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Volumn 1783, Issue 4, 2008, Pages 601-609

The Erv1-Mia40 disulfide relay system in the intermembrane space of mitochondria

Author keywords

Disulfide bond; Mitochondria; Oxidase; Protein assembly; Protein import; Protein oxidation

Indexed keywords

CYSTEINE RICH PROTEIN 61; OXIDOREDUCTASE; PROTEIN DERIVATIVE; PROTEIN MIA40; SULFHYDRYL OXIDASE ERV1; THIOL OXIDASE; UNCLASSIFIED DRUG;

EID: 41449099521     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2007.12.005     Document Type: Review
Times cited : (90)

References (98)
  • 1
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • Holmgren A. Thioredoxin and glutaredoxin systems. J. Biol. Chem. 264 (1989) 13963-13966
    • (1989) J. Biol. Chem. , vol.264 , pp. 13963-13966
    • Holmgren, A.1
  • 2
    • 0033767925 scopus 로고    scopus 로고
    • Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress
    • Carmel-Harel O., and Storz G. Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress. Annu. Rev. Microbiol. 54 (2000) 439-461
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 439-461
    • Carmel-Harel, O.1    Storz, G.2
  • 3
    • 0033025238 scopus 로고    scopus 로고
    • The thioredoxin superfamily: redundancy, specificity, and gray-area genomics
    • Aslund F., and Beckwith J. The thioredoxin superfamily: redundancy, specificity, and gray-area genomics. J. Bacteriol. 181 (1999) 1375-1379
    • (1999) J. Bacteriol. , vol.181 , pp. 1375-1379
    • Aslund, F.1    Beckwith, J.2
  • 4
  • 6
    • 0042768090 scopus 로고    scopus 로고
    • Protein disulfide bond formation in prokaryotes
    • Kadokura H., Katzen F., and Beckwith J. Protein disulfide bond formation in prokaryotes. Annu. Rev. Biochem. 72 (2003) 111-135
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 111-135
    • Kadokura, H.1    Katzen, F.2    Beckwith, J.3
  • 7
    • 8844270875 scopus 로고    scopus 로고
    • Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm
    • Nakamoto H., and Bardwell J.C. Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm. Biochim. Biophys. Acta 1694 (2004) 111-119
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 111-119
    • Nakamoto, H.1    Bardwell, J.C.2
  • 8
    • 0028341536 scopus 로고
    • Permeation of hydrophilic solutes through mitochondrial outer membranes: review on mitochondrial porins
    • Benz R. Permeation of hydrophilic solutes through mitochondrial outer membranes: review on mitochondrial porins. Biochim. Biophys. Acta 1197 (1994) 167-196
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 167-196
    • Benz, R.1
  • 11
    • 0036499987 scopus 로고    scopus 로고
    • The Tim9p-Tim10p complex binds to the transmembrane domains of the ADP/ATP carrier
    • Curran S.P., Leuenberger D., Oppliger W., and Koehler C.M. The Tim9p-Tim10p complex binds to the transmembrane domains of the ADP/ATP carrier. EMBO J. 21 (2002) 942-953
    • (2002) EMBO J. , vol.21 , pp. 942-953
    • Curran, S.P.1    Leuenberger, D.2    Oppliger, W.3    Koehler, C.M.4
  • 12
    • 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. The role of the Tim8p-Tim13p complex in a conserved import pathway for mitochondrial polytopic inner membrane proteins. J. Cell Biol. 158 (2002) 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
  • 13
    • 0041344579 scopus 로고    scopus 로고
    • Factors controlling the uptake of yeast copper/zinc superoxide dismutase into mitochondria
    • Field L.S., Furukawa Y., O'Halloran T.V., and Culotta V.C. Factors controlling the uptake of yeast copper/zinc superoxide dismutase into mitochondria. J. Biol. Chem. 278 (2003) 28052-28059
    • (2003) J. Biol. Chem. , vol.278 , pp. 28052-28059
    • Field, L.S.1    Furukawa, Y.2    O'Halloran, T.V.3    Culotta, V.C.4
  • 14
    • 21244445718 scopus 로고    scopus 로고
    • A disulfide relay system in the intermembrane space of mitochondria that mediates protein import
    • Mesecke N., Terziyska N., Kozany C., Baumann F., Neupert W., Hell K., and Herrmann J.M. A disulfide relay system in the intermembrane space of mitochondria that mediates protein import. Cell 121 (2005) 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
  • 15
    • 2442584610 scopus 로고    scopus 로고
    • Functional TIM10 chaperone assembly is redox-regulated in vivo
    • Lu H., Allen S., Wardleworth L., Savory P., and Tokatlidis K. Functional TIM10 chaperone assembly is redox-regulated in vivo. J. Biol. Chem. 279 (2004) 18952-18958
