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Volumn 365, Issue 3, 2007, Pages 612-620

Novel Mitochondrial Intermembrane Space Proteins as Substrates of the MIA Import Pathway

Author keywords

Erv1; intermembrane space; mitochondria; protein sorting; Saccharomyces cerevisiae

Indexed keywords

CARRIER PROTEIN; CELL PROTEIN; CYSTEINE; MEMBRANE PROTEIN; MITOCHONDRIAL PROTEIN; PROTEIN ERV1; PROTEIN MDM35; PROTEIN MIA40; PROTEIN MIC14; PROTEIN MIC17; PROTEIN SUBUNIT; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 33845630817     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.10.038     Document Type: Article
Times cited : (134)

References (48)
  • 1
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Neupert W. Protein import into mitochondria. Annu. Rev. Biochem. 66 (1997) 863-917
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 863-917
    • Neupert, W.1
  • 2
    • 33746575844 scopus 로고    scopus 로고
    • Evolution of the molecular machines for protein import into mitochondria
    • Dolezal P., Likic V., Tachezy J., and Lithgow T. Evolution of the molecular machines for protein import into mitochondria. Science 313 (2006) 314-318
    • (2006) Science , vol.313 , pp. 314-318
    • Dolezal, P.1    Likic, V.2    Tachezy, J.3    Lithgow, T.4
  • 3
    • 0037009108 scopus 로고    scopus 로고
    • Import and assembly of proteins into mitochondria of mammalian cells
    • Hoogenraad N.J., Ward L.A., and Ryan Import M.T. Import and assembly of proteins into mitochondria of mammalian cells. Biochim. Biophys. Acta 1592 (2002) 97-105
    • (2002) Biochim. Biophys. Acta , vol.1592 , pp. 97-105
    • Hoogenraad, N.J.1    Ward, L.A.2    Ryan Import, M.T.3
  • 4
    • 17044437776 scopus 로고    scopus 로고
    • A railroad switch in mitochondrial protein import
    • Oka T., and Mihara K. A railroad switch in mitochondrial protein import. Mol. Cell 18 (2005) 145-146
    • (2005) Mol. Cell , vol.18 , pp. 145-146
    • Oka, T.1    Mihara, K.2
  • 5
    • 0035190881 scopus 로고    scopus 로고
    • Opening the door to mitochondrial protein import
    • Jensen R.E., and Johnson A.E. Opening the door to mitochondrial protein import. Nature Struct. Biol. 8 (2001) 1008-1010
    • (2001) Nature Struct. Biol. , vol.8 , pp. 1008-1010
    • Jensen, R.E.1    Johnson, A.E.2
  • 6
    • 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
  • 7
    • 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
  • 9
    • 33646354157 scopus 로고    scopus 로고
    • Translocation of mitochondrial inner-membrane proteins: conformation matters
    • de Marcos-Lousa C., Sideris D.P., and Tokatlidis K. Translocation of mitochondrial inner-membrane proteins: conformation matters. Trends Biochem. Sci. 31 (2006) 259-267
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 259-267
    • de Marcos-Lousa, C.1    Sideris, D.P.2    Tokatlidis, K.3
  • 10
    • 0346687594 scopus 로고    scopus 로고
    • The small Tim proteins and the twin Cx3C motif
    • Koehler C.M. The small Tim proteins and the twin Cx3C motif. Trends Biochem. Sci. 29 (2004) 1-4
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 1-4
    • Koehler, C.M.1
  • 11
    • 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
  • 12
    • 30844449228 scopus 로고    scopus 로고
    • Chaperoning through the mitochondrial intermembrane space
    • Wiedemann N., Pfanner N., and Chacinska A. Chaperoning through the mitochondrial intermembrane space. Mol. Cell 21 (2006) 145-148
    • (2006) Mol. Cell , vol.21 , pp. 145-148
    • Wiedemann, N.1    Pfanner, N.2    Chacinska, A.3
  • 14
    • 9144273327 scopus 로고    scopus 로고
    • Identification of Tim40 that mediates protein sorting to the mitochondrial intermembrane space
