고    scopus 로고
    • Regulation of mitochondrial phospholipids by Ups1/PRELI-like proteins depends on proteolysis and Mdm35
    • Potting, C., Wilmes, C., Engmann, T., Osman, C., and Langer, T. (2010) Regulation of mitochondrial phospholipids by Ups1/PRELI-like proteins depends on proteolysis and Mdm35. EMBO J. 29, 2888-2898
    • (2010) EMBO J. , vol.29 , pp. 2888-2898
    • Potting, C.1    Wilmes, C.2    Engmann, T.3    Osman, C.4    Langer, T.5
  • 77
    • 67449138848 scopus 로고    scopus 로고
    • Ups1p and Ups2p antagonistically regulate cardiolipin metabolism in mitochondria
    • Tamura, Y., Endo, T., Iijima, M., and Sesaki, H. (2009) Ups1p and Ups2p antagonistically regulate cardiolipin metabolism in mitochondria. J. Cell Biol. 185, 1029-1045
    • (2009) J. Cell Biol. , vol.185 , pp. 1029-1045
    • Tamura, Y.1    Endo, T.2    Iijima, M.3    Sesaki, H.4
  • 78
    • 0033804253 scopus 로고    scopus 로고
    • Som1, a third component of the yeast mitochondrial inner membrane peptidase complex that contains Imp1 and Imp2
    • Jan, P. S., Esser, K., Pratje, E., and Michaelis, G. (2000) Som1, a third component of the yeast mitochondrial inner membrane peptidase complex that contains Imp1 and Imp2. Mol. Gen. Genet. 263, 483-491
    • (2000) Mol. Gen. Genet. , vol.263 , pp. 483-491
    • Jan, P.S.1    Esser, K.2    Pratje, E.3    Michaelis, G.4
  • 79
    • 0027752461 scopus 로고
    • A mitochondrial protease with two catalytic subunits of nonoverlapping specificities
    • Nunnari, J., Fox, T. D., and Walter, P. (1993) A mitochondrial protease with two catalytic subunits of nonoverlapping specificities. Science 262, 1997-2004 (Pubitemid 24041877)
    • (1993) Science , vol.262 , Issue.5142 , pp. 1997-2004
    • Nunnari, J.1    Fox, T.D.2    Walter, P.3
  • 80
    • 0026098773 scopus 로고
    • Inner membrane protease I, an enzyme mediating intramitochondrial protein sorting in yeast
    • Schneider, A., Behrens, M., Scherer, P., Pratje, E., Michaelis, G., and Schatz, G. (1991) Inner membrane protease I, an enzyme mediating intramitochondrial protein sorting in yeast. EMBO J. 10, 247-254 (Pubitemid 21905473)
    • (1991) EMBO Journal , vol.10 , Issue.2 , pp. 247-254
    • Schneider, A.1    Behrens, M.2    Scherer, P.3    Pratje, E.4    Michaelis, G.5    Schatz, G.6
  • 81
    • 3142712428 scopus 로고    scopus 로고
    • The mitochondrial IMP peptidase of yeast: Functional analysis of domains and identification of Gut2 as a new natural substrate
    • DOI 10.1007/s00438-004-1011-y
    • Esser, K., Jan, P. S., Pratje, E., and Michaelis, G. (2004) The mitochondrial IMP peptidase of yeast: functional analysis of domains and identification of Gut2 as a new natural substrate. Mol. Genet. Genomics 271, 616-626 (Pubitemid 38916404)
    • (2004) Molecular Genetics and Genomics , vol.271 , Issue.5 , pp. 616-626
    • Esser, K.1    Jan, P.-S.2    Pratje, E.3    Michaelis, G.4
  • 82
    • 4544254450 scopus 로고    scopus 로고
    • Cargo sequences are important for Som1p-dependent signal peptide cleavage in yeast mitochondria
    • DOI 10.1074/jbc.M406915200
    • Liang, H., Luo, W., Green, N., and Fang, H. (2004) Cargo sequences are important for Som1p-dependent signal peptide cleavage in yeast mitochondria. J. Biol. Chem. 279, 39396-39400 (Pubitemid 39258203)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.38 , pp. 39396-39400
    • Liang, H.1    Luo, W.2    Green, N.3    Fang, H.4
  • 84
    • 0035851122 scopus 로고    scopus 로고
    • A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage
    • Sturtz, L. A., Diekert, K., Jensen, L. T., Lill, R., and Culotta, V. C. (2001) A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage. J. Biol. Chem. 276, 38084-38089