    • (2004) J. Biol. Chem. , vol.279 , pp. 18952-18958
    • Lu, H.1    Allen, S.2    Wardleworth, L.3    Savory, P.4    Tokatlidis, K.5
  • 16
    • 29544436323 scopus 로고    scopus 로고
    • Crystal structure of the mitochondrial chaperone TIM9.10 reveals a six-bladed alpha-propeller
    • Webb C.T., Gorman M.A., Lazarou M., Ryan M.T., and Gulbis J.M. Crystal structure of the mitochondrial chaperone TIM9.10 reveals a six-bladed alpha-propeller. Mol. Cell 21 (2006) 123-133
    • (2006) Mol. Cell , vol.21 , pp. 123-133
    • Webb, C.T.1    Gorman, M.A.2    Lazarou, M.3    Ryan, M.T.4    Gulbis, J.M.5
  • 17
    • 2442421175 scopus 로고    scopus 로고
    • Biogenesis of the protein import channel Tom40 of the mitochondrial outer membrane: intermembrane space components are involved in an early stage of the assembly pathway
    • Wiedemann N., Truscott K.N., Pfannschmidt S., Guiard B., Meisinger C., and Pfanner N. Biogenesis of the protein import channel Tom40 of the mitochondrial outer membrane: intermembrane space components are involved in an early stage of the assembly pathway. J. Biol. Chem. 279 (2004) 18188-18194
    • (2004) J. Biol. Chem. , vol.279 , pp. 18188-18194
    • Wiedemann, N.1    Truscott, K.N.2    Pfannschmidt, S.3    Guiard, B.4    Meisinger, C.5    Pfanner, N.6
  • 18
    • 1842478040 scopus 로고    scopus 로고
    • The Tim8-Tim13 complex of Neurospora crassa functions in the assembly of proteins into both mitochondrial membranes
    • Hoppins S.C., and Nargang F.E. The Tim8-Tim13 complex of Neurospora crassa functions in the assembly of proteins into both mitochondrial membranes. J. Biol. Chem. 279 (2004) 12396-12405
    • (2004) J. Biol. Chem. , vol.279 , pp. 12396-12405
    • Hoppins, S.C.1    Nargang, F.E.2
  • 19
    • 0032568029 scopus 로고    scopus 로고
    • Carrier protein import into mitochondria mediated by the intermembrane proteins Tim10/Mrs11 and Tim12/Mrs5
    • Sirrenberg C., Endres M., Folsch H., Stuart R.A., Neupert W., and Brunner M. Carrier protein import into mitochondria mediated by the intermembrane proteins Tim10/Mrs11 and Tim12/Mrs5. Nature 391 (1998) 912-915
    • (1998) Nature , vol.391 , pp. 912-915
    • Sirrenberg, C.1    Endres, M.2    Folsch, H.3    Stuart, R.A.4    Neupert, W.5    Brunner, M.6
  • 20
    • 0346687594 scopus 로고    scopus 로고
    • The small Tim proteins and the twin Cx(3)C motif
    • Koehler C.M. The small Tim proteins and the twin Cx(3)C motif. Trends Biochem. Sci. 29 (2004) 1-4
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 1-4
    • Koehler, C.M.1
  • 21
    • 0032536045 scopus 로고    scopus 로고
    • Import of mitochondrial carriers mediated by essential proteins of the intermembrane space
    • Koehler C.M., Jarosch E., Tokatlidis K., Schmid K., Schweyen R.J., and Schatz G. Import of mitochondrial carriers mediated by essential proteins of the intermembrane space. Science 279 (1998) 369-373
    • (1998) Science , vol.279 , pp. 369-373
    • Koehler, C.M.1    Jarosch, E.2    Tokatlidis, K.3    Schmid, K.4    Schweyen, R.J.5    Schatz, G.6
  • 22
    • 0141643287 scopus 로고    scopus 로고
    • Juxtaposition of the two distal CX3C motifs via intrachain disulfide bonding is essential for the folding of Tim10
    • Allen S., Lu H., Thornton D., and Tokatlidis K. Juxtaposition of the two distal CX3C motifs via intrachain disulfide bonding is essential for the folding of Tim10. J. Biol. Chem. 278 (2003) 38505-38513
    • (2003) J. Biol. Chem. , vol.278 , pp. 38505-38513
    • Allen, S.1    Lu, H.2    Thornton, D.3    Tokatlidis, K.4
  • 24
    • 2642554608 scopus 로고    scopus 로고
    • C2360, a nuclear protein expressed in human proliferative cytotrophoblasts, is a representative member of a novel protein family with a conserved coiled coil-helix-coiled coil-helix domain
    • Westerman B.A., Poutsma A., Steegers E.A., and Oudejans C.B. C2360, a nuclear protein expressed in human proliferative cytotrophoblasts, is a representative member of a novel protein family with a conserved coiled coil-helix-coiled coil-helix domain. Genomics 83 (2004) 1094-1104
    • (2004) Genomics , vol.83 , pp. 1094-1104
    • Westerman, B.A.1    Poutsma, A.2    Steegers, E.A.3    Oudejans, C.B.4
  • 25
    • 0031452147 scopus 로고    scopus 로고
    • Purification, characterization, and localization of yeast Cox17p, a mitochondrial copper shuttle
