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Volumn 6, Issue 9, 2011, Pages

The neurospora crassa TOB complex: Analysis of the topology and function of Tob38 and Tob37

Author keywords

[No Author keywords available]

Indexed keywords

BETA BARREL PROTEIN; FUNGAL PROTEIN; PROTEIN MDM10; PROTEIN TOB37; PROTEIN TOB38; PROTEIN TOB55; UNCLASSIFIED DRUG;

EID: 80053269088     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0025650     Document Type: Article
Times cited : (21)

References (71)
  • 1
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Neupert W, Herrmann J, (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.2
  • 2
    • 70349451660 scopus 로고    scopus 로고
    • Multiple pathways for mitochondrial protein traffic
    • Endo T, Yamano K, (2009) Multiple pathways for mitochondrial protein traffic. Biol Chem 390: 723-730.
    • (2009) Biol Chem , vol.390 , pp. 723-730
    • Endo, T.1    Yamano, K.2
  • 3
  • 4
    • 77956090193 scopus 로고    scopus 로고
    • Mitochondrial protein import: from proteomics to functional mechanisms
    • Schmidt O, Pfanner N, Meisinger C, (2010) Mitochondrial protein import: from proteomics to functional mechanisms. Nat Rev Mol Cell Biol 11: 655-667.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 655-667
    • Schmidt, O.1    Pfanner, N.2    Meisinger, C.3
  • 5
    • 1842478040 scopus 로고    scopus 로고
    • The Tim8-Tim13 complex of Neurospora crassa functions in the assembly of proteins into both mitochondrial membranes
    • Hoppins SC, Nargang FE, (2004) The Tim8-Tim13 complex of Neurospora crassa functions in the assembly of proteins into both mitochondrial membranes. J Biol Chem 279: 12396-12405.
    • (2004) J Biol Chem , vol.279 , pp. 12396-12405
    • Hoppins, S.C.1    Nargang, F.E.2
  • 6
    • 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 KN, Pfannschmidt S, Guiard B, Meisinger C, et al. (2004) 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: 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
  • 7
    • 56349137240 scopus 로고    scopus 로고
    • Biogenesis of mitochondrial outer membrane proteins
    • Walther DM, Rapaport D, (2009) Biogenesis of mitochondrial outer membrane proteins. Biochim Biophys Acta 1793: 42-51.
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 42-51
    • Walther, D.M.1    Rapaport, D.2
  • 8
    • 77953027874 scopus 로고    scopus 로고
    • Transport of proteins across or into the mitochondrial outer membrane
    • Endo T, 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
  • 9
    • 4444290664 scopus 로고    scopus 로고
    • Two novel proteins in the mitochondrial outer membrane mediate b-barrel protein assembly
    • Ishikawa D, Yamamoto H, Tamura Y, Moritoh K, Endo T, (2004) Two novel proteins in the mitochondrial outer membrane mediate b-barrel protein assembly. J Cell Biol 166: 621-627.
    • (2004) J Cell Biol , vol.166 , pp. 621-627
    • Ishikawa, D.1    Yamamoto, H.2    Tamura, Y.3    Moritoh, K.4    Endo, T.5
  • 10
    • 2542499525 scopus 로고    scopus 로고
    • Sam35 of the mitochondrial protein sorting and assembly machinery is a peripheral outer membrane protein essential for cell viability
    • Milenkovic D, Kozjak V, Wiedemann N, Lohaus C, Meyer HE, et al. (2004) Sam35 of the mitochondrial protein sorting and assembly machinery is a peripheral outer membrane protein essential for cell viability. J Biol Chem 279: 22781-22785.
    • (2004) J Biol Chem , vol.279 , pp. 22781-22785
    • Milenkovic, D.1    Kozjak, V.2    Wiedemann, N.3    Lohaus, C.4    Meyer, H.E.5
  • 11
    • 4444376183 scopus 로고    scopus 로고
    • Tob38, a novel essential component in the biogenesis of b-barrel proteins of mitochondria
    • Waizenegger T, Habib SJ, Lech M, Mokranjac D, Paschen SA, et al. (2004) Tob38, a novel essential component in the biogenesis of b-barrel proteins of mitochondria. EMBO Rep 5: 704-709.
