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Volumn 268, Issue , 2008, Pages 147-190

Chapter 5 New Insights into the Mechanism of Precursor Protein Insertion into the Mitochondrial Membranes

Author keywords

Membrane insertion; Mitochondria; Oxa1; Protein import; TIM complex; TOB SAM complex; TOM complex

Indexed keywords

MEMBRANE PROTEIN; MITOCHONDRIAL PROTEIN; OUTER MEMBRANE PROTEIN; PROTEIN PRECURSOR; CARRIER PROTEIN; MULTIPROTEIN COMPLEX; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 52049121909     PISSN: 19376448     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1937-6448(08)00805-8     Document Type: Review
Times cited : (14)

References (218)
  • 1
    • 0033615958 scopus 로고    scopus 로고
    • The TOM core complex: The general protein import pore of the outer membrane of mitochondria
    • Ahting U., Thun C., Hegerl R., Typke D., Nargang F.E., Neupert W., and Nussberger S. The TOM core complex: The general protein import pore of the outer membrane of mitochondria. J. Cell Biol. 147 (2006) 959-968
    • (2006) J. Cell Biol. , vol.147 , pp. 959-968
    • Ahting, U.1    Thun, C.2    Hegerl, R.3    Typke, D.4    Nargang, F.E.5    Neupert, W.6    Nussberger, S.7
  • 2
    • 0035844870 scopus 로고    scopus 로고
    • Tom40, the pore-forming component of the protein-conducting TOM channel in the outer membrane of mitochondria
    • Ahting U., Thieffry M., Engelhardt H., Hegerl R., Neupert W., and Nussberger S. Tom40, the pore-forming component of the protein-conducting TOM channel in the outer membrane of mitochondria. J. Cell Biol. 153 (2001) 1151-1160
    • (2001) J. Cell Biol. , vol.153 , pp. 1151-1160
    • Ahting, U.1    Thieffry, M.2    Engelhardt, H.3    Hegerl, R.4    Neupert, W.5    Nussberger, S.6
  • 3
    • 0028862969 scopus 로고
    • The mitochondrial receptor complex: The small subunit Mom8b/Isp6 supports association of receptors with the general insertion pore and transfer of preproteins
    • Alconada A., Kübrich M., Moczko M., Hönlinger A., and Pfanner N. The mitochondrial receptor complex: The small subunit Mom8b/Isp6 supports association of receptors with the general insertion pore and transfer of preproteins. Mol. Cell. Biol. 15 (1995) 6196-6205
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6196-6205
    • Alconada, A.1    Kübrich, M.2    Moczko, M.3    Hönlinger, A.4    Pfanner, N.5
  • 4
    • 0037070570 scopus 로고    scopus 로고
    • A conserved proline residue is present in the transmembrane-spanning domain of Tom7 and other tail-anchored protein subunits of the TOM translocase
    • Allen R., Egan B., Gabriel K., Beilharz T., and Lithgow T. A conserved proline residue is present in the transmembrane-spanning domain of Tom7 and other tail-anchored protein subunits of the TOM translocase. FEBS Lett. 514 (2002) 347-350
    • (2002) FEBS Lett. , vol.514 , pp. 347-350
    • Allen, R.1    Egan, B.2    Gabriel, K.3    Beilharz, T.4    Lithgow, T.5
  • 5
    • 0345467690 scopus 로고
    • Organisation and expression of the mammalian mitochondrial genome: A lesson in economy
    • 100-103
    • Attardi G. Organisation and expression of the mammalian mitochondrial genome: A lesson in economy. Trends Biochem. Sci. 6 (1981) 86-89 100-103
    • (1981) Trends Biochem. Sci. , vol.6 , pp. 86-89
    • Attardi, G.1
  • 6
    • 0028073024 scopus 로고
    • PET1402, a nuclear gene required for proteolytic processing of cytochrome oxidase subunit 2 in yeast
    • Bauer M., Behrens M., Esser K., Michaelis G., and Pratje E. PET1402, a nuclear gene required for proteolytic processing of cytochrome oxidase subunit 2 in yeast. Mol. Gen. Genet. 245 (1994) 272-278
    • (1994) Mol. Gen. Genet. , vol.245 , pp. 272-278
    • Bauer, M.1    Behrens, M.2    Esser, K.3    Michaelis, G.4    Pratje, E.5
  • 7
    • 0030272378 scopus 로고    scopus 로고
    • Role of Tim23 as voltage sensor and presequence receptor in protein import into mitochondria
    • Bauer M.F., Sirrenberg C., Neupert W., and Brunner M. Role of Tim23 as voltage sensor and presequence receptor in protein import into mitochondria. Cell 87 (1996) 33-41
    • (1996) Cell , vol.87 , pp. 33-41
    • Bauer, M.F.1    Sirrenberg, C.2    Neupert, W.3    Brunner, M.4
  • 8
    • 0037077239 scopus 로고    scopus 로고
    • Insertion of bitopic membrane proteins into the inner membrane of mitochondria involves an export step from the matrix
    • Baumann F., Neupert W., and Herrmann J.M. Insertion of bitopic membrane proteins into the inner membrane of mitochondria involves an export step from the matrix. J. Biol. Chem. 277 (2002) 21405-21413
    • (2002) J. Biol. Chem. , vol.277 , pp. 21405-21413
    • Baumann, F.1    Neupert, W.2    Herrmann, J.M.3
  • 9
    • 0027273423 scopus 로고
    • The signal that sorts yeast cytochrome b2 to the mitochondrial intermembrane space contains three distinct functional regions
    • Beasley E.M., Muller S., and Schatz G. The signal that sorts yeast cytochrome b2 to the mitochondrial intermembrane space contains three distinct functional regions. EMBO J. 12 (1993) 2303-2311
    • (1993) EMBO J. , vol.12 , pp. 2303-2311
    • Beasley, E.M.1    Muller, S.2    Schatz, G.3
  • 10
    • 0037424360 scopus 로고    scopus 로고
    • Bipartite signals mediate subcellular targeting of tail-anchored membrane proteins in Saccharomyces cerevisiae
    • Beilharz T., Egan B., Silver P.A., Hofmann K., and Lithgow T. Bipartite signals mediate subcellular targeting of tail-anchored membrane proteins in Saccharomyces cerevisiae. J. Biol. Chem. 278 (2003) 8219-8223
    • (2003) J. Biol. Chem. , vol.278 , pp. 8219-8223
    • Beilharz, T.1    Egan, B.2    Silver, P.A.3    Hofmann, K.4    Lithgow, T.5
  • 11
    • 0029094657 scopus 로고
    • Functional and physical interactions of components of the yeast mitochondrial inner-membrane import machinery (MIM)
    • Blom J., Dekker P., and Meijer M. Functional and physical interactions of components of the yeast mitochondrial inner-membrane import machinery (MIM). Eur. J. Biochem. 232 (1995) 309-314
    • (1995) Eur. J. Biochem. , vol.232 , pp. 309-314
    • Blom, J.1    Dekker, P.2    Meijer, M.3
  • 13
    • 0028245283 scopus 로고
    • OXA1, a Saccharomyces cerevisiae nuclear gene whose sequence is conserved from prokaryotes to eukaryotes controls cytochrome oxidase biogenesis
    • Bonnefoy N., Chalvet F., Hamel P., Slominski P.P., and Dujardin G. OXA1, a Saccharomyces cerevisiae nuclear gene whose sequence is conserved from prokaryotes to eukaryotes controls cytochrome oxidase biogenesis. J. Mol. Biol. 239 (1994) 201-212
    • (1994) J. Mol. Biol. , vol.239 , pp. 201-212
    • Bonnefoy, N.1    Chalvet, F.2    Hamel, P.3    Slominski, P.P.4    Dujardin, G.5
  • 14
    • 34547937485 scopus 로고    scopus 로고
    • How tails guide tail-anchored proteins to their destinations
    • Borgese N., Brambillasca S., and Colombo S. How tails guide tail-anchored proteins to their destinations. Curr. Opin. Cell Biol. 19 (2007) 368-375
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 368-375
    • Borgese, N.1    Brambillasca, S.2    Colombo, S.3
  • 15
    • 0017340308 scopus 로고
    • Structure and function of mitochondrial DNA
    • Borst P. Structure and function of mitochondrial DNA. Trends Biochem. Sci. 2 (1977) 31-34
    • (1977) Trends Biochem. Sci. , vol.2 , pp. 31-34
    • Borst, P.1
  • 16
    • 0018036479 scopus 로고
    • The mitochondrial genome of yeast
    • Borst P., and Grivell L.A. The mitochondrial genome of yeast. Cell 15 (1978) 705-723
    • (1978) Cell , vol.15 , pp. 705-723
    • Borst, P.1    Grivell, L.A.2
  • 17
    • 14044257286 scopus 로고    scopus 로고
    • The carboxyl-terminal third of the dicarboxylate carrier is crucial for productive association with the inner membrane twin-pore translocase
    • Brandner K., Rehling P., and Truscott K.N. The carboxyl-terminal third of the dicarboxylate carrier is crucial for productive association with the inner membrane twin-pore translocase. J. Biol. Chem. 280 (2005) 6215-6221
    • (2005) J. Biol. Chem. , vol.280 , pp. 6215-6221
    • Brandner, K.1    Rehling, P.2    Truscott, K.N.3
  • 18
    • 0040610676 scopus 로고    scopus 로고
    • Distribution of binding sequences for the mitochondrial import receptors Tom20, Tom22, and Tom70 in a presequence-carrying preprotein and a non-cleavable preprotein