    • Beers J., Glerum D.M., and Tzagoloff A. Purification, characterization, and localization of yeast Cox17p, a mitochondrial copper shuttle. J. Biol. Chem. 272 (1997) 33191-33196
    • (1997) J. Biol. Chem. , vol.272 , pp. 33191-33196
    • Beers, J.1    Glerum, D.M.2    Tzagoloff, A.3
  • 26
    • 15844421373 scopus 로고    scopus 로고
    • Characterization of COX17, a yeast gene involved in copper metabolism and assembly of cytochrome oxidase
    • Glerum D.M., Shtanko A., and Tzagoloff A. 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
    • 18944396823 scopus 로고    scopus 로고
    • Folding studies of Cox17 reveal an important interplay of cysteine oxidation and copper binding
    • Arnesano F., Balatri E., Banci L., Bertini I., and Winge D.R. Folding studies of Cox17 reveal an important interplay of cysteine oxidation and copper binding. Structure 13 (2005) 713-722
    • (2005) Structure , vol.13 , pp. 713-722
    • Arnesano, F.1    Balatri, E.2    Banci, L.3    Bertini, I.4    Winge, D.R.5
  • 29
    • 3843110146 scopus 로고    scopus 로고
    • COX23, a homologue of COX17, is required for cytochrome oxidase assembly
    • Barros M.H., Johnson A., and Tzagoloff A. 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
  • 30
    • 0037174842 scopus 로고    scopus 로고
    • Characterization of COX19, a widely distributed gene required for expression of mitochondrial cytochrome oxidase
    • Nobrega M.P., Bandeira S.C., Beers J., and Tzagoloff A. 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
  • 32
    • 26244466764 scopus 로고    scopus 로고
    • Functional and mutational characterization of human MIA40 acting during import into the mitochondrial intermembrane space
    • Hofmann S., Rothbauer U., Muhlenbein N., Baiker K., Hell K., and Bauer M.F. Functional and mutational characterization of human MIA40 acting during import into the mitochondrial intermembrane space. J. Mol. Biol. 353 (2005) 517-528
    • (2005) J. Mol. Biol. , vol.353 , pp. 517-528
    • Hofmann, S.1    Rothbauer, U.2    Muhlenbein, N.3    Baiker, K.4    Hell, K.5    Bauer, M.F.6
  • 33
    • 38049132624 scopus 로고    scopus 로고
    • Functional characterization of Mia40p, the central component of the disulfide relay system of the mitochondrial intermembrane space
    • Grumbt B., Stroobant V., Terziyska N., Israel L., and Hell K. Functional characterization of Mia40p, the central component of the disulfide relay system of the mitochondrial intermembrane space. J. Biol. Chem. 282 (2007) 37461-137470
    • (2007) J. Biol. Chem. , vol.282 , pp. 37461-137470
    • Grumbt, B.1    Stroobant, V.2    Terziyska, N.3    Israel, L.4    Hell, K.5
  • 34
    • 0034660152 scopus 로고    scopus 로고
    • Structure at 2.3 A resolution of the cytochrome bc(1) complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment
    • Hunte C., Koepke J., Lange C., Rossmanith T., and Michel H. Structure at 2.3 A resolution of the cytochrome bc(1) complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment. Structure 8 (2000) 669-684
    • (2000) Structure , vol.8 , pp. 669-684
    • Hunte, C.1    Koepke, J.2    Lange, C.3    Rossmanith, T.4    Michel, H.5
  • 35
    • 18244382074 scopus 로고    scopus 로고
    • Roles of the disulfide bond and adjacent residues in determining the reduction potentials and stabilities of respiratory-type Rieske clusters
    • Leggate E.J., and Hirst J. Roles of the disulfide bond and adjacent residues in determining the reduction potentials and stabilities of respiratory-type Rieske clusters. Biochemistry 44 (2005) 7048-7058
    • (2005) Biochemistry , vol.44 , pp. 7048-7058
    • Leggate, E.J.1    Hirst, J.2
  • 36
    • 0344391926 scopus 로고    scopus 로고
    • 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 bc1 complex
    • Merbitz-Zahradnik T., Zwicker K., Nett J.H., Link T.A., and Trumpower B.L. 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 bc1 complex. Biochemistry 42 (2003) 13637-13645
    • (2003) Biochemistry , vol.42 , pp. 13637-13645
    • Merbitz-Zahradnik, T.1    Zwicker, K.2    Nett, J.H.3    Link, T.A.4    Trumpower, B.L.5
  • 37
    • 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. 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 (2001) 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
  • 38
    • 0028228085 scopus 로고
    • Conserved patterns in the Cu,Zn superoxide dismutase family
    • Bordo D., Djinovic K., and Bolognesi M. Conserved patterns in the Cu,Zn superoxide dismutase family. J. Mol. Biol. 238 (1994) 366-386