    • (2004) EMBO Rep , vol.5 , pp. 704-709
    • Waizenegger, T.1    Habib, S.J.2    Lech, M.3    Mokranjac, D.4    Paschen, S.A.5
  • 12
    • 4344640696 scopus 로고    scopus 로고
    • The mitochondrial morphology protein Mdm10 functions in assembly of the preprotein translocase of the outer membrane
    • Meisinger C, Rissler M, Chacinska A, Sanjuán Szklarz LK, Milenkovic D, et al. (2004) The mitochondrial morphology protein Mdm10 functions in assembly of the preprotein translocase of the outer membrane. Developmental Cell 7: 61-71.
    • (2004) Developmental Cell , vol.7 , pp. 61-71
    • Meisinger, C.1    Rissler, M.2    Chacinska, A.3    Sanjuán Szklarz, L.K.4    Milenkovic, D.5
  • 13
    • 33747353837 scopus 로고    scopus 로고
    • Mitochondrial protein sorting: Differentiation of b-barrel assembly by Tom7-mediated segregation of Mdm10
    • Meisinger C, Wiedemann N, Rissler M, Strub A, Milenkovic D, et al. (2006) Mitochondrial protein sorting: Differentiation of b-barrel assembly by Tom7-mediated segregation of Mdm10. J Biol Chem 281: 22819-22826.
    • (2006) J Biol Chem , vol.281 , pp. 22819-22826
    • Meisinger, C.1    Wiedemann, N.2    Rissler, M.3    Strub, A.4    Milenkovic, D.5
  • 14
    • 77949316294 scopus 로고    scopus 로고
    • Two modular forms of the mitochondrial sorting and assembly machinery are involved in biogenesis of a-helical outer membrane proteins
    • Thornton N, Stroud DA, Milenkovic D, Guiard B, Pfanner N, et al. (2010) Two modular forms of the mitochondrial sorting and assembly machinery are involved in biogenesis of a-helical outer membrane proteins. J Mol Biol 396: 540-549.
    • (2010) J Mol Biol , vol.396 , pp. 540-549
    • Thornton, N.1    Stroud, D.A.2    Milenkovic, D.3    Guiard, B.4    Pfanner, N.5
  • 15
    • 77649274082 scopus 로고    scopus 로고
    • Mdm10 as a dynamic constituent of the TOB/SAM complex directs coordinated assembly of Tom40
    • Yamano K, Tanaka-Yamano S, Endo T, (2010) Mdm10 as a dynamic constituent of the TOB/SAM complex directs coordinated assembly of Tom40. EMBO Rep 11: 187-193.
    • (2010) EMBO Rep , vol.11 , pp. 187-193
    • Yamano, K.1    Tanaka-Yamano, S.2    Endo, T.3
  • 16
    • 77952395425 scopus 로고    scopus 로고
    • Roles of the Mdm10, Tom7, Mdm12, and Mmm1 proteins in the assembly of mitochondrial outer membrane proteins in Neurospora crassa
    • Wideman JG, Go NE, Klein A, Redmond EK, Lackey SWK, et al. (2010) Roles of the Mdm10, Tom7, Mdm12, and Mmm1 proteins in the assembly of mitochondrial outer membrane proteins in Neurospora crassa. Mol Biol Cell 21: 1725-1736.
    • (2010) Mol Biol Cell , vol.21 , pp. 1725-1736
    • Wideman, J.G.1    Go, N.E.2    Klein, A.3    Redmond, E.K.4    Lackey, S.W.K.5
  • 17
    • 0028024592 scopus 로고
    • Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane
    • Sogo LF, Yaffe MP, (1994) Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane. J Cell Biol 126: 1361-1373.
    • (1994) J Cell Biol , vol.126 , pp. 1361-1373
    • Sogo, L.F.1    Yaffe, M.P.2
  • 18
    • 0344392841 scopus 로고    scopus 로고
    • A protein complex containing Mdm10p, Mdm12p, and Mmm1p links mitochondrial membranes and DNA to the cytoskeleton-based segregation machinery
    • Boldogh IR, Nowakowski DW, Yang H-C, Chung H, Karmon S, et al. (2003) A protein complex containing Mdm10p, Mdm12p, and Mmm1p links mitochondrial membranes and DNA to the cytoskeleton-based segregation machinery. Mol Biol Cell 14: 4618-4627.