    • Brix J., Rudiger S., Bukau B., Schneider-Mergener J., and Pfanner N. Distribution of binding sequences for the mitochondrial import receptors Tom20, Tom22, and Tom70 in a presequence-carrying preprotein and a non-cleavable preprotein. J. Biol. Chem. 274 (1999) 16522-16530
    • (1999) J. Biol. Chem. , vol.274 , pp. 16522-16530
    • Brix, J.1    Rudiger, S.2    Bukau, B.3    Schneider-Mergener, J.4    Pfanner, N.5
  • 19
    • 0034602242 scopus 로고    scopus 로고
    • The mitochondrial import receptor Tom70: Identification of a 25 kDa core domain with a specific binding site for preproteins
    • Brix J., Ziegler G.A., Dietmeier K., Schneider-Mergener J., Schulz G.E., and Pfanner N. The mitochondrial import receptor Tom70: Identification of a 25 kDa core domain with a specific binding site for preproteins. J. Mol. Biol. 303 (2000) 479-488
    • (2000) J. Mol. Biol. , vol.303 , pp. 479-488
    • Brix, J.1    Ziegler, G.A.2    Dietmeier, K.3    Schneider-Mergener, J.4    Schulz, G.E.5    Pfanner, N.6
  • 20
    • 0142105410 scopus 로고    scopus 로고
    • Mitochondrial translocation contact sites: Separation of dynamic and stabilizing elements in formation of a TOM-TIM-preprotein supercomplex
    • Chacinska A., Rehling P., Guiard B., Frazier A.E., Schulze-Specking A., Pfanner N., Voos W., and Meisinger C. Mitochondrial translocation contact sites: Separation of dynamic and stabilizing elements in formation of a TOM-TIM-preprotein supercomplex. EMBO J. 22 (2003) 5370-5381
    • (2003) EMBO J. , vol.22 , pp. 5370-5381
    • Chacinska, A.1    Rehling, P.2    Guiard, B.3    Frazier, A.E.4    Schulze-Specking, A.5    Pfanner, N.6    Voos, W.7    Meisinger, C.8
  • 22
    • 0028932673 scopus 로고
    • Limitations to in vivo import of hydrophobic proteins into yeast mitochondria-The case of a cytoplasmically synthesized apocytochrome b
    • Claros M.G., Perea J., Shu Y.M., Samatey F.A., Popot J.L., and Jacq C. Limitations to in vivo import of hydrophobic proteins into yeast mitochondria-The case of a cytoplasmically synthesized apocytochrome b. Eur. J. Biochem. 228 (1995) 762-771
    • (1995) Eur. J. Biochem. , vol.228 , pp. 762-771
    • Claros, M.G.1    Perea, J.2    Shu, Y.M.3    Samatey, F.A.4    Popot, J.L.5    Jacq, C.6
  • 23
    • 34247340596 scopus 로고    scopus 로고
    • Ugo1p is a multipass transmembrane protein with a single carrier domain required for mitochondrial fusion
    • Coonrod E.M., Karren M.A., and Shaw J.M. Ugo1p is a multipass transmembrane protein with a single carrier domain required for mitochondrial fusion. Traffic 8 (2007) 500-511
    • (2007) Traffic , vol.8 , pp. 500-511
    • Coonrod, E.M.1    Karren, M.A.2    Shaw, J.M.3
  • 24
    • 0036716281 scopus 로고    scopus 로고
    • The Bcl2 family: Regulators of the cellular life-or-death switch
    • Cory S., and Adams J.M. The Bcl2 family: Regulators of the cellular life-or-death switch. Nat. Rev. Cancer 2 (2002) 647-656
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 647-656
    • Cory, S.1    Adams, J.M.2
  • 25
    • 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., Kleene R., Neupert W., and Lill R. Role of the N- and C-termini of porin in import into the outer membrane of Neurospora mitochondria. FEBS Lett. 390 (1996) 73-77
    • (1996) FEBS Lett. , vol.390 , pp. 73-77
    • Court, D.A.1    Kleene, R.2    Neupert, W.3    Lill, R.4
  • 26
    • 0023182502 scopus 로고
    • SSC1, a member of the 70 kDa heat shock protein multigene family of Saccharomyces cerevisiae, is essential for growth
    • Craig E.A., Kramer J., and Kosic-Smithers J. SSC1, a member of the 70 kDa heat shock protein multigene family of Saccharomyces cerevisiae, is essential for growth. Proc. Natl. Acad. Sci. USA 84 (1987) 4156-4160
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 4156-4160
    • Craig, E.A.1    Kramer, J.2    Kosic-Smithers, J.3
  • 27
    • 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
  • 28
    • 0027536034 scopus 로고
    • The specific subcellular localization of two isoforms of cytochrome b5 suggests novel targeting pathways
    • D'Arrigo A., Manera E., Longhi R., and Borgese N. The specific subcellular localization of two isoforms of cytochrome b5 suggests novel targeting pathways. J. Biol. Chem. 268 (1993) 2802-2808
    • (1993) J. Biol. Chem. , vol.268 , pp. 2802-2808
    • D'Arrigo, A.1    Manera, E.2    Longhi, R.3    Borgese, N.4
  • 29
    • 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
  • 30
    • 0031741738 scopus 로고    scopus 로고
    • Preprotein translocase of the outer mitochondrial membrane: Molecular dissection and assembly of the general import pore complex
    • Dekker P.J., Ryan M.T., Brix J., Müller H., Hönlinger A., and Pfanner N. Preprotein translocase of the outer mitochondrial membrane: Molecular dissection and assembly of the general import pore complex. Mol. Cell Biol. 18 (1998) 6515-6524
    • (1998) Mol. Cell Biol. , vol.18 , pp. 6515-6524
    • Dekker, P.J.1    Ryan, M.T.2    Brix, J.3    Müller, H.4    Hönlinger, A.5    Pfanner, N.6
  • 31
    • 0035947723 scopus 로고    scopus 로고
    • Assembly of Tom6 and Tom7 into the TOM core complex of Neurospora crassa
    • Dembowski M., Kunkele K.P., Nargang F.E., Neupert W., and Rapaport D. Assembly of Tom6 and Tom7 into the TOM core complex of Neurospora crassa. J. Biol. Chem. 276 (2001) 17679-17685
    • (2001) J. Biol. Chem. , vol.276 , pp. 17679-17685
    • Dembowski, M.1    Kunkele, K.P.2    Nargang, F.E.3    Neupert, W.4    Rapaport, D.5
  • 33
    • 0345133332 scopus 로고    scopus 로고
    • J protein cochaperone of the mitochondrial inner membrane required for protein import into the mitochondrial matrix
    • D'Silva P.D., Schilke B., Walter W., Andrew A., and Craig E.A. J protein cochaperone of the mitochondrial inner membrane required for protein import into the mitochondrial matrix. Proc. Natl. Acad. Sci. USA 100 (2003) 13839-13844
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13839-13844
    • D'Silva, P.D.1    Schilke, B.2    Walter, W.3    Andrew, A.4    Craig, E.A.5
  • 34
    • 24644486039 scopus 로고    scopus 로고
    • Role of Pam16's degenerate J domain in protein import across the mitochondrial inner membrane
    • D'Silva P.R., Schilke B., Walter W., and Craig E.A. Role of Pam16's degenerate J domain in protein import across the mitochondrial inner membrane. Proc. Natl. Acad. Sci. USA 102 (2005) 12419-12424
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 12419-12424
    • D'Silva, P.R.1    Schilke, B.2    Walter, W.3    Craig, E.A.4
  • 36
    • 0027162057 scopus 로고
    • MAS6 encodes an essential inner membrane component of the yeast mitochondrial protein import pathway
    • Emtage J.L., and Jensen R.E. MAS6 encodes an essential inner membrane component of the yeast mitochondrial protein import pathway. J. Cell Biol. 122 (1993) 1003-1012
    • (1993) J. Cell Biol. , vol.122 , pp. 1003-1012
    • Emtage, J.L.1    Jensen, R.E.2
  • 37
    • 0033564856 scopus 로고    scopus 로고
    • Transport of the ADP/ATP carrier of mitochondria from the TOM complex to the TIM22.54 complex
    • Endres M., Neupert W., and Brunner M. Transport of the ADP/ATP carrier of mitochondria from the TOM complex to the TIM22.54 complex. EMBO J. 18 (1999) 3214-3221
    • (1999) EMBO J. , vol.18 , pp. 3214-3221
    • Endres, M.1    Neupert, W.2    Brunner, M.3
  • 38
    • 34347337609 scopus 로고    scopus 로고
    • Translocation of mitochondrially synthesized Cox2 domains from the matrix to the intermembrane space
    • Fiumera H.L., Broadley S.A., and Fox T.D. Translocation of mitochondrially synthesized Cox2 domains from the matrix to the intermembrane space. Mol. Cell Biol. 27 (2007) 4664-4673
    • (2007) Mol. Cell Biol. , vol.27 , pp. 4664-4673
    • Fiumera, H.L.1    Broadley, S.A.2    Fox, T.D.3
  • 39
    • 0030042248 scopus 로고    scopus 로고
    • Internal targeting signal of the BCS1 protein: A novel mechanism of import into mitochondria
    • Fölsch H., Guiard B., Neupert W., and Stuart R.A. Internal targeting signal of the BCS1 protein: A novel mechanism of import into mitochondria. EMBO J. 15 (1996) 479-487
    • (1996) EMBO J. , vol.15 , pp. 479-487