    • Naoé 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
    • Naoé, M.1    Ohwa, Y.2    Ishikawa, D.3    Ohshima, C.4    Nishikawa, S.5    Yamamoto, H.6    Endo, T.7
  • 15
    • 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
  • 16
    • 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., et al. Mia40, a novel factor for protein import into the intermembrane space of mitochondria is able to bind metal ions. FEBS Letters 579 (2005) 179-184
    • (2005) FEBS Letters , vol.579 , pp. 179-184
    • Terziyska, N.1    Lutz, T.2    Kozany, C.3    Mokranjac, D.4    Mesecke, N.5    Neupert, W.6
  • 17
    • 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
  • 18
    • 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
  • 19
    • 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
  • 20
    • 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
  • 21
    • 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 Letters 477 (2000) 62-66
    • (2000) FEBS Letters , vol.477 , pp. 62-66
    • Lee, J.1    Hofhaus, G.2    Lisowsky, T.3
  • 22
    • 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
  • 25
    • 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
  • 31
    • 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
  • 32
    • 0030965116 scopus 로고    scopus 로고
    • Cloning and characterization of MRP10, a yeast gene coding for a mitochondrial ribosomal protein
    • Jin C., Myers A.M., and Tzagoloff A. Cloning and characterization of MRP10, a yeast gene coding for a mitochondrial ribosomal protein. Curr. Genet. 31 (1997) 228-234
    • (1997) Curr. Genet. , vol.31 , pp. 228-234
    • Jin, C.1    Myers, A.M.2    Tzagoloff, A.3
  • 33
    • 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
  • 34
    • 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
  • 36
    • 0036840342 scopus 로고    scopus 로고
    • Mitochondrial import of the ADP/ATP carrier: the essential TIM complex of the intermembrane space is required for precursor release from the TOM complex
    • Truscott K.N., Wiedemann N., Rehling P., Müller H., Meisinger C., Pfanner N., and Guiard B. Mitochondrial import of the ADP/ATP carrier: the essential TIM complex of the intermembrane space is required for precursor release from the TOM complex. Mol. Cell. Biol. 22 (2002) 7780-7789
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7780-7789
    • Truscott, K.N.1    Wiedemann, N.2    Rehling, P.3    Müller, H.4    Meisinger, C.5    Pfanner, N.6    Guiard, B.7
  • 37
    • 0037566814 scopus 로고    scopus 로고
    • Tom40, the import channel of the mitochondrial outer membrane, plays an active role in sorting imported proteins
    • Gabriel K., Egan B., and Lithgow T. Tom40, the import channel of the mitochondrial outer membrane, plays an active role in sorting imported proteins. EMBO J. 22 (2003) 2380-2386
    • (2003) EMBO J. , vol.22 , pp. 2380-2386
    • Gabriel, K.1    Egan, B.2    Lithgow, T.3
  • 38
    • 30444449009 scopus 로고    scopus 로고
    • Essential role of Isd11 in mitochondrial iron-sulfur cluster synthesis on Isu scaffold proteins
    • Wiedemann N., Urzica E., Guiard B., Müller H., Lohaus C., Meyer H.E., et al. Essential role of Isd11 in mitochondrial iron-sulfur cluster synthesis on Isu scaffold proteins. EMBO J. 25 (2006) 184-195
    • (2006) EMBO J. , vol.25 , pp. 184-195
    • Wiedemann, N.1    Urzica, E.2    Guiard, B.3    Müller, H.4    Lohaus, C.5    Meyer, H.E.6
  • 39
    • 33644797502 scopus 로고    scopus 로고
    • Import of precursor proteins into isolated yeast mitochondria
    • Wiedemann N., Pfanner N., and Rehling P. Import of precursor proteins into isolated yeast mitochondria. Methods Mol. Biol. 313 (2006) 373-383
    • (2006) Methods Mol. Biol. , vol.313 , pp. 373-383