    • (2003) Mol Biol Cell , vol.14 , pp. 4618-4627
    • Boldogh, I.R.1    Nowakowski, D.W.2    Yang, H.-C.3    Chung, H.4    Karmon, S.5
  • 19
    • 67749122635 scopus 로고    scopus 로고
    • An ER-mitochondria tethering complex revealed by a synthetic biology screen
    • Kornmann B, Currie E, Collins SR, Schuldiner M, Nunnari J, et al. (2009) An ER-mitochondria tethering complex revealed by a synthetic biology screen. Science 325: 477-481.
    • (2009) Science , vol.325 , pp. 477-481
    • Kornmann, B.1    Currie, E.2    Collins, S.R.3    Schuldiner, M.4    Nunnari, J.5
  • 20
    • 0033619269 scopus 로고    scopus 로고
    • Tom22 is a multifunctional organizer of the mitochondrial preprotein translocase
    • van Wilpe S, Ryan MT, Hill K, Maarse AC, Meisinger C, et al. (1999) Tom22 is a multifunctional organizer of the mitochondrial preprotein translocase. Nature 401: 485-489.
    • (1999) Nature , vol.401 , pp. 485-489
    • van Wilpe, S.1    Ryan, M.T.2    Hill, K.3    Maarse, A.C.4    Meisinger, C.5
  • 21
    • 78650418885 scopus 로고    scopus 로고
    • Biogenesis of mitochondria: Dual role of Tom7 in modulating assembly of the preprotein translocase of the outer membrane
    • Becker T, Wenz L-S, Thornton N, Stroud DA, Meisinger C, et al. (2011) Biogenesis of mitochondria: Dual role of Tom7 in modulating assembly of the preprotein translocase of the outer membrane. J Mol Biol 405: 113-124.
    • (2011) J Mol Biol , vol.405 , pp. 113-124
    • Becker, T.1    Wenz, L.-S.2    Thornton, N.3    Stroud, D.A.4    Meisinger, C.5
  • 22
    • 38049184807 scopus 로고    scopus 로고
    • Biogenesis of the mitochondrial TOM complex. Mim1 promotes insertion and assembly of signal-anchored receptors
    • Becker T, Pfannschmidt S, Guiard B, Stojanovski D, Milenkovic D, et al. (2008) Biogenesis of the mitochondrial TOM complex. Mim1 promotes insertion and assembly of signal-anchored receptors. J Biol Chem 283: 120-127.
    • (2008) J Biol Chem , vol.283 , pp. 120-127
    • Becker, T.1    Pfannschmidt, S.2    Guiard, B.3    Stojanovski, D.4    Milenkovic, D.5
  • 23
    • 67349206741 scopus 로고    scopus 로고
    • The three domains of the mitochondrial outer membrane protein Mim1 have discrete functions in assembly of the TOM complex
    • Lueder F, Lithgow T, (2009) The three domains of the mitochondrial outer membrane protein Mim1 have discrete functions in assembly of the TOM complex. FEBS Lett 583: 1475-1480.
    • (2009) FEBS Lett , vol.583 , pp. 1475-1480
    • Lueder, F.1    Lithgow, T.2
  • 24
    • 0346727130 scopus 로고    scopus 로고
    • Evolutionary conservation of biogenesis of b-barrel membrane proteins
    • Paschen SA, Waizenegger T, Stan T, Preuss M, Cyrklaff M, et al. (2003) Evolutionary conservation of biogenesis of b-barrel membrane proteins. Nature 426: 862-866.
    • (2003) Nature , vol.426 , pp. 862-866
    • Paschen, S.A.1    Waizenegger, T.2    Stan, T.3    Preuss, M.4    Cyrklaff, M.5
  • 25
    • 0348093762 scopus 로고    scopus 로고
    • An essential role of Sam50 in the protein sorting and assembly machinery of the mitochondrial outer membrane
    • Kozjak V, Wiedemann N, Milenkovic D, Lohaus C, Meyer HE, et al. (2003) An essential role of Sam50 in the protein sorting and assembly machinery of the mitochondrial outer membrane. J Biol Chem 278: 48520-48523.
    • (2003) J Biol Chem , vol.278 , pp. 48520-48523
    • Kozjak, V.1    Wiedemann, N.2    Milenkovic, D.3    Lohaus, C.4    Meyer, H.E.5
  • 26
    • 0345861754 scopus 로고    scopus 로고
    • The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria
    • Gentle I, Gabriel K, Beech P, Waller R, Lithgow T, (2004) The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria. J Cell Biol 164: 19-24.
