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Volumn 176, Issue 1, 2007, Pages 77-88

The N-terminal domain of Tob55 has a receptor-like function in the biogenesis of mitochondrial β-barrel proteins

Author keywords

[No Author keywords available]

Indexed keywords

MITOCHONDRIAL PROTEIN; PROTEIN BETA BARREL; UNCLASSIFIED DRUG;

EID: 33846002342     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.200602050     Document Type: Article
Times cited : (73)

References (48)
  • 1
    • 8844219773 scopus 로고    scopus 로고
    • Biogenesis of the Gram-negative bacterial outer membrane
    • Bos, M.P., and J. Tommassen. 2004. Biogenesis of the Gram-negative bacterial outer membrane. Curr. Opin. Microbiol. 7:610-616.
    • (2004) Curr. Opin. Microbiol , vol.7 , pp. 610-616
    • Bos, M.P.1    Tommassen, J.2
  • 2
    • 0030586353 scopus 로고    scopus 로고
    • Role of the N- and C-termini of porin in import into the outer membrane of Neurospora mitochondria
    • Court, D.A., R. Kleene, W. Neupert, and R. Lill. 1996. Role of the N- and C-termini of porin in import into the outer membrane of Neurospora mitochondria. FEBS Lett. 390:73-77.
    • (1996) FEBS Lett , vol.390 , pp. 73-77
    • Court, D.A.1    Kleene, R.2    Neupert, W.3    Lill, R.4
  • 4
    • 0031580211 scopus 로고    scopus 로고
    • Role of the carboxy-terminal phenylalanine in the biogenesis of outer membrane protein PhoE of Escherichia coli K-12
    • de Cock, H., M. Struyve, M. Kleerebezem, T. van der Krift, and J. Tommassen. 1997. Role of the carboxy-terminal phenylalanine in the biogenesis of outer membrane protein PhoE of Escherichia coli K-12. J. Mol. Biol. 269:473-478.
    • (1997) J. Mol. Biol , vol.269 , pp. 473-478
    • de Cock, H.1    Struyve, M.2    Kleerebezem, M.3    van der Krift, T.4    Tommassen, J.5
  • 5
    • 33746575844 scopus 로고    scopus 로고
    • Evolution of the molecular machines for protein import into mitochondria
    • Dolezal, P., V. Likic, J. Tachezy, and T. Lithgow. 2006. Evolution of the molecular machines for protein import into mitochondria. Science. 313:314-318.
    • (2006) Science , vol.313 , pp. 314-318
    • Dolezal, P.1    Likic, V.2    Tachezy, J.3    Lithgow, T.4
  • 7
    • 23344442676 scopus 로고    scopus 로고
    • The evolutionarily related β-barrel polypeptide transporters from Pisum sativum and Nostoc PCC7120 contain two distinct functional domains
    • Ertel, F., O. Mirus, R. Bredemeier, S. Moslavac, T. Becker, and E. Schleiff. 2005. The evolutionarily related β-barrel polypeptide transporters from Pisum sativum and Nostoc PCC7120 contain two distinct functional domains. J. Biol. Chem. 280:28281-28289.
    • (2005) J. Biol. Chem , vol.280 , pp. 28281-28289
    • Ertel, F.1    Mirus, O.2    Bredemeier, R.3    Moslavac, S.4    Becker, T.5    Schleiff, E.6
  • 8
    • 0035153316 scopus 로고    scopus 로고
    • The alpha and beta: Protein translocation across mitochondrial and plastid outer membranes
    • Gabriel, K., S.K. Buchanan, and T. Lithgow. 2001. The alpha and beta: protein translocation across mitochondrial and plastid outer membranes. Trends Biochem. Sci. 26:36-40.
    • (2001) Trends Biochem. Sci , vol.26 , pp. 36-40
    • Gabriel, K.1    Buchanan, S.K.2    Lithgow, T.3
  • 9
    • 0345861754 scopus 로고    scopus 로고
    • The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria
    • Gentle, I., K. Gabriel, P. Beech, R. Waller, and T. Lithgow. 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
  • 11
    • 21244447713 scopus 로고    scopus 로고
    • The periplasmic chaperone SurA exploits two features characteristic of integral outer membrane proteins for selective substrate recognition
    • Hennecke, G., J. Nolte, R. Volkmer-Engert, J. Schneider-Mergener, and S. Behrens. 2005. The periplasmic chaperone SurA exploits two features characteristic of integral outer membrane proteins for selective substrate recognition. J. Biol. Chem. 280:23540-23548.
    • (2005) J. Biol. Chem , vol.280 , pp. 23540-23548
    • Hennecke, G.1    Nolte, J.2    Volkmer-Engert, R.3    Schneider-Mergener, J.4    Behrens, S.5
  • 12
    • 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 F.E. Nargang. 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
  • 13
    • 0024327616 scopus 로고
    • Disrupted yeast mitochondria can import precursor proteins directly through their inner membrane