    • (1994) J. Mol. Biol. , vol.238 , pp. 366-386
    • Bordo, D.1    Djinovic, K.2    Bolognesi, M.3
  • 40
    • 0034878525 scopus 로고    scopus 로고
    • Heterodimeric structure of superoxide dismutase in complex with its metallochaperone
    • Lamb A.L., Torres A.S., O'Halloran T.V., and Rosenzweig A.C. Heterodimeric structure of superoxide dismutase in complex with its metallochaperone. Nat. Struct. Biol. 8 (2001) 751-755
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 751-755
    • Lamb, A.L.1    Torres, A.S.2    O'Halloran, T.V.3    Rosenzweig, A.C.4
  • 42
    • 0025071742 scopus 로고
    • Cytochrome oxidase assembly in yeast requires the product of COX11, a homolog of the P. denitrificans protein encoded by ORF3
    • Tzagoloff A., Capitanio N., Nobrega M.P., and Gatti D. Cytochrome oxidase assembly in yeast requires the product of COX11, a homolog of the P. denitrificans protein encoded by ORF3. EMBO J. 9 (1990) 2759-2764
    • (1990) EMBO J. , vol.9 , pp. 2759-2764
    • Tzagoloff, A.1    Capitanio, N.2    Nobrega, M.P.3    Gatti, D.4
  • 43
    • 0034614510 scopus 로고    scopus 로고
    • Cox11p is required for stable formation of the Cu(B) and magnesium centers of cytochrome c oxidase
    • Hiser L., Di Valentin M., Hamer A.G., and Hosler J.P. Cox11p is required for stable formation of the Cu(B) and magnesium centers of cytochrome c oxidase. J. Biol. Chem. 275 (2000) 619-623
    • (2000) J. Biol. Chem. , vol.275 , pp. 619-623
    • Hiser, L.1    Di Valentin, M.2    Hamer, A.G.3    Hosler, J.P.4
  • 44
    • 4544227787 scopus 로고    scopus 로고
    • Solution structure of Cox11, a novel type of beta-immunoglobulin-like fold involved in CuB site formation of cytochrome c oxidase
    • Banci L., Bertini I., Cantini F., Ciofi-Baffoni S., Gonnelli L., and Mangani S. Solution structure of Cox11, a novel type of beta-immunoglobulin-like fold involved in CuB site formation of cytochrome c oxidase. J. Biol. Chem. 279 (2004) 34833-34839
    • (2004) J. Biol. Chem. , vol.279 , pp. 34833-34839
    • Banci, L.1    Bertini, I.2    Cantini, F.3    Ciofi-Baffoni, S.4    Gonnelli, L.5    Mangani, S.6
  • 45
    • 9444296498 scopus 로고    scopus 로고
    • SCO1 and SCO2 act as high copy suppressors of a mitochondrial copper recruitment defect in Saccharomyces cerevisiae
    • Glerum D.M., Shtanko A., and Tzagoloff A. SCO1 and SCO2 act as high copy suppressors of a mitochondrial copper recruitment defect in Saccharomyces cerevisiae. J. Biol. Chem. 271 (1996) 20531-20535
    • (1996) J. Biol. Chem. , vol.271 , pp. 20531-20535
    • Glerum, D.M.1    Shtanko, A.2    Tzagoloff, A.3
  • 46
    • 0035834661 scopus 로고    scopus 로고
    • Yeast Sco1, a protein essential for cytochrome c oxidase function is a Cu(I)-binding protein
    • Nittis T., George G.N., and Winge D.R. Yeast Sco1, a protein essential for cytochrome c oxidase function is a Cu(I)-binding protein. J. Biol. Chem. 276 (2001) 42520-42526
    • (2001) J. Biol. Chem. , vol.276 , pp. 42520-42526
    • Nittis, T.1    George, G.N.2    Winge, D.R.3
  • 47
    • 0242541974 scopus 로고    scopus 로고
    • Solution structure of Sco1: a thioredoxin-like protein involved in cytochrome c oxidase assembly
    • Balatri E., Banci L., Bertini I., Cantini F., and Ciofi-Baffoni S. Solution structure of Sco1: a thioredoxin-like protein involved in cytochrome c oxidase assembly. Structure 11 (2003) 1431-1443
    • (2003) Structure , vol.11 , pp. 1431-1443
    • Balatri, E.1    Banci, L.2    Bertini, I.3    Cantini, F.4    Ciofi-Baffoni, S.5
  • 49
    • 17644415027 scopus 로고    scopus 로고
    • Crystal structure of human SCO1: implications for redox signaling by a mitochondrial cytochrome c oxidase "assembly" protein
    • Williams J.C., Sue C., Banting G.S., Yang H., Glerum D.M., Hendrickson W.A., and Schon E.A. Crystal structure of human SCO1: implications for redox signaling by a mitochondrial cytochrome c oxidase "assembly" protein. J. Biol. Chem. 280 (2005) 15202-15211
    • (2005) J. Biol. Chem. , vol.280 , pp. 15202-15211
    • Williams, J.C.1    Sue, C.2    Banting, G.S.3    Yang, H.4    Glerum, D.M.5    Hendrickson, W.A.6    Schon, E.A.7
  • 50
    • 26244464441 scopus 로고    scopus 로고
    • The essential mitochondrial protein Erv1 cooperates with Mia40 in biogenesis of intermembrane space proteins