    • (2004) J Cell Biol , vol.164 , pp. 19-24
    • Gentle, I.1    Gabriel, K.2    Beech, P.3    Waller, R.4    Lithgow, T.5
  • 27
    • 35048829823 scopus 로고    scopus 로고
    • Alternative splicing gives rise to different isoforms of the Neurospora crassa Tob55 protein that vary in their ability to insert b-barrel proteins into the outer mitochondrial membrane
    • Hoppins SC, Go NE, Klein A, Schmitt S, Neupert W, et al. (2007) Alternative splicing gives rise to different isoforms of the Neurospora crassa Tob55 protein that vary in their ability to insert b-barrel proteins into the outer mitochondrial membrane. Genetics 177: 137-149.
    • (2007) Genetics , vol.177 , pp. 137-149
    • Hoppins, S.C.1    Go, N.E.2    Klein, A.3    Schmitt, S.4    Neupert, W.5
  • 28
    • 40749159588 scopus 로고    scopus 로고
    • Dissecting membrane insertion of mitochondrial b-barrel proteins
    • Kutik S, Stojanovski D, Becker L, Becker T, Meinecke M, et al. (2008) Dissecting membrane insertion of mitochondrial b-barrel proteins. Cell 132: 1011-1024.
    • (2008) Cell , vol.132 , pp. 1011-1024
    • Kutik, S.1    Stojanovski, D.2    Becker, L.3    Becker, T.4    Meinecke, M.5
  • 29
    • 80051698640 scopus 로고    scopus 로고
    • Biogenesis of mtiochondrial b-barrel proteins: the POTRA domain is involved in precursor release from the SAM complex
    • Stroud DA, Becker T, Qiu J, Stojanovski D, Pfannschmidt S, et al. (2011) Biogenesis of mtiochondrial b-barrel proteins: the POTRA domain is involved in precursor release from the SAM complex. Mol Biol Cell 22: 2823-2833.
    • (2011) Mol Biol Cell , vol.22 , pp. 2823-2833
    • Stroud, D.A.1    Becker, T.2    Qiu, J.3    Stojanovski, D.4    Pfannschmidt, S.5
  • 30
    • 0028967994 scopus 로고
    • Mas37p, a novel receptor subunit for protein import into mitochondria
    • Gratzer S, Lithgow T, Bauer RE, Lamping E, Paltauf F, et al. (1995) Mas37p, a novel receptor subunit for protein import into mitochondria. J Cell Biol 129: 25-34.
    • (1995) J Cell Biol , vol.129 , pp. 25-34
    • Gratzer, S.1    Lithgow, T.2    Bauer, R.E.3    Lamping, E.4    Paltauf, F.5
  • 31
    • 0040610684 scopus 로고    scopus 로고
    • Functional staging of ADP/ATP carrier translocation across the outer mitochondrial membrane
    • Ryan MT, Muller H, Pfanner N, (1999) Functional staging of ADP/ATP carrier translocation across the outer mitochondrial membrane. J Biol Chem 274: 20619-20627.
    • (1999) J Biol Chem , vol.274 , pp. 20619-20627
    • Ryan, M.T.1    Muller, H.2    Pfanner, N.3
  • 32
    • 0042163218 scopus 로고    scopus 로고
    • Machinery for protein sorting and assembly in the mitochondrial outer membrane
    • Wiedemann N, Kozjak V, Chacinska A, Schönfisch B, Rospert S, et al. (2003) Machinery for protein sorting and assembly in the mitochondrial outer membrane. Nature 424: 565-571.
    • (2003) Nature , vol.424 , pp. 565-571
    • Wiedemann, N.1    Kozjak, V.2    Chacinska, A.3    Schönfisch, B.4    Rospert, S.5
  • 33
    • 38749085210 scopus 로고    scopus 로고
    • The peripheral membrane subunits of the SAM complex function codependently in mitochondrial outer membrane biogenesis
    • Chan NC, Lithgow T, (2008) The peripheral membrane subunits of the SAM complex function codependently in mitochondrial outer membrane biogenesis. Mol Biol Cell 19: 126-136.
    • (2008) Mol Biol Cell , vol.19 , pp. 126-136
    • Chan, N.C.1    Lithgow, T.2
  • 34
    • 71949129385 scopus 로고    scopus 로고
    • Genetic and functional interactions between the mitochondrial outer membrane proteins Tom6 and Sam37
    • Dukanovic J, Dimmer KS, Bonnefoy N, Krumpe K, Rapaport D, (2009) Genetic and functional interactions between the mitochondrial outer membrane proteins Tom6 and Sam37. Mol Cell Biol 29: 5975-5988.