    • (2001) J. Biol. Chem. , vol.276 , pp. 38084-38089
    • Sturtz, L.A.1    Diekert, K.2    Jensen, L.T.3    Lill, R.4    Culotta, V.C.5
  • 85
    • 0032508609 scopus 로고    scopus 로고
    • The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase
    • DOI 10.1074/jbc.273.37.23625
    • Casareno, R. L., Waggoner, D., and Gitlin, J. D. (1998) The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase. J. Biol. Chem. 273, 23625-23628 (Pubitemid 28435686)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.37 , pp. 23625-23628
    • Casareno, R.L.B.1    Waggoner, D.2    Gitlin, J.D.3
  • 86
    • 78649699760 scopus 로고    scopus 로고
    • In yeast redistribution of Sod1 to the mitochondrial intermembrane space provides protection against respiration-derived oxidative stress
    • Klöppel, C., Michels, C., Zimmer, J., Herrmann, J. M., and Riemer, J. (2010) In yeast redistribution of Sod1 to the mitochondrial intermembrane space provides protection against respiration-derived oxidative stress. Biochem. Biophys. Res. Commun. 403, 114-119
    • (2010) Biochem. Biophys. Res. Commun. , vol.403 , pp. 114-119
    • Klöppel, C.1    Michels, C.2    Zimmer, J.3    Herrmann, J.M.4    Riemer, J.5
  • 87
    • 78650681173 scopus 로고    scopus 로고
    • SOD1 targeted to the mitochondrial intermembrane space prevents motor neuropathy in the Sod1 knockout mouse
    • Fischer, L. R., Igoudjil, A., Magrane, J., Li, Y., Hansen, J. M., Manfredi, G., and Glass, J. D. (2011) SOD1 targeted to the mitochondrial intermembrane space prevents motor neuropathy in the Sod1 knockout mouse. Brain 134, 196-209
    • (2011) Brain , vol.134 , pp. 196-209
    • Fischer, L.R.1    Igoudjil, A.2    Magrane, J.3    Li, Y.4    Hansen, J.M.5    Manfredi, G.6    Glass, J.D.7
  • 88
    • 0034878525 scopus 로고    scopus 로고
    • Heterodimeric structure of superoxide dismutase in complex with its metallochaperone
    • DOI 10.1038/nsb0901-751
    • Lamb, A. L., Torres, A. S., O'Halloran, T. V., and Rosenzweig, A. C. (2001) Heterodimeric structure of superoxide dismutase in complex with its metallochaperone. Nat. Struct. Biol. 8, 751-755 (Pubitemid 32803590)
    • (2001) Nature Structural Biology , vol.8 , Issue.9 , pp. 751-755
    • Lamb, A.L.1    Torres, A.S.2    O'Halloran, T.V.3    Rosenzweig, A.C.4
  • 89
    • 58149102066 scopus 로고    scopus 로고
    • The disulfide relay system of mitochondria is required for the biogenesis of mitochondrial Ccs1 and Sod1
    • Reddehase, S., Grumbt, B., Neupert, W., and Hell, K. (2009) The disulfide relay system of mitochondria is required for the biogenesis of mitochondrial Ccs1 and Sod1. J. Mol. Biol. 385, 331-338
    • (2009) J. Mol. Biol. , vol.385 , pp. 331-338
    • Reddehase, S.1    Grumbt, B.2    Neupert, W.3    Hell, K.4
  • 90
    • 33847726691 scopus 로고    scopus 로고
    • The sulfhydryl oxidase Erv1 is a substrate of the Mia40-dependent protein translocation pathway
    • DOI 10.1016/j.febslet.2007.02.014, PII S0014579307001597
    • Terziyska, N., Grumbt, B., Bien, M., Neupert, W., Herrmann, J. M., and Hell, K. (2007) The sulfhydryl oxidase Erv1 is a substrate of the Mia40-dependent protein translocation pathway. FEBS Lett. 581, 1098-1102 (Pubitemid 46385931)
    • (2007) FEBS Letters , vol.581 , Issue.6 , pp. 1098-1102
    • Terziyska, N.1    Grumbt, B.2    Bien, M.3    Neupert, W.4    Herrmann, J.M.5    Hell, K.6
  • 92
    • 0025884019 scopus 로고
    • 1 complex of iron-sulfur protein lacking the iron-sulfur cluster