    • Hwang, S., T. Jascur, D. Vestweber, L. Pon, and G. Schatz. 1989. Disrupted yeast mitochondria can import precursor proteins directly through their inner membrane. J. Cell Biol. 109:487-493.
    • (1989) J. Cell Biol , vol.109 , pp. 487-493
    • Hwang, S.1    Jascur, T.2    Vestweber, D.3    Pon, L.4    Schatz, G.5
  • 14
    • 4444290664 scopus 로고    scopus 로고
    • Two novel proteins in the mitochondrial outer membrane mediate β-barrel protein assembly
    • Ishikawa, D., H. Yamamoto, Y. Tamura, K. Moritoh, and T. Endo. 2004. Two novel proteins in the mitochondrial outer membrane mediate β-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
  • 16
  • 19
    • 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., V. Kozjak, N. Wiedemann, C. Lohaus, H.E. Meyer, B. Guiard, N. Pfanner, and C. Meisinger. 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    Guiard, B.6    Pfanner, N.7    Meisinger, C.8
  • 23
    • 25144452723 scopus 로고    scopus 로고
    • Biogenesis of beta-barrel membrane proteins of mitochondria
    • Paschen, S.A., W. Neupert, and D. Rapaport. 2005. Biogenesis of beta-barrel membrane proteins of mitochondria. Trends Biochem. Sci. 30:575-582.
    • (2005) Trends Biochem. Sci , vol.30 , pp. 575-582
    • Paschen, S.A.1    Neupert, W.2    Rapaport, D.3
  • 24
    • 0023403476 scopus 로고
    • High-affinity binding sites involved in the import of porin into mitochondria
    • Pfaller, R., and W. Neupert. 1987. High-affinity binding sites involved in the import of porin into mitochondria. EMBO J. 6:2635-2642.
    • (1987) EMBO J , vol.6 , pp. 2635-2642
    • Pfaller, R.1    Neupert, W.2
  • 25
    • 0021930556 scopus 로고
    • A water-soluble form of porin from the mitochondrial outer membrane of Neurospora crassa
    • Pfaller, R., H. Freitag, M. Harmey, R. Benz, and W. Neupert. 1985. A water-soluble form of porin from the mitochondrial outer membrane of Neurospora crassa. J. Biol. Chem. 260:8188-8193.
    • (1985) J. Biol. Chem , vol.260 , pp. 8188-8193
    • Pfaller, R.1    Freitag, H.2    Harmey, M.3    Benz, R.4    Neupert, W.5
  • 26
    • 0024219719 scopus 로고
    • Import pathways of precursor proteins into mitochondria: Multiple receptor sites are followed by a common insertion site
    • Pfaller, R., H.F. Steger, J. Rassow, N. Pfanner, and W. Neupert. 1988. Import pathways of precursor proteins into mitochondria: multiple receptor sites are followed by a common insertion site. J. Cell Biol. 107:2483-2490.
    • (1988) J. Cell Biol , vol.107 , pp. 2483-2490
    • Pfaller, R.1    Steger, H.F.2    Rassow, J.3    Pfanner, N.4    Neupert, W.5
  • 27
    • 0036535035 scopus 로고    scopus 로고
    • Biogenesis of the mitochondrial TOM complex
    • Rapaport, D. 2002. Biogenesis of the mitochondrial TOM complex. Trends Biochem. Sci. 27:191-197.
    • (2002) Trends Biochem. Sci , vol.27 , pp. 191-197
    • Rapaport, D.1
  • 28
    • 0242607644 scopus 로고    scopus 로고
    • How to find the right organelle - targeting signals in mitochondrial outer membrane proteins
    • 4:948-952
    • Rapaport, D. 2003. How to find the right organelle - targeting signals in mitochondrial outer membrane proteins. EMBO Rep. 4:948-952.
    • (2003) EMBO Rep
    • Rapaport, D.1
  • 29
    • 0033606811 scopus 로고    scopus 로고
    • Biogenesis of Tom40, core component of the TOM complex of mitochondria
    • Rapaport, D., and W. Neupert. 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
  • 30
    • 0034756937 scopus 로고    scopus 로고
    • Structural requirements of Tom40 for assembly into preexisting TOM complexes of mitochondria
    • Rapaport, D., R.D. Taylor, M. Kaeser, T. Langer, W. Neupert, and F.E. Nargang. 2001. Structural requirements of Tom40 for assembly into preexisting TOM complexes of mitochondria. Mol. Biol. Cell. 12:1189-1198.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1189-1198
    • Rapaport, D.1    Taylor, R.D.2    Kaeser, M.3    Langer, T.4    Neupert, W.5    Nargang, F.E.6
  • 31
    • 0642377467 scopus 로고    scopus 로고
    • POTRA: A conserved domain in the FtsQ family and a class of beta-barrel outer membrane proteins
    • Sanchez-Pulido, L., D. Devos, S. Genevrois, M. Vicente, and A. Valencia. 2003. POTRA: a conserved domain in the FtsQ family and a class of beta-barrel outer membrane proteins. Trends Biochem. Sci. 28:523-526.
    • (2003) Trends Biochem. Sci , vol.28 , pp. 523-526
    • Sanchez-Pulido, L.1    Devos, D.2    Genevrois, S.3    Vicente, M.4    Valencia, A.5