    • (2009) Mol Cell Biol , vol.29 , pp. 5975-5988
    • Dukanovic, J.1    Dimmer, K.S.2    Bonnefoy, N.3    Krumpe, K.4    Rapaport, D.5
  • 35
    • 34247583466 scopus 로고    scopus 로고
    • The morphology proteins Mdm12/Mmm1 function in the major b-barrel assembly pathway of mitochondria
    • Meisinger C, Pfannschmidt S, Rissler M, Milenkovic D, Becker T, et al. (2007) The morphology proteins Mdm12/Mmm1 function in the major b-barrel assembly pathway of mitochondria. EMBO J 26: 2229-2239.
    • (2007) EMBO J , vol.26 , pp. 2229-2239
    • Meisinger, C.1    Pfannschmidt, S.2    Rissler, M.3    Milenkovic, D.4    Becker, T.5
  • 36
    • 79551670803 scopus 로고    scopus 로고
    • Cell wall integrity is linked to mitochondria and phospholipid homeostasis in Candida albicans through the activity of the post-transcriptional regulator Ccr4-Pop2
    • Dagley MJ, Gentle IE, Beilharz TH, Pettolino FA, Djordjevic JT, et al. (2011) Cell wall integrity is linked to mitochondria and phospholipid homeostasis in Candida albicans through the activity of the post-transcriptional regulator Ccr4-Pop2. Mol Micro 79: 968-989.
    • (2011) Mol Micro , vol.79 , pp. 968-989
    • Dagley, M.J.1    Gentle, I.E.2    Beilharz, T.H.3    Pettolino, F.A.4    Djordjevic, J.T.5
  • 37
  • 38
    • 0030934657 scopus 로고    scopus 로고
    • Metaxin is a component of a preprotein import complex in the outer membrane of the mammalian mitochondrion
    • Armstrong LC, Komiya T, Bergman BE, Mihara K, Bornstein P, (1997) Metaxin is a component of a preprotein import complex in the outer membrane of the mammalian mitochondrion. J Biol Chem 272: 6510-6518.
    • (1997) J Biol Chem , vol.272 , pp. 6510-6518
    • Armstrong, L.C.1    Komiya, T.2    Bergman, B.E.3    Mihara, K.4    Bornstein, P.5
  • 39
    • 0033168413 scopus 로고    scopus 로고
    • Metaxin 1 interacts with metaxin 2, a novel related protein associated with the mammalian mitochondrial outer membrane
    • Armstrong LC, Saenz AJ, Bornstein P, (1999) Metaxin 1 interacts with metaxin 2, a novel related protein associated with the mammalian mitochondrial outer membrane. J Cell Biochem 74: 11-22.
    • (1999) J Cell Biochem , vol.74 , pp. 11-22
    • Armstrong, L.C.1    Saenz, A.J.2    Bornstein, P.3
  • 41
    • 0034609954 scopus 로고    scopus 로고
    • Functional analysis of human metaxin in mitochondrial protein import in cultured cells and its relationship with the TOM complex
    • Abdul KM, Terada K, Yano M, Ryan MT, Streimann I, et al. (2000) Functional analysis of human metaxin in mitochondrial protein import in cultured cells and its relationship with the TOM complex. Biochem Biophys Res Commun 276: 1028-1034.
    • (2000) Biochem Biophys Res Commun , vol.276 , pp. 1028-1034
    • Abdul, K.M.1    Terada, K.2    Yano, M.3    Ryan, M.T.4    Streimann, I.5
  • 42
    • 34447268008 scopus 로고    scopus 로고
    • The mitochondrial inner membrane protein mitofilin exists as a complex with SAM50, metaxins 1 and 2, coiled-coil-helix coiled-coil-helix domain containing protein 3 and 6 and DnaJC11
    • Xie J, Marusich MF, Souda P, Whitelegge J, Capaldi RA, (2007) The mitochondrial inner membrane protein mitofilin exists as a complex with SAM50, metaxins 1 and 2, coiled-coil-helix coiled-coil-helix domain containing protein 3 and 6 and DnaJC11. FEBS Lett 581: 3545-3549.