    • Rissler M., Wiedemann N., Pfannschmidt S., Gabriel K., Guiard B., Pfanner N., and Chacinska A. The essential mitochondrial protein Erv1 cooperates with Mia40 in biogenesis of intermembrane space proteins. J. Mol. Biol. 353 (2005) 485-492
    • (2005) J. Mol. Biol. , vol.353 , pp. 485-492
    • Rissler, M.1    Wiedemann, N.2    Pfannschmidt, S.3    Gabriel, K.4    Guiard, B.5    Pfanner, N.6    Chacinska, A.7
  • 51
    • 21244497717 scopus 로고    scopus 로고
    • A disulfide relay system in mitochondria
    • Tokatlidis K. A disulfide relay system in mitochondria. Cell 121 (2005) 965-967
    • (2005) Cell , vol.121 , pp. 965-967
    • Tokatlidis, K.1
  • 52
    • 0026544596 scopus 로고
    • Dual function of a new nuclear gene for oxidative phosphorylation and vegetative growth in yeast
    • Lisowsky T. Dual function of a new nuclear gene for oxidative phosphorylation and vegetative growth in yeast. Mol. Gen. Genet. 232 (1992) 58-64
    • (1992) Mol. Gen. Genet. , vol.232 , pp. 58-64
    • Lisowsky, T.1
  • 53
    • 0034866458 scopus 로고    scopus 로고
    • An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteins
    • Lange H., Lisowsky T., Gerber J., Muhlenhoff U., Kispal G., and Lill R. An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteins. EMBO Rep. 2 (2001) 715-720
    • (2001) EMBO Rep. , vol.2 , pp. 715-720
    • Lange, H.1    Lisowsky, T.2    Gerber, J.3    Muhlenhoff, U.4    Kispal, G.5    Lill, R.6
  • 54
    • 0028318596 scopus 로고
    • ERV1 is involved in the cell-division cycle and the maintenance of mitochondrial genomes in Saccharomyces cerevisiae
    • Lisowsky T. ERV1 is involved in the cell-division cycle and the maintenance of mitochondrial genomes in Saccharomyces cerevisiae. Curr. Genet. 26 (1994) 15-20
    • (1994) Curr. Genet. , vol.26 , pp. 15-20
    • Lisowsky, T.1
  • 55
    • 0033568154 scopus 로고    scopus 로고
    • A mutant for the yeast scERV1 gene displays a new defect in mitochondrial morphology and distribution
    • Becher D., Kricke J., Stein G., and Lisowsky T. A mutant for the yeast scERV1 gene displays a new defect in mitochondrial morphology and distribution. Yeast 15 (1999) 1171-1181
    • (1999) Yeast , vol.15 , pp. 1171-1181
    • Becher, D.1    Kricke, J.2    Stein, G.3    Lisowsky, T.4
  • 57
    • 26244464441 scopus 로고    scopus 로고
    • The essential mitochondrial protein Erv1 cooperates with Mia40 in biogenesis of intermembrane space proteins
    • Rissler M., Wiedemann N., Pfannschmidt S., Gabriel K., Guiard B., Pfanner N., and Chacinska A. The essential mitochondrial protein Erv1 cooperates with Mia40 in biogenesis of intermembrane space proteins. J. Mol. Biol. 353 (2005) 485-492
    • (2005) J. Mol. Biol. , vol.353 , pp. 485-492
    • Rissler, M.1    Wiedemann, N.2    Pfannschmidt, S.3    Gabriel, K.4    Guiard, B.5    Pfanner, N.6    Chacinska, A.7
  • 58
    • 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
    • Allen S., Balabanidou V., Sideris D.P., Lisowsky T., and Tokatlidis K. 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 (2005) 937-944
    • (2005) J. Mol. Biol. , vol.353 , pp. 937-944
    • Allen, S.1    Balabanidou, V.2    Sideris, D.P.3    Lisowsky, T.4    Tokatlidis, K.5
  • 59
    • 33748178465 scopus 로고    scopus 로고
    • ALR and liver regeneration
    • Pawlowski R., and Jura J. ALR and liver regeneration. Mol. Cell. Biochem. 288 (2006) 159-169
    • (2006) Mol. Cell. Biochem. , vol.288 , pp. 159-169
    • Pawlowski, R.1    Jura, J.2
  • 60
    • 22444432755 scopus 로고    scopus 로고
    • The prokaryotic enzyme DsbB may share key structural features with eukaryotic disulfide bond forming oxidoreductases
    • Sevier C.S., Kadokura H., Tam V.C., Beckwith J., Fass D., and Kaiser C.A. The prokaryotic enzyme DsbB may share key structural features with eukaryotic disulfide bond forming oxidoreductases. Protein Sci. 14 (2005) 1630-1642
    • (2005) Protein Sci. , vol.14 , pp. 1630-1642
    • Sevier, C.S.1    Kadokura, H.2    Tam, V.C.3    Beckwith, J.4    Fass, D.5    Kaiser, C.A.6
  • 61
    • 33646688670 scopus 로고    scopus 로고
    • Multidomain flavin-dependent sulfhydryl oxidases
    • Coppock D.L., and Thorpe C. Multidomain flavin-dependent sulfhydryl oxidases. Antioxid. Redox Signal. 8 (2006) 300-311
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 300-311
    • Coppock, D.L.1    Thorpe, C.2
  • 62
    • 0035968186 scopus 로고    scopus 로고
    • Yeast ERV2p is the first microsomal FAD-linked sulfhydryl oxidase of the Erv1p/Alrp protein family