    • Wiedemann, N.1    Pfanner, N.2    Rehling, P.3
  • 40
    • 0029974008 scopus 로고    scopus 로고
    • Removal of an intron with unique 3′ branch site creates an amino-terminal protein sequence directing the scERV1 gene product to mitochondria
    • Lisowsky T. Removal of an intron with unique 3′ branch site creates an amino-terminal protein sequence directing the scERV1 gene product to mitochondria. Yeast 12 (1996) 1501-1510
    • (1996) Yeast , vol.12 , pp. 1501-1510
    • Lisowsky, T.1
  • 41
    • 20244373481 scopus 로고    scopus 로고
    • Mitochondrial presequence translocase: switching between TOM tethering and motor recruitment involves Tim21 and Tim17
    • Chacinska A., Lind M., Frazier A.E., Dudek J., Meisinger C., Geissler A., et al. Mitochondrial presequence translocase: switching between TOM tethering and motor recruitment involves Tim21 and Tim17. Cell 120 (2005) 817-829
    • (2005) Cell , vol.120 , pp. 817-829
    • Chacinska, A.1    Lind, M.2    Frazier, A.E.3    Dudek, J.4    Meisinger, C.5    Geissler, A.6
  • 42
    • 23844454079 scopus 로고    scopus 로고
    • Pam17 is required for architecture and translocation activity of the mitochondrial protein import motor
    • van der Laan M., Chacinska A., Lind M., Perschil I., Sickmann A., Meyer H.E., et al. Pam17 is required for architecture and translocation activity of the mitochondrial protein import motor. Mol. Cell. Biol. 25 (2005) 7449-7458
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 7449-7458
    • van der Laan, M.1    Chacinska, A.2    Lind, M.3    Perschil, I.4    Sickmann, A.5    Meyer, H.E.6
  • 43
    • 0020479807 scopus 로고
    • 2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria
    • 2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria. J. Biol. Chem. 257 (1982) 13028-13033
    • (1982) J. Biol. Chem. , vol.257 , pp. 13028-13033
    • Daum, G.1    Böhni, P.C.2    Schatz, G.3
  • 44
    • 0034672334 scopus 로고    scopus 로고
    • Purification of Saccharomcyes cerevisiae mitochondria devoid of microsomal and cytosolic contaminations
    • Meisinger C., Sommer T., and Pfanner N. Purification of Saccharomcyes cerevisiae mitochondria devoid of microsomal and cytosolic contaminations. Anal. Biochem. 287 (2000) 339-342
    • (2000) Anal. Biochem. , vol.287 , pp. 339-342
    • Meisinger, C.1    Sommer, T.2    Pfanner, N.3
  • 45
    • 0029851886 scopus 로고    scopus 로고
    • Characterization of the preprotein translocase of the outer mitochondrial membrane by blue native electrophoresis
    • Dekker P.J., Müller H., Rassow J., and Pfanner N. Characterization of the preprotein translocase of the outer mitochondrial membrane by blue native electrophoresis. Biol. Chem. 377 (1996) 535-538
    • (1996) Biol. Chem. , vol.377 , pp. 535-538
    • Dekker, P.J.1    Müller, H.2    Rassow, J.3    Pfanner, N.4
  • 46
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of head bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of head bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 47
    • 0019320778 scopus 로고
    • Synthesis, assembly into the cytoplasmic membrane, and proteolytic processing of the precursor of coliphage M13 coat protein
    • Ito K., Date T., and Wickner W. Synthesis, assembly into the cytoplasmic membrane, and proteolytic processing of the precursor of coliphage M13 coat protein. J. Biol. Chem. 255 (1980) 2123-2130
    • (1980) J. Biol. Chem. , vol.255 , pp. 2123-2130
    • Ito, K.1    Date, T.2    Wickner, W.3
  • 48
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger H., and von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166 (1987) 368-379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    von Jagow, G.2


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