    • (2007) FEBS Lett , vol.581 , pp. 3545-3549
    • Xie, J.1    Marusich, M.F.2    Souda, P.3    Whitelegge, J.4    Capaldi, R.A.5
  • 43
    • 0029015815 scopus 로고
    • Metaxin, a gene contiguous to both thrombospondin 3 and glucocerebrosidase, is required for embryonic development in the mouse: implications for Gaucher disease
    • Bornstein P, McKinney CE, LaMarca ME, Winfield S, Shingu T, et al. (1995) Metaxin, a gene contiguous to both thrombospondin 3 and glucocerebrosidase, is required for embryonic development in the mouse: implications for Gaucher disease. Proc Natl Acad Sci USA 92: 4547-4551.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4547-4551
    • Bornstein, P.1    McKinney, C.E.2    LaMarca, M.E.3    Winfield, S.4    Shingu, T.5
  • 44
    • 77956995235 scopus 로고
    • Genetic and microbiological research techniques for Neurospora crassa
    • Davis RH, De Serres FJ, (1970) Genetic and microbiological research techniques for Neurospora crassa. Methods Enzymol 17: 79-143.
    • (1970) Methods Enzymol , vol.17 , pp. 79-143
    • Davis, R.H.1    De Serres, F.J.2
  • 45
    • 33745924142 scopus 로고    scopus 로고
    • A high-throughput gene knockout procedure for Neurospora reveals functions for multiple transcription factors
    • Colot HV, Park G, Turner GE, Ringelberg C, Crew C, et al. (2006) A high-throughput gene knockout procedure for Neurospora reveals functions for multiple transcription factors. Proc Natl Acad Sci USA 103: 10352-10357.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 10352-10357
    • Colot, H.V.1    Park, G.2    Turner, G.E.3    Ringelberg, C.4    Crew, C.5
  • 46
    • 0028955901 scopus 로고
    • "Sheltered disruption" of Neurospora crassa MOM22, an essential component of the mitochondrial protein import complex
    • Nargang FE, Künkele K-P, Mayer A, Ritzel RG, Neupert W, et al. (1995) "Sheltered disruption" of Neurospora crassa MOM22, an essential component of the mitochondrial protein import complex. EMBO J 14: 1099-1108.
    • (1995) EMBO J , vol.14 , pp. 1099-1108
    • Nargang, F.E.1    Künkele, K.-P.2    Mayer, A.3    Ritzel, R.G.4    Neupert, W.5
  • 47
    • 0028949233 scopus 로고
    • Some property of the nucleus determines the competence of Neurospora crassa for transformation
    • Grotelueschen J, Metzenberg R, (1995) Some property of the nucleus determines the competence of Neurospora crassa for transformation. Genetics 139: 1545-1551.
    • (1995) Genetics , vol.139 , pp. 1545-1551
    • Grotelueschen, J.1    Metzenberg, R.2
  • 48
    • 0025059745 scopus 로고
    • Optimized vectors and selection for transformation of Neurospora crassa and Aspergillus nidulans to bleomycin and phleomycin resistance
    • Austin B, Hall RM, Tyler BM, (1990) Optimized vectors and selection for transformation of Neurospora crassa and Aspergillus nidulans to bleomycin and phleomycin resistance. Gene 93: 157-162.
    • (1990) Gene , vol.93 , pp. 157-162
    • Austin, B.1    Hall, R.M.2    Tyler, B.M.3
  • 49
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK, (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 50
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane complexes in enzymatically active form
    • Schägger H, von Jagow G, (1991) Blue native electrophoresis for isolation of membrane complexes in enzymatically active form. Anal Biochem 199: 223-231.
    • (1991) Anal Biochem , vol.199 , pp. 223-231
    • Schägger, H.1    von Jagow, G.2
  • 51
    • 0028214450 scopus 로고
    • Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis
    • Schägger H, Cramer WA, von Jagow G, (1994) Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis. Anal Biochem 217: 220-230.
    • (1994) Anal Biochem , vol.217 , pp. 220-230
    • Schägger, H.1    Cramer, W.A.2    von Jagow, G.3
  • 52
    • 77952384264 scopus 로고    scopus 로고
    • Neurospora crassa as a model organism for mitochondrial biogenesis
    • In: Leister DL, Herrmann J, editors, Totowa, NJ, Humana Press
    • Nargang FE, Rapaport D, (2007) Neurospora crassa as a model organism for mitochondrial biogenesis. In: Leister DL, Herrmann J, editors. Mitochondria Practical Protocols Totowa, NJ Humana Press.