    • Fölsch, H.1    Guiard, B.2    Neupert, W.3    Stuart, R.A.4
  • 42
    • 0035911154 scopus 로고    scopus 로고
    • Connection of the mitochondrial outer and inner membranes by Fzo1 is critical for organellar fusion
    • Fritz S., Rapaport D., Klanner E., Neupert W., and Westermann B. Connection of the mitochondrial outer and inner membranes by Fzo1 is critical for organellar fusion. J. Cell Biol. 152 (2001) 683-692
    • (2001) J. Cell Biol. , vol.152 , pp. 683-692
    • Fritz, S.1    Rapaport, D.2    Klanner, E.3    Neupert, W.4    Westermann, B.5
  • 43
    • 1642423514 scopus 로고    scopus 로고
    • The Oxa2 protein of Neurospora crassa plays a critical role in the biogenesis of cytochrome oxidase and defines a ubiquitous subbranch of the Oxa1/YidC/Alb3 protein family
    • Funes S., Nargang F.E., Neupert W., and Herrmann J.M. The Oxa2 protein of Neurospora crassa plays a critical role in the biogenesis of cytochrome oxidase and defines a ubiquitous subbranch of the Oxa1/YidC/Alb3 protein family. Mol. Biol. Cell 15 (2004) 1853-1861
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1853-1861
    • Funes, S.1    Nargang, F.E.2    Neupert, W.3    Herrmann, J.M.4
  • 44
    • 0035153316 scopus 로고    scopus 로고
    • The alpha and the beta: Protein translocation across mitochondrial and plastid outer membranes
    • Gabriel K., Buchanan S.K., and Lithgow T. The alpha and the beta: Protein translocation across mitochondrial and plastid outer membranes. Trends Biochem. Sci. 26 (2001) 36-40
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 36-40
    • Gabriel, K.1    Buchanan, S.K.2    Lithgow, T.3
  • 45
    • 0026609104 scopus 로고
    • The distribution of charged amino acids in mitochondrial inner-membrane proteins suggests different modes of membrane integration for nuclearly and mitochondrially encoded proteins
    • Gavel Y., and von H.G. The distribution of charged amino acids in mitochondrial inner-membrane proteins suggests different modes of membrane integration for nuclearly and mitochondrially encoded proteins. Eur. J. Biochem. 205 (1992) 1207-1215
    • (1992) Eur. J. Biochem. , vol.205 , pp. 1207-1215
    • Gavel, Y.1    von, H.G.2
  • 47
    • 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., and Lithgow T. The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria. J. Cell Biol. 164 (2004) 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
  • 48
    • 28244436432 scopus 로고    scopus 로고
    • Molecular architecture and function of the Omp85 family of proteins
    • Gentle I.E., Burri L., and Lithgow T. Molecular architecture and function of the Omp85 family of proteins. Mol. Microbiol. 58 (2005) 1216-1225
    • (2005) Mol. Microbiol. , vol.58 , pp. 1216-1225
    • Gentle, I.E.1    Burri, L.2    Lithgow, T.3
  • 50
    • 0025317093 scopus 로고
    • Removal of a hydrophobic domain within the mature portion of a mitochondrial inner membrane protein causes its mislocalization to the matrix
    • Glaser S.M., Miller B.R., and Cumsky M.G. Removal of a hydrophobic domain within the mature portion of a mitochondrial inner membrane protein causes its mislocalization to the matrix. Mol. Cell. Biol. 10 (1990) 1873-1881
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1873-1881
    • Glaser, S.M.1    Miller, B.R.2    Cumsky, M.G.3
  • 51
    • 0033525788 scopus 로고    scopus 로고
    • Mitochondrial evolution
    • Gray M.W., Burger G., and Lang B.F. Mitochondrial evolution. Science 283 (1999) 1476-1481
    • (1999) Science , vol.283 , pp. 1476-1481
    • Gray, M.W.1    Burger, G.2    Lang, B.F.3
  • 53
    • 34147113774 scopus 로고    scopus 로고
    • Analysis and prediction of mitochondrial targeting signals
    • Habib S.J., Neupert W., and Rapaport D. Analysis and prediction of mitochondrial targeting signals. Methods Cell Biol. 80 (2007) 761-781
    • (2007) Methods Cell Biol. , vol.80 , pp. 761-781
    • Habib, S.J.1    Neupert, W.2    Rapaport, D.3
  • 54
    • 0027940215 scopus 로고
    • Incomplete arrest in the outer membrane sorts NADH-cytochrome b5 reductase to two different submitochondrial compartments
    • Hahne K., Haucke V., Ramage L., and Schatz G. Incomplete arrest in the outer membrane sorts NADH-cytochrome b5 reductase to two different submitochondrial compartments. Cell 79 (1994) 829-839
    • (1994) Cell , vol.79 , pp. 829-839
    • Hahne, K.1    Haucke, V.2    Ramage, L.3    Schatz, G.4
  • 55
    • 0024085635 scopus 로고
    • Both amino- and carboxyterminal portions are required for insertion of yeast porin into the outer mitochondrial membrane
    • Hamajima S., Sakagushi M., Mihara K., Ono S., and Sato R. Both amino- and carboxyterminal portions are required for insertion of yeast porin into the outer mitochondrial membrane. J. Biochem. 104 (1988) 362-367
    • (1988) J. Biochem. , vol.104 , pp. 362-367
    • Hamajima, S.1    Sakagushi, M.2    Mihara, K.3    Ono, S.4    Sato, R.5
  • 57
    • 0028316039 scopus 로고
    • A crucial role of the mitochondrial protein import receptor MOM19 for the biogenesis of mitochondria
    • Harkness T.A., Nargang F.E., van der Klei I., Neupert W., and Lill R. A crucial role of the mitochondrial protein import receptor MOM19 for the biogenesis of mitochondria. J. Cell Biol. 124 (1994) 637-648
    • (1994) J. Cell Biol. , vol.124 , pp. 637-648
    • Harkness, T.A.1    Nargang, F.E.2    van der Klei, I.3    Neupert, W.4    Lill, R.5
  • 58
    • 0022895277 scopus 로고
    • Transport into mitochondria and intramitochondrial sorting of the Fe/S protein of ubiquinol-cytochrome c reductase
    • Hartl F.U., Schmidt B., Wachter E., Weiss H., and Neupert W. Transport into mitochondria and intramitochondrial sorting of the Fe/S protein of ubiquinol-cytochrome c reductase. Cell 47 (1986) 939-951
    • (1986) Cell , vol.47 , pp. 939-951
    • Hartl, F.U.1    Schmidt, B.2    Wachter, E.3    Weiss, H.4    Neupert, W.5
  • 59
    • 0030952628 scopus 로고    scopus 로고
    • Membrane translocation of mitochondrially coded Cox2p: Distinct requirements for export of N and C termini and dependence on the conserved protein Oxa1p
    • He S., and Fox T.D. Membrane translocation of mitochondrially coded Cox2p: Distinct requirements for export of N and C termini and dependence on the conserved protein Oxa1p. Mol. Biol. Cell 8 (1997) 1449-1460
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1449-1460
    • He, S.1    Fox, T.D.2
  • 60
    • 0030656514 scopus 로고    scopus 로고
    • Oxa1p mediates the export of the N- and C-termini of pCoxII from the mitochondrial matrix to the intermembrane space
    • Hell K., Herrmann J., Pratje E., Neupert W., and Stuart R.A. Oxa1p mediates the export of the N- and C-termini of pCoxII from the mitochondrial matrix to the intermembrane space. FEBS Lett. 418 (1997) 367-370
    • (1997) FEBS Lett. , vol.418 , pp. 367-370
    • Hell, K.1    Herrmann, J.2    Pratje, E.3    Neupert, W.4    Stuart, R.A.5
  • 61
    • 0032478139 scopus 로고    scopus 로고
    • Oxa1p, an essential component of the N-tail protein export machinery in mitochondria
    • Hell K., Herrmann J.M., Pratje E., Neupert W., and Stuart R.A. Oxa1p, an essential component of the N-tail protein export machinery in mitochondria. Proc. Natl. Acad. Sci. USA 95 (1998) 2250-2255
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2250-2255
    • Hell, K.1    Herrmann, J.M.2    Pratje, E.3    Neupert, W.4    Stuart, R.A.5
  • 62
    • 0035868763 scopus 로고    scopus 로고
    • Oxa1p acts as a general membrane insertion machinery for proteins encoded by mitochondrial DNA
    • Hell K., Neupert W., and Stuart R.A. Oxa1p acts as a general membrane insertion machinery for proteins encoded by mitochondrial DNA. EMBO J. 20 (2001) 1281-1288
    • (2001) EMBO J. , vol.20 , pp. 1281-1288
    • Hell, K.1    Neupert, W.2    Stuart, R.A.3
  • 63
    • 1642535436 scopus 로고    scopus 로고
    • Protein export across the inner membrane of mitochondria: The nature of translocated domains determines the dependence on the Oxa1 translocase
    • Herrmann J.M., and Bonnefoy N. Protein export across the inner membrane of mitochondria: The nature of translocated domains determines the dependence on the Oxa1 translocase. J. Biol. Chem. 279 (2004) 2507-2512