    • Gerber J., Muhlenhoff U., Hofhaus G., Lill R., and Lisowsky T. Yeast ERV2p is the first microsomal FAD-linked sulfhydryl oxidase of the Erv1p/Alrp protein family. J. Biol. Chem. 276 (2001) 23486-23491
    • (2001) J. Biol. Chem. , vol.276 , pp. 23486-23491
    • Gerber, J.1    Muhlenhoff, U.2    Hofhaus, G.3    Lill, R.4    Lisowsky, T.5
  • 63
    • 0034790475 scopus 로고    scopus 로고
    • A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation
    • Sevier C.S., Cuozzo J.W., Vala A., Aslund F., and Kaiser C.A. A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation. Nat. Cell Biol. 3 (2001) 874-882
    • (2001) Nat. Cell Biol. , vol.3 , pp. 874-882
    • Sevier, C.S.1    Cuozzo, J.W.2    Vala, A.3    Aslund, F.4    Kaiser, C.A.5
  • 64
    • 0034710899 scopus 로고    scopus 로고
    • A viral member of the ERV1/ALR protein family participates in a cytoplasmic pathway of disulfide bond formation
    • Senkevich T.G., White C.L., Koonin E.V., and Moss B. A viral member of the ERV1/ALR protein family participates in a cytoplasmic pathway of disulfide bond formation. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 12068-12073
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 12068-12073
    • Senkevich, T.G.1    White, C.L.2    Koonin, E.V.3    Moss, B.4
  • 65
    • 0036142325 scopus 로고    scopus 로고
    • A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p
    • Gross E., Sevier C.S., Vala A., Kaiser C.A., and Fass D. A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p. Nat. Struct. Biol. 9 (2002) 61-67
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 61-67
    • Gross, E.1    Sevier, C.S.2    Vala, A.3    Kaiser, C.A.4    Fass, D.5
  • 66
    • 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. Gain of function in an ERV/ALR sulfhydryl oxidase by molecular engineering of the shuttle disulfide. J. Mol. Biol. 362 (2006) 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
  • 67
    • 0037407929 scopus 로고    scopus 로고
    • The crystal structure of augmenter of liver regeneration: a mammalian FAD-dependent sulfhydryl oxidase
    • Wu C.K., Dailey T.A., Dailey H.A., Wang B.C., and Rose J.P. The crystal structure of augmenter of liver regeneration: a mammalian FAD-dependent sulfhydryl oxidase. Protein Sci. 12 (2003) 1109-1118
    • (2003) Protein Sci. , vol.12 , pp. 1109-1118
    • Wu, C.K.1    Dailey, T.A.2    Dailey, H.A.3    Wang, B.C.4    Rose, J.P.5
  • 68
    • 0034647976 scopus 로고    scopus 로고
    • Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase
    • Lee J., Hofhaus G., and Lisowsky T. Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase. FEBS Lett. 477 (2000) 62-66
    • (2000) FEBS Lett. , vol.477 , pp. 62-66
    • Lee, J.1    Hofhaus, G.2    Lisowsky, T.3
  • 69
    • 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
    • Hofhaus G., Lee J.E., Tews I., Rosenberg B., and Lisowsky T. The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centre. Eur. J. Biochem. 270 (2003) 1528-1535
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1528-1535
    • Hofhaus, G.1    Lee, J.E.2    Tews, I.3    Rosenberg, B.4    Lisowsky, T.5
  • 70
    • 0032986628 scopus 로고    scopus 로고
    • Highly divergent amino termini of the homologous human ALR and yeast scERV1 gene products define species specific differences in cellular localization
    • Hofhaus G., Stein G., Polimeno L., Francavilla A., and Lisowsky T. Highly divergent amino termini of the homologous human ALR and yeast scERV1 gene products define species specific differences in cellular localization. Eur. J. Cell Biol. 78 (1999) 349-356
    • (1999) Eur. J. Cell Biol. , vol.78 , pp. 349-356
    • Hofhaus, G.1    Stein, G.2    Polimeno, L.3    Francavilla, A.4    Lisowsky, T.5
  • 71
    • 2442567796 scopus 로고    scopus 로고
    • Unique features of plant mitochondrial sulfhydryl oxidase
    • Levitan A., Danon A., and Lisowsky T. Unique features of plant mitochondrial sulfhydryl oxidase. J. Biol. Chem. 279 (2004) 20002-20008
    • (2004) J. Biol. Chem. , vol.279 , pp. 20002-20008
    • Levitan, A.1    Danon, A.2    Lisowsky, T.3
  • 72
    • 28444436253 scopus 로고    scopus 로고
    • Structural determinants of substrate access to the disulfide oxidase Erv2p
    • Vala A., Sevier C.S., and Kaiser C.A. Structural determinants of substrate access to the disulfide oxidase Erv2p. J. Mol. Biol. 354 (2005) 952-966
    • (2005) J. Mol. Biol. , vol.354 , pp. 952-966