  • 32
    • 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., W.A. Cramer, and G. von Jagow. 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
  • 33
    • 0033620612 scopus 로고    scopus 로고
    • Direct membrane insertion of voltage-dependent anion-selective channel protein catalyzed by mitochondrial Tom20
    • Schleiff, E., J.R. Silvius, and G.C. Shore. 1999. Direct membrane insertion of voltage-dependent anion-selective channel protein catalyzed by mitochondrial Tom20. J. Cell Biol. 145:973-978.
    • (1999) J. Cell Biol , vol.145 , pp. 973-978
    • Schleiff, E.1    Silvius, J.R.2    Shore, G.C.3
  • 34
    • 0037379183 scopus 로고    scopus 로고
    • Prediction of the plant beta-barrel proteome: A case study of the chloroplast outer envelope
    • Schleiff, E., L.A. Eichacker, K. Eckart, T. Becker, O. Mirus, T. Stahl, and J. Soll. 2003. Prediction of the plant beta-barrel proteome: a case study of the chloroplast outer envelope. Protein Sci. 12:748-759.
    • (2003) Protein Sci , vol.12 , pp. 748-759
    • Schleiff, E.1    Eichacker, L.A.2    Eckart, K.3    Becker, T.4    Mirus, O.5    Stahl, T.6    Soll, J.7
  • 37
    • 0028149597 scopus 로고
    • Rupture of the mitochondrial outer membrane impairs porin assembly
    • Smith, M., S. Hicks, K. Baker, and R. MacCauley. 1994. Rupture of the mitochondrial outer membrane impairs porin assembly. J. Biol. Chem. 269:28460-28464.
    • (1994) J. Biol. Chem , vol.269 , pp. 28460-28464
    • Smith, M.1    Hicks, S.2    Baker, K.3    MacCauley, R.4
  • 38
    • 0028024592 scopus 로고
    • Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane
    • Sogo, L.F., and M.P. Yaffe. 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
  • 40
    • 0037379222 scopus 로고    scopus 로고
    • Mitochondrial protein import: Recognition of internal import signals of BCS1 by the TOM complex
    • Stan, T., J. Brix, J. Schneider-Mergener, N. Pfanner, W. Neupert, and D. Rapaport. 2003. Mitochondrial protein import: recognition of internal import signals of BCS1 by the TOM complex. Mol. Cell. Biol. 23:2239-2250.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 2239-2250
    • Stan, T.1    Brix, J.2    Schneider-Mergener, J.3    Pfanner, N.4    Neupert, W.5    Rapaport, D.6
  • 41
    • 0035980137 scopus 로고    scopus 로고
    • Structure and assembly of β-barrel membrane proteins
    • Tamm, L.K., A. Arora, and J.H. Kleinschmidt. 2001. Structure and assembly of β-barrel membrane proteins. J. Biol. Chem. 276:32399-32402.
    • (2001) J. Biol. Chem , vol.276 , pp. 32399-32402
    • Tamm, L.K.1    Arora, A.2    Kleinschmidt, J.H.3
  • 42
    • 1842471109 scopus 로고    scopus 로고
    • Omp85, an evolutionarily conserved bacterial protein involved in outer-membrane-protein assembly
    • Voulhoux, R., and J. Tommassen. 2004. Omp85, an evolutionarily conserved bacterial protein involved in outer-membrane-protein assembly. Res. Microbiol. 155:129-135.
    • (2004) Res. Microbiol , vol.155 , pp. 129-135
    • Voulhoux, R.1    Tommassen, J.2
  • 43
    • 0037428132 scopus 로고    scopus 로고
    • Role of a highly conserved bacterial protein in outer membrane protein assembly
    • Voulhoux, R., M.P. Bos, J. Geurtsen, M. Mols, and J. Tommassen. 2003. Role of a highly conserved bacterial protein in outer membrane protein assembly. Science. 299:262-265.
    • (2003) Science , vol.299 , pp. 262-265
    • Voulhoux, R.1    Bos, M.P.2    Geurtsen, J.3    Mols, M.4    Tommassen, J.5
  • 46
    • 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., K.N. Truscott, S. Pfannschmidt, B. Guiard, C. Meisinger, and N. Pfanner. 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    Pfanner, N.6
  • 47
    • 0041428149 scopus 로고    scopus 로고
    • The versatile beta-barrel membrane protein
    • Wimley, W.C. 2003. The versatile beta-barrel membrane protein. Curr. Opin. Struct. Biol. 13:404-411.
    • (2003) Curr. Opin. Struct. Biol , vol.13 , pp. 404-411
    • Wimley, W.C.1
  • 48
    • 17444381980 scopus 로고    scopus 로고
    • Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli
    • Wu, T., J. Malinverni, N. Ruiz, S. Kim, T.J. Silhavy, and D. Kahne. 2005. Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli. Cell. 121:235-245.
    • (2005) Cell , vol.121 , pp. 235-245
    • Wu, T.1    Malinverni, J.2    Ruiz, N.3    Kim, S.4    Silhavy, T.J.5    Kahne, D.6


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