    • Graham, L. A., and Trumpower, B. L. (1991) Mutational analysis of the mitochondrial Rieske iron-sulfur protein of Saccharomyces cerevisiae. III. Import, protease processing, and assembly into the cytochrome bc1complex of iron-sulfur protein lacking the iron-sulfur cluster. J. Biol. Chem. 266, 22485-22492 (Pubitemid 21908679)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.33 , pp. 22485-22492
    • Graham, L.A.1    Trumpower, B.L.2
  • 93
    • 0344391926 scopus 로고    scopus 로고
    • 1 Complex
    • DOI 10.1021/bi035344r
    • Merbitz-Zahradnik, T., Zwicker, K., Nett, J. H., Link, T. A., and Trumpower, B. L. (2003) Elimination of the disulfide bridge in the Rieske iron-sulfur protein allows assembly of the [2Fe-2S] cluster into the Rieske protein but damages the ubiquinol oxidation site in the cytochrome bc1complex. Biochemistry 42, 13637-13645 (Pubitemid 37444914)
    • (2003) Biochemistry , vol.42 , Issue.46 , pp. 13637-13645
    • Merbitz-Zahradnik, T.1    Zwicker, K.2    Nett, J.H.3    Link, T.A.4    Trumpower, B.L.5
  • 94
    • 0037163087 scopus 로고    scopus 로고
    • Yeast Cox11, a protein essential for cytochrome c oxidase assembly, is a Cu(I)-binding protein
    • DOI 10.1074/jbc.M204854200
    • Carr, H. S., George, G. N., and Winge, D. R. (2002) Yeast Cox11, a protein essential for cytochrome c oxidase assembly, is a Cu(I)-binding protein. J. Biol. Chem. 277, 31237-31242 (Pubitemid 34970831)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.34 , pp. 31237-31242
    • Carr, H.S.1    George, G.N.2    Winge, D.R.3
  • 95
  • 97
    • 66149139796 scopus 로고    scopus 로고
    • Human SCO2 is required for the synthesis of CO II and as a thiol-disulfide oxidoreductase for SCO1
    • Leary, S. C., Sasarman, F., Nishimura, T., and Shoubridge, E. A. (2009) Human SCO2 is required for the synthesis of CO II and as a thiol-disulfide oxidoreductase for SCO1. Hum. Mol. Genet. 18, 2230-2240
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 2230-2240
    • Leary, S.C.1    Sasarman, F.2    Nishimura, T.3    Shoubridge, E.A.4
  • 98
    • 17644415027 scopus 로고    scopus 로고
    • Crystal structure of human SCO1: Implications for redox signaling by a mitochondrial cytochrome c oxidase "assembly" protein
    • DOI 10.1074/jbc.M410705200
    • Williams, J. C., Sue, C., Banting, G. S., Yang, H., Glerum, D. M., Hendrickson, W. A., and Schon, E. A. (2005) Crystal structure of human SCO1: implications for redox signaling by a mitochondrial cytochrome c oxidase "assembly" protein. J. Biol. Chem. 280, 15202-15211 (Pubitemid 40562876)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.15 , pp. 15202-15211
    • Williams, J.C.1    Sue, C.2    Banting, G.B.3    Yang, H.4    Glerum, D.M.5    Hendrickson, W.A.6    Schon, E.A.7
  • 99
    • 77957085271 scopus 로고    scopus 로고
    • Redox regulation of SCO protein function: Controlling copper at a mitochondrial crossroad
    • Leary, S. C. (2010) Redox regulation of SCO protein function: controlling copper at a mitochondrial crossroad. Antioxid. Redox Signal. 13, 1403-1416
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 1403-1416
    • Leary, S.C.1
  • 100
    • 80054690509 scopus 로고    scopus 로고
    • Mia40-dependent oxidation of cysteines in domain I of Ccs1 controls its distribution between mitochondria and the cytosol
    • Klöppel, C., Suzuki, Y., Kojer, K., Petrungaro, C., Longen, S., Fiedler, S., Keller, S., Riemer, J. (2011) Mia40-dependent oxidation of cysteines in domain I of Ccs1 controls its distribution between mitochondria and the cytosol. Mol. Biol. Cell 22, 3749-3757
    • (2011) Mol. Biol. Cell , vol.22 , pp. 3749-3757
    • Klöppel, C.1    Suzuki, Y.2    Kojer, K.3    Petrungaro, C.4    Longen, S.5    Fiedler, S.6    Keller, S.7    Riemer, J.8


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