    • Vala, A.1    Sevier, C.S.2    Kaiser, C.A.3
  • 73
    • 13444304104 scopus 로고    scopus 로고
    • Augmenter of liver regeneration: a flavin-dependent sulfhydryl oxidase with cytochrome c reductase activity
    • Farrell S.R., and Thorpe C. Augmenter of liver regeneration: a flavin-dependent sulfhydryl oxidase with cytochrome c reductase activity. Biochemistry 44 (2005) 1532-1541
    • (2005) Biochemistry , vol.44 , pp. 1532-1541
    • Farrell, S.R.1    Thorpe, C.2
  • 74
    • 35948991049 scopus 로고    scopus 로고
    • The mitochondrial disulfide relay system is connected to the electron transport chain
    • Bihlmaier K., Mesecke N., Terzyska N., Bien M., Hell K., and Herrmann J.M. The mitochondrial disulfide relay system is connected to the electron transport chain. J. Cell Biol. 179 (2007) 389-395
    • (2007) J. Cell Biol. , vol.179 , pp. 389-395
    • Bihlmaier, K.1    Mesecke, N.2    Terzyska, N.3    Bien, M.4    Hell, K.5    Herrmann, J.M.6
  • 77
    • 9144273327 scopus 로고    scopus 로고
    • Identification of Tim40 that mediates protein sorting to the mitochondrial intermembrane space
    • Naoe M., Ohwa Y., Ishikawa D., Ohshima C., Nishikawa S., Yamamoto H., and Endo T. Identification of Tim40 that mediates protein sorting to the mitochondrial intermembrane space. J. Biol. Chem. 279 (2004) 47815-47821
    • (2004) J. Biol. Chem. , vol.279 , pp. 47815-47821
    • Naoe, M.1    Ohwa, Y.2    Ishikawa, D.3    Ohshima, C.4    Nishikawa, S.5    Yamamoto, H.6    Endo, T.7
  • 78
    • 11144339526 scopus 로고    scopus 로고
    • Mia40, a novel factor for protein import into the intermembrane space of mitochondria is able to bind metal ions
    • Terziyska N., Lutz T., Kozany C., Mokranjac D., Mesecke N., Neupert W., Herrmann J.M., and Hell K. Mia40, a novel factor for protein import into the intermembrane space of mitochondria is able to bind metal ions. FEBS Lett. 579 (2005) 179-184
    • (2005) FEBS Lett. , vol.579 , 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
  • 79
    • 7544219638 scopus 로고    scopus 로고
    • New developments in mitochondrial assembly
    • Koehler C.M. New developments in mitochondrial assembly. Annu. Rev. Cell Dev. Biol. 20 (2004) 309-335
    • (2004) Annu. Rev. Cell Dev. Biol. , vol.20 , pp. 309-335
    • Koehler, C.M.1
  • 80
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Neupert W., and Herrmann J.M. Translocation of proteins into mitochondria. Annu. Rev. Biochem. 76 (2007) 723-749
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 82
    • 0042386354 scopus 로고    scopus 로고
    • Functional cooperation and separation of translocators in protein import into mitochondria, the double-membrane bounded organelles
    • Endo T., Yamamoto H., and Esaki M. Functional cooperation and separation of translocators in protein import into mitochondria, the double-membrane bounded organelles. J. Cell Sci. 116 (2003) 3259-3267
    • (2003) J. Cell Sci. , vol.116 , pp. 3259-3267
    • Endo, T.1    Yamamoto, H.2    Esaki, M.3
  • 83
    • 16244380159 scopus 로고    scopus 로고
    • Chopped, trapped or tacked-protein translocation into the IMS of mitochondria
    • Herrmann J.M., and Hell K. Chopped, trapped or tacked-protein translocation into the IMS of mitochondria. Trends Biochem. Sci. 30 (2005) 205-211
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 205-211
    • Herrmann, J.M.1    Hell, K.2
  • 84
    • 33847365287 scopus 로고    scopus 로고
    • Catch me if you can! Oxidative protein trapping in the intermembrane space of mitochondria
    • Herrmann J.M., and Kohl R. Catch me if you can! Oxidative protein trapping in the intermembrane space of mitochondria. J. Cell Biol. 176 (2007) 559-563
    • (2007) J. Cell Biol. , vol.176 , pp. 559-563
    • Herrmann, J.M.1    Kohl, R.2
  • 85
    • 33847726691 scopus 로고    scopus 로고
    • The sulfhydryl oxidase Erv1 is a substrate of the Mia40-dependent protein translocation pathway
    • Terziyska N., Grumbt B., Bien M., Neupert W., Herrmann J.M., and Hell K. The sulfhydryl oxidase Erv1 is a substrate of the Mia40-dependent protein translocation pathway. FEBS Lett. 581 (2007) 1098-1102
    • (2007) FEBS Lett. , vol.581 , pp. 1098-1102
    • Terziyska, N.1    Grumbt, B.2    Bien, M.3    Neupert, W.4    Herrmann, J.M.5    Hell, K.6
  • 86
    • 0043239359 scopus 로고    scopus 로고
    • Import of small Tim proteins into the mitochondrial intermembrane space