    • (2004) J. Biol. Chem. , vol.279 , pp. 2507-2512
    • Herrmann, J.M.1    Bonnefoy, N.2
  • 64
    • 0028866982 scopus 로고
    • Topogenesis of cytochrome oxidase subunit II-Mechanisms of protein export from the mitochondrial matrix
    • Herrmann J.M., Koll H., Cook R.A., Neupert W., and Stuart R.A. Topogenesis of cytochrome oxidase subunit II-Mechanisms of protein export from the mitochondrial matrix. J. Biol. Chem. 270 (1995) 27079-27086
    • (1995) J. Biol. Chem. , vol.270 , pp. 27079-27086
    • Herrmann, J.M.1    Koll, H.2    Cook, R.A.3    Neupert, W.4    Stuart, R.A.5
  • 65
    • 0030908894 scopus 로고    scopus 로고
    • Insertion into the mitochondrial inner membrane of a polytopic protein, the nuclear encoded Oxa1p
    • Herrmann J.M., Neupert W., and Stuart R.A. Insertion into the mitochondrial inner membrane of a polytopic protein, the nuclear encoded Oxa1p. EMBO J. 16 (1997) 2217-2226
    • (1997) EMBO J. , vol.16 , pp. 2217-2226
    • Herrmann, J.M.1    Neupert, W.2    Stuart, R.A.3
  • 66
    • 4944228608 scopus 로고    scopus 로고
    • Topogenesis of membrane proteins at the endoplasmic reticulum
    • Higy M., Junne T., and Spiess M. Topogenesis of membrane proteins at the endoplasmic reticulum. Biochemistry 43 (2004) 12716-12722
    • (2004) Biochemistry , vol.43 , pp. 12716-12722
    • Higy, M.1    Junne, T.2    Spiess, M.3
  • 67
    • 0032188847 scopus 로고    scopus 로고
    • Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins
    • Hill K., Model K., Ryan M.T., Dietmeier K., Martin F., Wagner R., and Pfanner N. Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins. Nature 395 (1998) 516-521
    • (1998) Nature , vol.395 , pp. 516-521
    • Hill, K.1    Model, K.2    Ryan, M.T.3    Dietmeier, K.4    Martin, F.5    Wagner, R.6    Pfanner, N.7
  • 68
    • 0029927409 scopus 로고    scopus 로고
    • Tom7 modulates the dynamics of the mitochondrial outer membrane translocase and plays a pathway-related role in protein import
    • Honlinger A., Bomer U., Alconada A., Eckerskorn C., Lottspeich F., Dietmeier K., and Pfanner N. Tom7 modulates the dynamics of the mitochondrial outer membrane translocase and plays a pathway-related role in protein import. EMBO J. 15 (1996) 2125-2137
    • (1996) EMBO J. , vol.15 , pp. 2125-2137
    • Honlinger, A.1    Bomer, U.2    Alconada, A.3    Eckerskorn, C.4    Lottspeich, F.5    Dietmeier, K.6    Pfanner, N.7
  • 69
    • 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
  • 70
    • 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 beta-barrel proteins into the outer mitochondrial membrane
    • Hoppins S.C., Go N.E., Klein A., Schmitt S., Neupert W., Rapaport D., and Nargang F.E. Alternative splicing gives rise to different isoforms of the Neurospora crassa Tob55 protein that vary in their ability to insert beta-barrel proteins into the outer mitochondrial membrane. Genetics 177 (2007) 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    Rapaport, D.6    Nargang, F.E.7
  • 72
    • 0035816591 scopus 로고    scopus 로고
    • Insertion of mitochondrial DNA-encoded F1F0-ATPase subunit 8 across the mitochondrial inner membrane in vitro
    • Ii M., and Mihara K. Insertion of mitochondrial DNA-encoded F1F0-ATPase subunit 8 across the mitochondrial inner membrane in vitro. J. Biol. Chem. 276 (2001) 24704-24712
    • (2001) J. Biol. Chem. , vol.276 , pp. 24704-24712
    • Ii, M.1    Mihara, K.2
  • 73
    • 0028137887 scopus 로고
    • YGE1 is a yeast homologue of Escherichia coli grpE and is required for maintenance of mitochondrial functions
    • [published erratum appears in
    • Ikeda E., Yoshida S., Mitsuzawa H., Uno I., and Toh-e A. YGE1 is a yeast homologue of Escherichia coli grpE and is required for maintenance of mitochondrial functions. FEBS Lett. 339 (1994) 265-268 [published erratum appears in
    • (1994) FEBS Lett. , vol.339 , pp. 265-268
    • Ikeda, E.1    Yoshida, S.2    Mitsuzawa, H.3    Uno, I.4    Toh-e, A.5
  • 74
    • 0028207649 scopus 로고
    • YGE1 is a yeast homologue of Escherichia coli grpE and is required for maintenance of mitochondrial functions
    • Ikeda E., Yoshida S., Mitsuzawa H., Uno I., and Toh-e A. YGE1 is a yeast homologue of Escherichia coli grpE and is required for maintenance of mitochondrial functions. FEBS Lett 343 2 (1994 Apr 25) 181
    • (1994) FEBS Lett , vol.343 , Issue.2 , pp. 181
    • Ikeda, E.1    Yoshida, S.2    Mitsuzawa, H.3    Uno, I.4    Toh-e, A.5
  • 75
    • 0031871330 scopus 로고    scopus 로고
    • A splice isoform of vesicle-associated membrane protein-1 (VAMP-1) contains a mitochondrial targeting signal
    • Isenmann S., Khew-Goodall Y., Gamble J., Vadas M., and Wattenberg B.W. A splice isoform of vesicle-associated membrane protein-1 (VAMP-1) contains a mitochondrial targeting signal. Mol. Biol. Cell 9 (1998) 1649-1660
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1649-1660
    • Isenmann, S.1    Khew-Goodall, Y.2    Gamble, J.3    Vadas, M.4    Wattenberg, B.W.5
  • 76
    • 4444290664 scopus 로고    scopus 로고
    • Two novel proteins in the mitochondrial outer membrane mediate beta-barrel protein assembly
    • Ishikawa D., Yamamoto H., Tamura Y., Moritoh K., and Endo T. Two novel proteins in the mitochondrial outer membrane mediate beta-barrel protein assembly. J. Cell Biol. 166 (2004) 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
  • 77
    • 0348136787 scopus 로고    scopus 로고
    • Yeast Oxa1 interacts with mitochondrial ribosomes: The importance of the C-terminal hydrophilic region of Oxa1
    • Jia L., Dienhart M., Schramp M., McCauley M., Hell K., and Stuart R.A. Yeast Oxa1 interacts with mitochondrial ribosomes: The importance of the C-terminal hydrophilic region of Oxa1. EMBO J. 22 (2003) 6438-6447
    • (2003) EMBO J. , vol.22 , pp. 6438-6447
    • Jia, L.1    Dienhart, M.2    Schramp, M.3    McCauley, M.4    Hell, K.5    Stuart, R.A.6
  • 78
    • 34248138912 scopus 로고    scopus 로고
    • Oxa1 directly interacts with Atp9 and mediates its assembly into the mitochondrial F1Fo-ATP synthase complex
    • Jia L., Dienhart M.K., and Stuart R.A. Oxa1 directly interacts with Atp9 and mediates its assembly into the mitochondrial F1Fo-ATP synthase complex. Mol. Biol. Cell 18 (2007) 1897-1908
    • (2007) Mol. Biol. Cell , vol.18 , pp. 1897-1908
    • Jia, L.1    Dienhart, M.K.2    Stuart, R.A.3
  • 79
    • 0034675885 scopus 로고    scopus 로고
    • Characterization of the signal that directs Tom20 to the mitochondrial outer membrane
    • Kanaji S., Iwahashi J., Kida Y., Sakaguchi M., and Mihara K. Characterization of the signal that directs Tom20 to the mitochondrial outer membrane. J. Cell Biol. 151 (2000) 277-288
    • (2000) J. Cell Biol. , vol.151 , pp. 277-288
    • Kanaji, S.1    Iwahashi, J.2    Kida, Y.3    Sakaguchi, M.4    Mihara, K.5
  • 80
    • 0025039149 scopus 로고
    • Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins
    • Kang P.J., Ostermann J., Shilling J., Neupert W., Craig E.A., and Pfanner N. Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins. Nature 348 (1990) 137-143
    • (1990) Nature , vol.348 , pp. 137-143
    • Kang, P.J.1    Ostermann, J.2    Shilling, J.3    Neupert, W.4    Craig, E.A.5    Pfanner, N.6
  • 81
    • 0027317448 scopus 로고
    • Biogenesis of the mitochondrial receptor complex. Two receptors are required for binding of MOM38 to the outer membrane surface
    • Keil P., Weinzierl A., Kiebler M., Dietmeier K., Sollner T., and Pfanner N. Biogenesis of the mitochondrial receptor complex. Two receptors are required for binding of MOM38 to the outer membrane surface. J. Biol. Chem. 268 (1993) 19177-19180
    • (1993) J. Biol. Chem. , vol.268 , pp. 19177-19180
    • Keil, P.1    Weinzierl, A.2    Kiebler, M.3    Dietmeier, K.4    Sollner, T.5    Pfanner, N.6
  • 82
    • 47649126755 scopus 로고    scopus 로고
    • The integration of tail-anchored proteins into the mitochondrial outer membrane does not require the known import components
    • doi: 10.1242/jcs.024034
    • Kemper C., Habib S.J., Engl G., Heckmeyer P., Dimmer K.S., and Rapaport D. The integration of tail-anchored proteins into the mitochondrial outer membrane does not require the known import components. doi: 10.1242/jcs.024034. J. Cell Sci. (2008)
    • (2008) J. Cell Sci.