    • (2007) Mitochondria Practical Protocols
    • Nargang, F.E.1    Rapaport, D.2
  • 53
    • 0028316039 scopus 로고
    • A crucial role of the mitochondrial protein import receptor MOM19 for the biogenesis of mitochondria
    • Harkness TAA, Nargang FE, Van der Klei I, Neupert W, Lill R, (1994) A crucial role of the mitochondrial protein import receptor MOM19 for the biogenesis of mitochondria. J Cell Biol 124: 637-648.
    • (1994) J Cell Biol , vol.124 , pp. 637-648
    • Harkness, T.A.A.1    Nargang, F.E.2    van der Klei, I.3    Neupert, W.4    Lill, R.5
  • 54
    • 0032857837 scopus 로고    scopus 로고
    • Inactivation of the Neurospora crassa mitochondrial outer membrane protein TOM70 by repeat-induced point mutation (RIP) causes defects in mitochondrial protein import and morphology
    • Grad L, Descheneau A, Neupert W, Lill R, Nargang F, (1999) Inactivation of the Neurospora crassa mitochondrial outer membrane protein TOM70 by repeat-induced point mutation (RIP) causes defects in mitochondrial protein import and morphology. Curr Genet 36: 137-146.
    • (1999) Curr Genet , vol.36 , pp. 137-146
    • Grad, L.1    Descheneau, A.2    Neupert, W.3    Lill, R.4    Nargang, F.5
  • 55
    • 0035066635 scopus 로고    scopus 로고
    • Multistep assembly of the protein import channel of the mitochondrial outer membrane
    • Model K, Meisinger C, Prinz T, Wiedemann N, Truscott KN, et al. (2001) Multistep assembly of the protein import channel of the mitochondrial outer membrane. Nat Struct Biol 8: 361-370.
    • (2001) Nat Struct Biol , vol.8 , pp. 361-370
    • Model, K.1    Meisinger, C.2    Prinz, T.3    Wiedemann, N.4    Truscott, K.N.5
  • 56
    • 0033606811 scopus 로고    scopus 로고
    • Biogenesis of Tom40, core component of the TOM complex of mitochondria
    • Rapaport D, Neupert W, (1999) Biogenesis of Tom40, core component of the TOM complex of mitochondria. J Cell Biol 146: 321-331.
    • (1999) J Cell Biol , vol.146 , pp. 321-331
    • Rapaport, D.1    Neupert, W.2
  • 57
    • 0037428379 scopus 로고    scopus 로고
    • Characterization of Neurospora crassa Tom40-deficient mutants and effect of specific mutations on Tom40 assembly
    • Taylor R, McHale B, Nargang FE, (2003) Characterization of Neurospora crassa Tom40-deficient mutants and effect of specific mutations on Tom40 assembly. J Biol Chem 278: 765-775.
    • (2003) J Biol Chem , vol.278 , pp. 765-775
    • Taylor, R.1    McHale, B.2    Nargang, F.E.3
  • 58
    • 0036499987 scopus 로고    scopus 로고
    • The Tim9p-Tim10p complex binds to the transmembrane domains of the ADP/ATP carrier
    • Curran SP, Leuenberger D, Oppliger W, Koehler CM, (2002) The Tim9p-Tim10p complex binds to the transmembrane domains of the ADP/ATP carrier. EMBO J 21: 942-953.
    • (2002) EMBO J , vol.21 , pp. 942-953
    • Curran, S.P.1    Leuenberger, D.2    Oppliger, W.3    Koehler, C.M.4
  • 59
    • 0037119946 scopus 로고    scopus 로고
    • The role of the Tim8p-Tim13p complex in a conserved import pathway for mitochondrial polytopic inner membrane proteins
    • Curran SP, Leuenberger D, Schmidt E, Koehler CM, (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
  • 60
    • 12144287756 scopus 로고    scopus 로고
    • Reconstituted TOM core complex and Tim9/Tim10 complex of mitochondria are sufficient for translocation of the ADP/ATP carrier across membranes
    • Vasiljev A, Ahting U, Nargang FE, Go NE, Habib SJ, et al. (2004) Reconstituted TOM core complex and Tim9/Tim10 complex of mitochondria are sufficient for translocation of the ADP/ATP carrier across membranes. Mol Biol Cell 15: 1445-1458.