    • Lutz T., Neupert W., and Herrmann J.M. Import of small Tim proteins into the mitochondrial intermembrane space. EMBO J. 22 (2003) 4400-4408
    • (2003) EMBO J. , vol.22 , pp. 4400-4408
    • Lutz, T.1    Neupert, W.2    Herrmann, J.M.3
  • 88
    • 38749148392 scopus 로고    scopus 로고
    • Precursor oxidation by Mia40 and Erv1 promotes vectorial transport of proteins into the mitochondrial intermembrane space
    • Muller J.M., Milenkovic D., Guiard B., Pfanner N., and Chacinska A. Precursor oxidation by Mia40 and Erv1 promotes vectorial transport of proteins into the mitochondrial intermembrane space. Mol. Biol. Cell 19 (2008) 226-236
    • (2008) Mol. Biol. Cell , vol.19 , pp. 226-236
    • Muller, J.M.1    Milenkovic, D.2    Guiard, B.3    Pfanner, N.4    Chacinska, A.5
  • 89
    • 26844501423 scopus 로고    scopus 로고
    • Zinc binding stabilizes mitochondrial Tim10 in a reduced and import-competent state kinetically
    • Lu H., and Woodburn J. Zinc binding stabilizes mitochondrial Tim10 in a reduced and import-competent state kinetically. J. Mol. Biol. 353 (2005) 897-910
    • (2005) J. Mol. Biol. , vol.353 , pp. 897-910
    • Lu, H.1    Woodburn, J.2
  • 90
    • 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. Human deafness dystonia syndrome is caused by a defect in assembly of the DDP1/TIMM8a-TIMM13 complex. Hum. Mol. Genet. 11 (2002) 477-486
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 477-486
    • Roesch, K.1    Curran, S.P.2    Tranebjaerg, L.3    Koehler, C.M.4
  • 91
    • 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
    • Hofmann S., Rothbauer U., Muhlenbein N., Neupert W., Gerbitz K.D., Brunner M., and Bauer M.F. 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 (2002) 23287-23293
    • (2002) J. Biol. Chem. , vol.277 , 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
  • 92
    • 34547929482 scopus 로고    scopus 로고
    • Biogenesis of the essential Tim9-Tim10 chaperone complex of mitochondria: site-specific recognition of cysteine residues by the intermembrane space receptor Mia40
    • Milenkovic D., Gabriel K., Guiard B., Schulze-Specking A., Pfanner N., and Chacinska A. Biogenesis of the essential Tim9-Tim10 chaperone complex of mitochondria: site-specific recognition of cysteine residues by the intermembrane space receptor Mia40. J. Biol. Chem. 282 (2007) 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
  • 93
    • 34547896606 scopus 로고    scopus 로고
    • Oxidative folding of small Tims is mediated by site-specific docking onto Mia40 in the mitochondrial intermembrane space
    • Sideris D.P., and Tokatlidis K. Oxidative folding of small Tims is mediated by site-specific docking onto Mia40 in the mitochondrial intermembrane space. Mol. Microbiol. 65 (2007) 1360-1373
    • (2007) Mol. Microbiol. , vol.65 , pp. 1360-1373
    • Sideris, D.P.1    Tokatlidis, K.2
  • 95
    • 0842266604 scopus 로고    scopus 로고
    • Oxidative protein folding in eukaryotes: mechanisms and consequences
    • Tu B.P., and Weissman J.S. Oxidative protein folding in eukaryotes: mechanisms and consequences. J. Cell Biol. 164 (2004) 341-346
    • (2004) J. Cell Biol. , vol.164 , pp. 341-346
    • Tu, B.P.1    Weissman, J.S.2
  • 96
    • 33745861722 scopus 로고    scopus 로고
    • Conservation and diversity of the cellular disulfide bond formation pathways
    • Sevier C.S., and Kaiser C.A. Conservation and diversity of the cellular disulfide bond formation pathways. Antioxid. Redox Signal. 8 (2006) 797-811
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 797-811
    • Sevier, C.S.1    Kaiser, C.A.2
  • 97
    • 2542475140 scopus 로고    scopus 로고
    • Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell
    • Gross E., Kastner D.B., Kaiser C.A., and Fass D. Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell. Cell 117 (2004) 601-610
    • (2004) Cell , vol.117 , pp. 601-610
    • Gross, E.1    Kastner, D.B.2    Kaiser, C.A.3    Fass, D.4
  • 98
    • 33750813327 scopus 로고    scopus 로고
    • Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation
    • Inaba K., Murakami S., Suzuki M., Nakagawa A., Yamashita E., Okada K., and Ito K. Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation. Cell 127 (2006) 789-801
    • (2006) Cell , vol.127 , pp. 789-801
    • Inaba, K.1    Murakami, S.2    Suzuki, M.3    Nakagawa, A.4    Yamashita, E.5    Okada, K.6    Ito, K.7


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