    • Kemper, C.1    Habib, S.J.2    Engl, G.3    Heckmeyer, P.4    Dimmer, K.S.5    Rapaport, D.6
  • 83
    • 0031408095 scopus 로고    scopus 로고
    • The Tim54p-Tim22p complex mediates insertion of proteins into the mitochondrial inner membrane
    • Kerscher O., Holder J., Srinivasan M., Leung R.S., and Jensen R.E. The Tim54p-Tim22p complex mediates insertion of proteins into the mitochondrial inner membrane. J. Cell Biol. 139 (1997) 1663-1675
    • (1997) J. Cell Biol. , vol.139 , pp. 1663-1675
    • Kerscher, O.1    Holder, J.2    Srinivasan, M.3    Leung, R.S.4    Jensen, R.E.5
  • 84
    • 0033963688 scopus 로고    scopus 로고
    • Tim18p is a new component of the Tim54p-Tim22p translocon in the mitochondrial inner membrane
    • Kerscher O., Sepuri N.B., and Jensen R.E. Tim18p is a new component of the Tim54p-Tim22p translocon in the mitochondrial inner membrane. Mol. Biol. Cell. 11 (2000) 103-116
    • (2000) Mol. Biol. Cell. , vol.11 , pp. 103-116
    • Kerscher, O.1    Sepuri, N.B.2    Jensen, R.E.3
  • 85
    • 18944364732 scopus 로고    scopus 로고
    • Evidence for the association of yeast mitochondrial ribosomes with Cox11p, a protein required for the Cu(B) site formation of cytochrome c oxidase
    • Khalimonchuk O., Ostermann K., and Rödel G. Evidence for the association of yeast mitochondrial ribosomes with Cox11p, a protein required for the Cu(B) site formation of cytochrome c oxidase. Curr. Genet. 47 (2005) 223-233
    • (2005) Curr. Genet. , vol.47 , pp. 223-233
    • Khalimonchuk, O.1    Ostermann, K.2    Rödel, G.3
  • 86
    • 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
  • 87
    • 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
  • 88
    • 0033978123 scopus 로고    scopus 로고
    • Tim18p, a new subunit of the TIM22 complex that mediates insertion of imported proteins into the yeast mitochondrial inner membrane
    • Koehler C.M., Murphy M.P., Bally N.A., Leuenberger D., Oppliger W., Dolfini L., Junne T., Schatz G., and Or E. Tim18p, a new subunit of the TIM22 complex that mediates insertion of imported proteins into the yeast mitochondrial inner membrane. Mol. Cell Biol. 20 (2000) 1187-1193
    • (2000) Mol. Cell Biol. , vol.20 , pp. 1187-1193
    • Koehler, C.M.1    Murphy, M.P.2    Bally, N.A.3    Leuenberger, D.4    Oppliger, W.5    Dolfini, L.6    Junne, T.7    Schatz, G.8    Or, E.9
  • 90
    • 1442335996 scopus 로고    scopus 로고
    • The J domain-related cochaperone Tim16 is a constituent of the mitochondrial TIM23 preprotein translocase
    • Kozany C., Mokranjac D., Sichting M., Neupert W., and Hell K. The J domain-related cochaperone Tim16 is a constituent of the mitochondrial TIM23 preprotein translocase. Nat. Struct. Mol. Biol. 11 (2004) 234-241
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 234-241
    • Kozany, C.1    Mokranjac, D.2    Sichting, M.3    Neupert, W.4    Hell, K.5
  • 94
    • 0028356858 scopus 로고
    • A role for a eukaryotic GrpE-related protein, Mge1p, in protein translocation
    • Laloraya S., Gambill B.D., and Craig E.A. A role for a eukaryotic GrpE-related protein, Mge1p, in protein translocation. Proc. Natl. Acad. Sci. USA 91 (1994) 6481-6485
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6481-6485
    • Laloraya, S.1    Gambill, B.D.2    Craig, E.A.3
  • 95
    • 0034661510 scopus 로고    scopus 로고
    • Targeting and insertion of C-terminally anchored proteins to the mitochondrial outer membrane is specific and saturable but does not strictly require ATP or molecular chaperones
    • Lan L., Isenmann S., and Wattenberg B.W. Targeting and insertion of C-terminally anchored proteins to the mitochondrial outer membrane is specific and saturable but does not strictly require ATP or molecular chaperones. Biochem. J. 349 (2000) 611-621
    • (2000) Biochem. J. , vol.349 , pp. 611-621
    • Lan, L.1    Isenmann, S.2    Wattenberg, B.W.3
  • 97
    • 0034604519 scopus 로고    scopus 로고
    • 0-ATPase subunit accumulation in an oxa1 deletion mutant of Saccharomyces cerevisiae
    • 0-ATPase subunit accumulation in an oxa1 deletion mutant of Saccharomyces cerevisiae. J. Biol. Chem. 275 (2000) 23471-23475
    • (2000) J. Biol. Chem. , vol.275 , pp. 23471-23475
    • Lemaire, C.1    Hamel, P.2    Velours, J.3    Dujardin, G.4
  • 98
    • 9144265611 scopus 로고    scopus 로고
    • A yeast mitochondrial membrane methyltransferase-like protein can compensate for oxa1 mutations
    • Lemaire C., Guibet-Grandmougin F., Angles D., Dujardin G., and Bonnefoy N. A yeast mitochondrial membrane methyltransferase-like protein can compensate for oxa1 mutations. J. Biol. Chem. 279 (2004) 47464-47472
    • (2004) J. Biol. Chem. , vol.279 , pp. 47464-47472
    • Lemaire, C.1    Guibet-Grandmougin, F.2    Angles, D.3    Dujardin, G.4    Bonnefoy, N.5
  • 100
    • 0030968336 scopus 로고    scopus 로고
    • Tim23, a protein import component of the mitochondrial inner membrane, is required for normal activity of the multiple conductance channel, MCC
    • Lohret T.A., Jensen R.E., and Kinnally K.W. Tim23, a protein import component of the mitochondrial inner membrane, is required for normal activity of the multiple conductance channel, MCC. J. Cell Biol. 137 (1997) 377-386
    • (1997) J. Cell Biol. , vol.137 , pp. 377-386
    • Lohret, T.A.1    Jensen, R.E.2    Kinnally, K.W.3
  • 101
    • 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
  • 102
    • 0026657841 scopus 로고
    • MPI1, an essential gene encoding a mitochondrial membrane protein, is possibly involved in protein import into yeast mitochondria
    • Maarse A.C., Blom J., Grivell L.A., and Meijer M. MPI1, an essential gene encoding a mitochondrial membrane protein, is possibly involved in protein import into yeast mitochondria. EMBO J. 11 (1992) 3619-3628
    • (1992) EMBO J. , vol.11 , pp. 3619-3628
    • Maarse, A.C.1    Blom, J.2    Grivell, L.A.3    Meijer, M.4
  • 103
    • 0027934739 scopus 로고
    • Identification of the essential yeast protein MIM17, an integral mitochondrial inner membrane protein involved in protein import
    • Maarse A.C., Blom J., Keil P., Pfanner N., and Meijer M. Identification of the essential yeast protein MIM17, an integral mitochondrial inner membrane protein involved in protein import. FEBS Lett. 349 (1994) 215-221
    • (1994) FEBS Lett. , vol.349 , pp. 215-221
    • Maarse, A.C.1    Blom, J.2    Keil, P.3    Pfanner, N.4    Meijer, M.5
  • 104
    • 0029971312 scopus 로고    scopus 로고
    • Detection of likely beta-strand regions in sequences of mitochondrial pore proteins using the Gibbs sampler
    • Mannella C., Neuwald A., and Lawrence C. Detection of likely beta-strand regions in sequences of mitochondrial pore proteins using the Gibbs sampler. J. Bioenerg. Biomembr. 28 (1996) 163-169
    • (1996) J. Bioenerg. Biomembr. , vol.28 , pp. 163-169
    • Mannella, C.1    Neuwald, A.2    Lawrence, C.3
  • 105
    • 0026070260 scopus 로고
    • Sequential action of mitochondrial chaperones in protein import into the matrix
    • Manning-Krieg U.C., Scherer P.E., and Schatz G. Sequential action of mitochondrial chaperones in protein import into the matrix. EMBO J. 10 (1991) 3273-3280
    • (1991) EMBO J. , vol.10 , pp. 3273-3280
    • Manning-Krieg, U.C.1    Scherer, P.E.2    Schatz, G.3
  • 106
    • 33947509012 scopus 로고    scopus 로고
    • Tim17p regulates the twin pore structure and voltage gating of the mitochondrial protein import complex TIM23
    • Martinez-Caballero S., Grigoriev S.M., Herrmann J.M., Campo M.L., and Kinnally K.W. Tim17p regulates the twin pore structure and voltage gating of the mitochondrial protein import complex TIM23. J. Biol. Chem. 282 (2007) 3584-3593
    • (2007) J. Biol. Chem. , vol.282 , pp. 3584-3593
    • Martinez-Caballero, S.1    Grigoriev, S.M.2    Herrmann, J.M.3    Campo, M.L.4    Kinnally, K.W.5
  • 107
    • 0027049521 scopus 로고
    • A signal-anchor sequence selective for the mitochondrial outer membrane
    • McBride H.M., Millar D.G., Li J.M., and Shore G.C. A signal-anchor sequence selective for the mitochondrial outer membrane. J. Cell Biol. 119 (1992) 1451-1457
    • (1992) J. Cell Biol. , vol.119 , pp. 1451-1457
    • McBride, H.M.1    Millar, D.G.2    Li, J.M.3    Shore, G.C.4
  • 108
    • 33845992498 scopus 로고    scopus 로고
    • Expanding the subproteome of the inner mitochondria using protein separation technologies: One- and two-dimensional liquid chromatography and two-dimensional gel electrophoresis
    • McDonald T., Sheng S., Stanley B., Chen D., Ko Y., Cole R.N., Pedersen P., and Van Eyk J.E. Expanding the subproteome of the inner mitochondria using protein separation technologies: One- and two-dimensional liquid chromatography and two-dimensional gel electrophoresis. Mol. Cell Proteomics 5 (2006) 2392-2411