    • (2004) Mol Biol Cell , vol.15 , pp. 1445-1458
    • Vasiljev, A.1    Ahting, U.2    Nargang, F.E.3    Go, N.E.4    Habib, S.J.5
  • 61
    • 29544436323 scopus 로고    scopus 로고
    • Crystal structure of the mitochondrial chaperone TIM9-10 reveals a six-bladed a-propeller
    • Webb CT, Gorman MA, Lazarou M, Ryan MT, Gulbis JM, (2006) Crystal structure of the mitochondrial chaperone TIM9-10 reveals a six-bladed a-propeller. Mol Cell 21: 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
  • 65
    • 0029994354 scopus 로고    scopus 로고
    • Tom71, a novel homologue of the mitochondrial preprotein receptor Tom70
    • Schlossmann J, Lill R, Neupert W, Court DA, (1996) Tom71, a novel homologue of the mitochondrial preprotein receptor Tom70. J Biol Chem 271: 17890-17896.
    • (1996) J Biol Chem , vol.271 , pp. 17890-17896
    • Schlossmann, J.1    Lill, R.2    Neupert, W.3    Court, D.A.4
  • 66
    • 0023478499 scopus 로고
    • Relationship between two major immunoreactive forms of arginase in Neurospora crassa
    • Borkovich KA, Weiss RL, (1987) Relationship between two major immunoreactive forms of arginase in Neurospora crassa. J Bact 169: 5510-5517.
    • (1987) J Bact , vol.169 , pp. 5510-5517
    • Borkovich, K.A.1    Weiss, R.L.2
  • 67
    • 14444270121 scopus 로고    scopus 로고
    • Multiple forms of arginase are differentially expressed from a single locus in Neurospora crassa
    • Marathe S, Yu YG, Turner GE, Palmier C, Weiss RL, (1998) Multiple forms of arginase are differentially expressed from a single locus in Neurospora crassa. J Biol Chem 273: 29776-29785.
    • (1998) J Biol Chem , vol.273 , pp. 29776-29785
    • Marathe, S.1    Yu, Y.G.2    Turner, G.E.3    Palmier, C.4    Weiss, R.L.5
  • 68
    • 0036000002 scopus 로고    scopus 로고
    • Characterization of signal that directs C-tail-anchored proteins to mammalian mitochondrial outer membrane
    • Horie C, Suzuki H, Sakaguchi M, Mihara K, (2002) Characterization of signal that directs C-tail-anchored proteins to mammalian mitochondrial outer membrane. Mol Biol Cell 13: 1615-1625.
    • (2002) Mol Biol Cell , vol.13 , pp. 1615-1625
    • Horie, C.1    Suzuki, H.2    Sakaguchi, M.3    Mihara, K.4
  • 69
    • 33747331322 scopus 로고    scopus 로고
    • Mitochondrial biogenesis: Protein import into and across the outer membrane
    • In: Bauer M, Koehler C, editors, Berlin Heidelberg, Springer-Verlag
    • Rapaport D, Nargang FE, (2004) Mitochondrial biogenesis: Protein import into and across the outer membrane. In: Bauer M, Koehler C, editors. Topics in Current Genetics, Vol 8 Biogenesis of mitochondria and associated diseases Berlin Heidelberg Springer-Verlag pp. 37-58.
    • (2004) Topics in Current Genetics, Biogenesis of Mitochondria and Associated Diseases , vol.8 , pp. 37-58
    • Rapaport, D.1    Nargang, F.E.2
  • 70
    • 77956700810 scopus 로고    scopus 로고
    • Assembly of the mitochondrial protein import channel. Role of Tom5 in two-stage interaction of Tom40 with the SAM complex
    • Becker T, Guiard B, Thornton N, Zufall N, Stroud DA, et al. (2010) Assembly of the mitochondrial protein import channel. Role of Tom5 in two-stage interaction of Tom40 with the SAM complex. Mol Biol Cell 21: 3106-3113.
    • (2010) Mol Biol Cell , vol.21 , pp. 3106-3113
    • Becker, T.1    Guiard, B.2    Thornton, N.3    Zufall, N.4    Stroud, D.A.5
  • 71
    • 24344508557 scopus 로고    scopus 로고
    • Functions of the small proteins in the TOM complex of Neurospora crassa
    • Sherman EL, Go NE, Nargang FE, (2005) Functions of the small proteins in the TOM complex of Neurospora crassa. Mol Biol Cell 16: 4172-4182.
    • (2005) Mol Biol Cell , vol.16 , pp. 4172-4182
    • Sherman, E.L.1    Go, N.E.2    Nargang, F.E.3


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