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 2392-2411
    • McDonald, T.1    Sheng, S.2    Stanley, B.3    Chen, D.4    Ko, Y.5    Cole, R.N.6    Pedersen, P.7    Van Eyk, J.E.8
  • 109
    • 14844334925 scopus 로고    scopus 로고
    • Conserved N-terminal negative charges in the Tim17 subunit of the TIM23 translocase play a critical role in the import of preproteins into mitochondria
    • Meier S., Neupert W., and Herrmann J.M. Conserved N-terminal negative charges in the Tim17 subunit of the TIM23 translocase play a critical role in the import of preproteins into mitochondria. J. Biol. Chem. 280 (2005) 7777-7785
    • (2005) J. Biol. Chem. , vol.280 , pp. 7777-7785
    • Meier, S.1    Neupert, W.2    Herrmann, J.M.3
  • 110
    • 24944483742 scopus 로고    scopus 로고
    • Proline residues of transmembrane domains determine the sorting of inner membrane proteins in mitochondria
    • Meier S., Neupert W., and Herrmann J.M. Proline residues of transmembrane domains determine the sorting of inner membrane proteins in mitochondria. J. Cell Biol. 170 (2005) 881-888
    • (2005) J. Cell Biol. , vol.170 , pp. 881-888
    • Meier, S.1    Neupert, W.2    Herrmann, J.M.3
  • 112
    • 40149096482 scopus 로고    scopus 로고
    • The outer membrane form of the mitochondrial protein Mcr1 follows a TOM-independent membrane insertion pathway
    • Meinecke B., Engl G., Kemper C., Vasiljev-Neumeyer A., Paulitschke H., and Rapaport D. The outer membrane form of the mitochondrial protein Mcr1 follows a TOM-independent membrane insertion pathway. FEBS Lett. 582 (2008) 855-860
    • (2008) FEBS Lett. , vol.582 , pp. 855-860
    • Meinecke, B.1    Engl, G.2    Kemper, C.3    Vasiljev-Neumeyer, A.4    Paulitschke, H.5    Rapaport, D.6
  • 116
    • 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 H.E., Guiard B., Pfanner N., and Meisinger C. Sam35 of the mitochondrial protein sorting and assembly machinery is a peripheral outer membrane protein essential for cell viability. J. Biol. Chem. 279 (2004) 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
  • 118
    • 33749624260 scopus 로고    scopus 로고
    • Recent surprises in protein targeting to mitochondria and plastids
    • Millar A.H., Whelan J., and Small I. Recent surprises in protein targeting to mitochondria and plastids. Curr. Opin. Plant Biol. 9 (2006) 610-615
    • (2006) Curr. Opin. Plant Biol. , vol.9 , pp. 610-615
    • Millar, A.H.1    Whelan, J.2    Small, I.3
  • 119
    • 0027192990 scopus 로고
    • Intramitochondrial sorting of the precursor to yeast cytochrome c oxidase subunit Va
    • Miller B.R., and Cumsky M.G. Intramitochondrial sorting of the precursor to yeast cytochrome c oxidase subunit Va. J. Cell Biol. 121 (1993) 1021-1029
    • (1993) J. Cell Biol. , vol.121 , pp. 1021-1029
    • Miller, B.R.1    Cumsky, M.G.2
  • 121
    • 0036306343 scopus 로고    scopus 로고
    • Protein translocase of the outer mitochondrial membrane: Role of import receptors in the structural organization of the TOM complex
    • Model K., Prinz T., Ruiz T., Radermacher M., Krimmer T., Kuhlbrandt W., Pfanner N., and Meisinger C. Protein translocase of the outer mitochondrial membrane: Role of import receptors in the structural organization of the TOM complex. J. Mol. Biol. 316 (2002) 657-666
    • (2002) J. Mol. Biol. , vol.316 , pp. 657-666
    • Model, K.1    Prinz, T.2    Ruiz, T.3    Radermacher, M.4    Krimmer, T.5    Kuhlbrandt, W.6    Pfanner, N.7    Meisinger, C.8
  • 123
    • 0141865519 scopus 로고    scopus 로고
    • Tim14, a novel key component of the import motor of the TIM23 protein translocase of mitochondria
    • Mokranjac D., Sichting M., Neupert W., and Hell K. Tim14, a novel key component of the import motor of the TIM23 protein translocase of mitochondria. EMBO J. 22 (2003) 4945-4956
    • (2003) EMBO J. , vol.22 , pp. 4945-4956
    • Mokranjac, D.1    Sichting, M.2    Neupert, W.3    Hell, K.4
  • 124
    • 21244458136 scopus 로고    scopus 로고
    • Role of Tim21 in mitochondrial translocation contact sites
    • Mokranjac D., Popov-Celeketic D., Hell K., and Neupert W. Role of Tim21 in mitochondrial translocation contact sites. J. Biol. Chem. 280 (2005) 23437-23440
    • (2005) J. Biol. Chem. , vol.280 , pp. 23437-23440
    • Mokranjac, D.1    Popov-Celeketic, D.2    Hell, K.3    Neupert, W.4
  • 125
    • 33749360278 scopus 로고    scopus 로고
    • Structure and function of Tim14 and Tim16, the J and J-like components of the mitochondrial protein import motor
    • Mokranjac D., Bourenkov G., Hell K., Neupert W., and Groll M. Structure and function of Tim14 and Tim16, the J and J-like components of the mitochondrial protein import motor. EMBO J. 25 (2006) 4675-4685
    • (2006) EMBO J. , vol.25 , pp. 4675-4685
    • Mokranjac, D.1    Bourenkov, G.2    Hell, K.3    Neupert, W.4    Groll, M.5
  • 127
    • 0033168677 scopus 로고    scopus 로고
    • .23 preprotein translocase of mitochondria: Composition and function in protein transport of mitochondria
    • .23 preprotein translocase of mitochondria: Composition and function in protein transport of mitochondria. EMBO J. 18 (1999) 3667-3675
    • (1999) EMBO J. , vol.18 , pp. 3667-3675
    • Moro, F.1    Sirrenberg, C.2    Schneider, H.-C.3    Neupert, W.4    Brunner, M.5
  • 128
    • 0036977273 scopus 로고    scopus 로고
    • Bcl-2 and porin follow different pathways of TOM-dependent insertion into the mitochondrial outer membrane
    • Motz C., Martin H., Krimmer T., and Rassow J. Bcl-2 and porin follow different pathways of TOM-dependent insertion into the mitochondrial outer membrane. J. Mol. Biol. 323 (2002) 729-738
    • (2002) J. Mol. Biol. , vol.323 , pp. 729-738
    • Motz, C.1    Martin, H.2    Krimmer, T.3    Rassow, J.4
  • 129
    • 0034676096 scopus 로고    scopus 로고
    • Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p
    • Mozdy A.D., McCaffery J.M., and Shaw J.M. Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p. J. Cell Biol. 151 (2000) 367-380
    • (2000) J. Cell Biol. , vol.151 , pp. 367-380
    • Mozdy, A.D.1    McCaffery, J.M.2    Shaw, J.M.3
  • 130
    • 0035726162 scopus 로고    scopus 로고
    • The essential function of the small Tim proteins in the TIM22 import pathway does not depend on formation of the soluble 70-kilodalton complex
    • Murphy M.P., Leuenberger D., Curran S.P., Oppliger W., and Koehler C.M. The essential function of the small Tim proteins in the TIM22 import pathway does not depend on formation of the soluble 70-kilodalton complex. Mol. Cell Biol. 21 (2001) 6132-6138
    • (2001) Mol. Cell Biol. , vol.21 , pp. 6132-6138
    • Murphy, M.P.1    Leuenberger, D.2    Curran, S.P.3    Oppliger, W.4    Koehler, C.M.5
  • 131
    • 2442585126 scopus 로고    scopus 로고
    • Role of YidC in folding of polytopic membrane proteins
    • Nagamori S., Smirnova I.N., and Kaback H.R. Role of YidC in folding of polytopic membrane proteins. J. Cell Biol. 165 (2004) 53-62
    • (2004) J. Cell Biol. , vol.165 , pp. 53-62
    • Nagamori, S.1    Smirnova, I.N.2    Kaback, H.R.3
  • 132
    • 0028955901 scopus 로고
    • 'Sheltered disruption' of Neurospora crassa MOM22, an essential component of the mitochondrial protein import complex
    • Nargang F.E., Künkele K.P., Mayer A., Ritzel R.G., Neupert W., and Lill R. 'Sheltered disruption' of Neurospora crassa MOM22, an essential component of the mitochondrial protein import complex. EMBO J. 14 (1995) 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    Lill, R.6
  • 133
    • 0037066703 scopus 로고    scopus 로고
    • The Oxa1 protein forms a homooligomeric complex and is an essential part of the mitochondrial export translocase in Neurospora crassa
    • Nargang F.E., Preuss M., Neupert W., and Herrmann J.M. The Oxa1 protein forms a homooligomeric complex and is an essential part of the mitochondrial export translocase in Neurospora crassa. J. Biol. Chem. 277 (2002) 12846-12853
    • (2002) J. Biol. Chem. , vol.277 , pp. 12846-12853
    • Nargang, F.E.1    Preuss, M.2    Neupert, W.3    Herrmann, J.M.4
  • 134
    • 0033152496 scopus 로고    scopus 로고
    • Recruitment of an alternatively spliced form of synaptojanin 2 to mitochondria by the interaction with the PDZ domain of a mitochondrial outer membrane protein
    • Nemoto Y., and De Camilli P. Recruitment of an alternatively spliced form of synaptojanin 2 to mitochondria by the interaction with the PDZ domain of a mitochondrial outer membrane protein. EMBO J. 18 (1999) 2991-3006
    • (1999) EMBO J. , vol.18 , pp. 2991-3006
    • Nemoto, Y.1    De Camilli, P.2
  • 135
    • 0036343904 scopus 로고    scopus 로고
    • The protein import motor of mitochondria
    • Neupert W., and Brunner M. The protein import motor of mitochondria. Nat. Rev. Mol. Cell Biol. 3 (2002) 555-565
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 555-565
    • Neupert, W.1    Brunner, M.2
  • 136
    • 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
  • 137
    • 0027525536 scopus 로고
    • Targeting of Bcl-2 to the mitochondrial outer membrane by a COOH-terminal signal anchor sequence
    • Nguyen M., Millar D.G., Yong V.W., Korsmeyer S.J., and Shore G.C. Targeting of Bcl-2 to the mitochondrial outer membrane by a COOH-terminal signal anchor sequence. J. Biol. Chem. 268 (1993) 25265-25268
    • (1993) J. Biol. Chem. , vol.268 , pp. 25265-25268
    • Nguyen, M.1    Millar, D.G.2    Yong, V.W.3    Korsmeyer, S.J.4    Shore, G.C.5
  • 141
    • 34547100322 scopus 로고    scopus 로고
    • Awaking TIM22, a dynamic ligand-gated channel for protein insertion in the mitochondrial inner membrane
    • Peixoto P.M., Grana F., Roy T.J., Dunn C.D., Flores M., Jensen R.E., and Campo M.L. Awaking TIM22, a dynamic ligand-gated channel for protein insertion in the mitochondrial inner membrane. J. Biol. Chem. 282 (2007) 18694-18701
    • (2007) J. Biol. Chem. , vol.282 , pp. 18694-18701
    • Peixoto, P.M.1    Grana, F.2    Roy, T.J.3    Dunn, C.D.4    Flores, M.5    Jensen, R.E.6    Campo, M.L.7
  • 142
    • 0035344460 scopus 로고    scopus 로고
    • Versatility of the mitochondrial protein import machinery
    • Pfanner N., and Geissler A. Versatility of the mitochondrial protein import machinery. Nat. Rev. Mol. Cell Biol. 2 (2001) 339-349
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 339-349
    • Pfanner, N.1    Geissler, A.2
  • 144
    • 0035947767 scopus 로고    scopus 로고
    • Mba1, a novel component of the mitochondrial protein export machinery of the yeast Saccharomyces cerevisiae
    • Preuss M., Leonhard K., Hell K., Stuart R.A., Neupert W., and Herrmann J.M. Mba1, a novel component of the mitochondrial protein export machinery of the yeast Saccharomyces cerevisiae. J. Cell Biol. 153 (2001) 1085-1096
    • (2001) J. Cell Biol. , vol.153 , pp. 1085-1096
    • Preuss, M.1    Leonhard, K.2    Hell, K.3    Stuart, R.A.4    Neupert, W.5    Herrmann, J.M.6
  • 145
    • 0036535035 scopus 로고    scopus 로고
    • Biogenesis of the mitochondrial TOM complex
    • Rapaport D. Biogenesis of the mitochondrial TOM complex. Trends Biochem. Sci. 27 (2002) 191-197
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 191-197
    • Rapaport, D.1
  • 146
    • 0242607644 scopus 로고    scopus 로고
    • Finding the right organelle. Targeting signals in mitochondrial outer-membrane proteins
    • Rapaport D. Finding the right organelle. Targeting signals in mitochondrial outer-membrane proteins. EMBO Rep. 4 (2003) 948-952
    • (2003) EMBO Rep. , vol.4 , pp. 948-952
    • Rapaport, D.1
  • 147
    • 0033606811 scopus 로고    scopus 로고
    • Biogenesis of Tom40, core component of the TOM complex in mitochondria
    • Rapaport D., and Neupert W. Biogenesis of Tom40, core component of the TOM complex in mitochondria. J. Cell Biol. 146 (1999) 321-331
    • (1999) J. Cell Biol. , vol.146 , pp. 321-331
    • Rapaport, D.1    Neupert, W.2
  • 149
    • 0037459118 scopus 로고    scopus 로고
    • Insertion of hydrophobic membrane proteins into the inner mitochondrial membrane-A guided tour
    • Rehling P., Pfanner N., and Meisinger C. Insertion of hydrophobic membrane proteins into the inner mitochondrial membrane-A guided tour. J. Mol. Biol. 326 (2003) 639-657
    • (2003) J. Mol. Biol. , vol.326 , pp. 639-657
    • Rehling, P.1    Pfanner, N.2    Meisinger, C.3
  • 151
    • 0030591445 scopus 로고    scopus 로고
    • MBA1 encodes a mitochondrial membrane-associated protein required for biogenesis of the respiratory chain
    • Rep M., and Grivell L.A. MBA1 encodes a mitochondrial membrane-associated protein required for biogenesis of the respiratory chain. FEBS Lett. 388 (1996) 185-188
    • (1996) FEBS Lett. , vol.388 , pp. 185-188
    • Rep, M.1    Grivell, L.A.2
  • 152
    • 0028981021 scopus 로고
    • 0-ATPase subunit 9: Export from matrix requires delta pH across inner membrane and matrix ATP
    • 0-ATPase subunit 9: Export from matrix requires delta pH across inner membrane and matrix ATP. EMBO J. 14 (1995) 3445-3451
    • (1995) EMBO J. , vol.14 , pp. 3445-3451
    • Rojo, E.E.1    Stuart, R.A.2    Neupert, W.3
  • 153
    • 0032478794 scopus 로고    scopus 로고
    • Sorting of D-lactate dehydrogenase to the inner membrane of mitochondria: Analysis of topogenic signal and energetic requirements
    • Rojo E.E., Guiard B., Neupert W., and Stuart R.A. Sorting of D-lactate dehydrogenase to the inner membrane of mitochondria: Analysis of topogenic signal and energetic requirements. J. Biol. Chem. 273 (1998) 8040-8047
    • (1998) J. Biol. Chem. , vol.273 , pp. 8040-8047
    • Rojo, E.E.1    Guiard, B.2    Neupert, W.3    Stuart, R.A.4
  • 154
    • 0033538499 scopus 로고    scopus 로고
    • N-terminal tail export from the mitochondrial matrix. Adherence to the prokaryotic "positive-inside" rule of membane protein topology
    • Rojo E.E., Guiard B., Neupert W., and Stuart R.A. N-terminal tail export from the mitochondrial matrix. Adherence to the prokaryotic "positive-inside" rule of membane protein topology. J. Biol. Chem. 274 (1999) 19617-19622
    • (1999) J. Biol. Chem. , vol.274 , pp. 19617-19622
    • Rojo, E.E.1    Guiard, B.2    Neupert, W.3    Stuart, R.A.4
  • 155
    • 0037089084 scopus 로고    scopus 로고
    • Membrane topology and mitochondrial targeting of mitofusins, ubiquitous mammalian homologs of the transmembrane GTPase Fzo
    • Rojo M., Legros F., Chateau D., and Lombes A. Membrane topology and mitochondrial targeting of mitofusins, ubiquitous mammalian homologs of the transmembrane GTPase Fzo. J. Cell Sci. 115 (2002) 1663-1674
    • (2002) J. Cell Sci. , vol.115 , pp. 1663-1674
    • Rojo, M.1    Legros, F.2    Chateau, D.3    Lombes, A.4
  • 156
    • 0031961784 scopus 로고    scopus 로고
    • Characterisation of the mitochondrial inner membrane translocase complex: The Tim23p hydrophobic domain interacts with Tim17p but not with other Tim23p molecules
    • Ryan K.R., Leung R.S., and Jensen R.J. Characterisation of the mitochondrial inner membrane translocase complex: The Tim23p hydrophobic domain interacts with Tim17p but not with other Tim23p molecules. Mol. Cell. Biol. 18 (1998) 178-187
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 178-187
    • Ryan, K.R.1    Leung, R.S.2    Jensen, R.J.3
  • 157
    • 0035923538 scopus 로고    scopus 로고
    • Role of positively charged transmembrane segments in the insertion and assembly of mitochondrial inner-membrane proteins
    • Saint-Georges Y., Hamel P., Lemaire C., and Dujardin G. Role of positively charged transmembrane segments in the insertion and assembly of mitochondrial inner-membrane proteins. Proc. Natl. Acad. Sci. USA 98 (2001) 13814-13819
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13814-13819
    • Saint-Georges, Y.1    Hamel, P.2    Lemaire, C.3    Dujardin, G.4
  • 158
    • 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., Devos D., Genevrois S., Vicente M., and Valencia A. POTRA: A conserved domain in the FtsQ family and a class of beta-barrel outer membrane proteins. Trends Biochem. Sci. 28 (2003) 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
  • 159
    • 0036223216 scopus 로고    scopus 로고
    • Cox18p is required for export of the mitochondrially encoded Saccharomyces cerevisiae Cox2p C-tail and interacts with Pnt1p and Mss2p in the inner membrane
    • Saracco S.A., and Fox T.D. Cox18p is required for export of the mitochondrially encoded Saccharomyces cerevisiae Cox2p C-tail and interacts with Pnt1p and Mss2p in the inner membrane. Mol. Biol. Cell 13 (2002) 1122-1131
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1122-1131
    • Saracco, S.A.1    Fox, T.D.2
  • 160
    • 0025673942 scopus 로고
    • A precursor protein partly translocated into yeast mitochondria is bound to a 70 kDa mitochondrial stress protein
    • Scherer P.E., Krieg U.C., Hwang S.T., Vestweber D., and Schatz G. A precursor protein partly translocated into yeast mitochondria is bound to a 70 kDa mitochondrial stress protein. EMBO J. 9 (1990) 4315-4322
    • (1990) EMBO J. , vol.9 , pp. 4315-4322
    • Scherer, P.E.1    Krieg, U.C.2    Hwang, S.T.3    Vestweber, D.4    Schatz, G.5
  • 161
    • 0027049693 scopus 로고
    • Identification of a 45-kDa protein at the protein import site of the yeast mitochondrial inner membrane
    • Scherer P.E., Manning K.U., Jeno P., Schatz G., and Horst M. Identification of a 45-kDa protein at the protein import site of the yeast mitochondrial inner membrane. Proc. Natl. Acad. Sci. USA 89 (1992) 11930-11934
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11930-11934
    • Scherer, P.E.1    Manning, K.U.2    Jeno, P.3    Schatz, G.4    Horst, M.5
  • 162
    • 0033620612 scopus 로고    scopus 로고
    • Direct membrane insertion of voltage-dependent anion-selective channel protein catalyzed by mitochondrial Tom20
    • Schleiff E., Silvius J.R., and Shore G.C. Direct membrane insertion of voltage-dependent anion-selective channel protein catalyzed by mitochondrial Tom20. J. Cell Biol. 145 (1999) 973-978
    • (1999) J. Cell Biol. , vol.145 , pp. 973-978
    • Schleiff, E.1    Silvius, J.R.2    Shore, G.C.3
  • 163
    • 0037379183 scopus 로고    scopus 로고
    • Prediction of the plant beta-barrel proteome: A case study of the chloroplast outer envelope
    • Schleiff E., Eichacker L.A., Eckart K., Becker T., Mirus O., Stahl T., and Soll J. Prediction of the plant beta-barrel proteome: A case study of the chloroplast outer envelope. Protein Sci. 12 (2003) 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
  • 164
    • 0028803669 scopus 로고
    • Assembly of the preprotein receptor MOM72/MAS70 into the protein import complex of the outer membrane of mitochondria
    • Schlossmann J., and Neupert W. Assembly of the preprotein receptor MOM72/MAS70 into the protein import complex of the outer membrane of mitochondria. J. Biol. Chem. 270 (1995) 27116-27121
    • (1995) J. Biol. Chem. , vol.270 , pp. 27116-27121
    • Schlossmann, J.1    Neupert, W.2
  • 165
    • 0028365278 scopus 로고
    • Specific recognition of mitochondrial preproteins by the cytosolic domain of the import receptor MOM72
    • Schlossmann J., Dietmeier K., Pfanner N., and Neupert W. Specific recognition of mitochondrial preproteins by the cytosolic domain of the import receptor MOM72. J. Biol. Chem. 269 (1994) 11893-11901
    • (1994) J. Biol. Chem. , vol.269 , pp. 11893-11901
    • Schlossmann, J.1    Dietmeier, K.2    Pfanner, N.3    Neupert, W.4
  • 169
    • 0033539505 scopus 로고    scopus 로고
    • The dimensions of the protein import channels in the outer and inner mitochondrial membranes
    • Schwartz M.P., and Matouschek A. The dimensions of the protein import channels in the outer and inner mitochondrial membranes. Proc. Natl. Acad. Sci. USA 96 (1999) 13086-13090
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13086-13090
    • Schwartz, M.P.1    Matouschek, A.2
  • 171
    • 33845685298 scopus 로고    scopus 로고
    • Cytosolic factor- and TOM-independent import of C-tail-anchored mitochondrial outer membrane proteins
    • Setoguchi K., Otera H., and Mihara K. Cytosolic factor- and TOM-independent import of C-tail-anchored mitochondrial outer membrane proteins. EMBO J. 25 (2006) 5635-5647
    • (2006) EMBO J. , vol.25 , pp. 5635-5647
    • Setoguchi, K.1    Otera, H.2    Mihara, K.3
  • 174
    • 0029827853 scopus 로고    scopus 로고
    • Import of carrier proteins into the mitochondrial inner membrane mediated by Tim22
    • Sirrenberg C., Bauer M.F., Guiard B., Neupert W., and Brunner M. Import of carrier proteins into the mitochondrial inner membrane mediated by Tim22. Nature 384 (1996) 582-585
    • (1996) Nature , vol.384 , pp. 582-585
    • Sirrenberg, C.1    Bauer, M.F.2    Guiard, B.3    Neupert, W.4    Brunner, M.5
  • 175
    • 0032568029 scopus 로고    scopus 로고
    • Carrier protein import into mitochondria mediated by the intermembrane proteins Tim10/Mrs11p and Tim12/Mrs5p
    • Sirrenberg C., Endres M., Fölsch H., Stuart R.A., Neupert W., and Brunner M. Carrier protein import into mitochondria mediated by the intermembrane proteins Tim10/Mrs11p and Tim12/Mrs5p. Nature 391 (1998) 912-915
    • (1998) Nature , vol.391 , pp. 912-915
    • Sirrenberg, C.1    Endres, M.2    Fölsch, H.3    Stuart, R.A.4    Neupert, W.5    Brunner, M.6
  • 176
    • 36349010951 scopus 로고    scopus 로고
    • The interplay between components of the mitochondrial protein translocation motor studied using purified components
    • Slutsky-Leiderman O., Marom M., Iosefson O., Levy R., Maoz S., and Azem A. The interplay between components of the mitochondrial protein translocation motor studied using purified components. J. Biol. Chem. 282 (2007) 33935-33942
    • (2007) J. Biol. Chem. , vol.282 , pp. 33935-33942
    • Slutsky-Leiderman, O.1    Marom, M.2    Iosefson, O.3    Levy, R.4    Maoz, S.5    Azem, A.6
  • 178
    • 0028024592 scopus 로고
    • Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane
    • Sogo L.F., and Yaffe M.P. Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane. J. Cell Biol. 130 (1994) 1361-1373
    • (1994) J. Cell Biol. , vol.130 , pp. 1361-1373
    • Sogo, L.F.1    Yaffe, M.P.2
  • 179
    • 0034685890 scopus 로고    scopus 로고
    • Cloning and characterization of COX18, a Saccharomyces cerevisiae PET gene required for the assembly of cytochrome oxidase
    • Souza R.L., Green-Willms N.S., Fox T.D., Tzagoloff A., and Nobrega F.G. Cloning and characterization of COX18, a Saccharomyces cerevisiae PET gene required for the assembly of cytochrome oxidase. J. Biol. Chem. 275 (2000) 14898-14902
    • (2000) J. Biol. Chem. , vol.275 , pp. 14898-14902
    • Souza, R.L.1    Green-Willms, N.S.2    Fox, T.D.3    Tzagoloff, A.4    Nobrega, F.G.5
  • 180
    • 35548996344 scopus 로고    scopus 로고
    • Knockdown of human Oxa1l impairs the biogenesis of F(1)F(0)-ATP synthase and NADH:ubiquinone oxidoreductase
    • Stiburek L., Fornuskova D., Wenchich L., Pejznochova M., Hansikova H., and Zeman J. Knockdown of human Oxa1l impairs the biogenesis of F(1)F(0)-ATP synthase and NADH:ubiquinone oxidoreductase. J. Mol. Biol. 374 (2007) 506-516
    • (2007) J. Mol. Biol. , vol.374 , pp. 506-516
    • Stiburek, L.1    Fornuskova, D.2    Wenchich, L.3    Pejznochova, M.4    Hansikova, H.5    Zeman, J.6
  • 181
    • 0036558288 scopus 로고    scopus 로고
    • Characterization of rat TOM70 as a receptor of the preprotein translocase of the mitochondrial outer membrane
    • Suzuki H., Maeda M., and Mihara K. Characterization of rat TOM70 as a receptor of the preprotein translocase of the mitochondrial outer membrane. J. Cell Sci. 115 (2002) 1895-1905
    • (2002) J. Cell Sci. , vol.115 , pp. 1895-1905
    • Suzuki, H.1    Maeda, M.2    Mihara, K.3
  • 182
    • 0345732691 scopus 로고    scopus 로고
    • Ribosome binding to the Oxa1 complex facilitates cotranslational protein insertion in mitochondria
    • Szyrach G., Ott M., Bonnefoy N., Neupert W., and Herrmann J.M. Ribosome binding to the Oxa1 complex facilitates cotranslational protein insertion in mitochondria. EMBO J. 22 (2003) 6448-6457
    • (2003) EMBO J. , vol.22 , pp. 6448-6457
    • Szyrach, G.1    Ott, M.2    Bonnefoy, N.3    Neupert, W.4    Herrmann, J.M.5
  • 183
    • 0035980137 scopus 로고    scopus 로고
    • Structure and assembly of beta-barrel membrane proteins
    • Tamm L.K., Arora A., and Kleinschmidt J.H. Structure and assembly of beta-barrel membrane proteins. J. Biol. Chem. 276 (2001) 32399-32402
    • (2001) J. Biol. Chem. , vol.276 , pp. 32399-32402
    • Tamm, L.K.1    Arora, A.2    Kleinschmidt, J.H.3
  • 188
    • 33750949389 scopus 로고    scopus 로고
    • A role for Tim21 in membrane potential-dependent preprotein sorting in mitochondria
    • van der Laan M., Wiedemann N., Mick D.U., Guiard B., Rehling P., and Pfanner N. A role for Tim21 in membrane potential-dependent preprotein sorting in mitochondria. Curr. Biol. 16 (2006) 2271-2276
    • (2006) Curr. Biol. , vol.16 , pp. 2271-2276
    • van der Laan, M.1    Wiedemann, N.2    Mick, D.U.3    Guiard, B.4    Rehling, P.5    Pfanner, N.6
  • 190
    • 0023387650 scopus 로고
    • 1 presequence is a stop-transfer sequence for the mitochondrial inner membrane
    • 1 presequence is a stop-transfer sequence for the mitochondrial inner membrane. EMBO J. 6 (1987) 2441-2448
    • (1987) EMBO J. , vol.6 , pp. 2441-2448
    • Van Loon, A.P.1    Schatz, G.2
  • 194
    • 33750305666 scopus 로고    scopus 로고
    • Dynamic subcompartmentalization of the mitochondrial inner membrane
    • Vogel F., Bornhovd C., Neupert W., and Reichert A.S. Dynamic subcompartmentalization of the mitochondrial inner membrane. J. Cell Biol. 175 (2006) 237-247
    • (2006) J. Cell Biol. , vol.175 , pp. 237-247
    • Vogel, F.1    Bornhovd, C.2    Neupert, W.3    Reichert, A.S.4
  • 195
    • 0024442722 scopus 로고
    • Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues
    • von Heijne G. Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues. Nature 341 (1989) 456-458
    • (1989) Nature , vol.341 , pp. 456-458
    • von Heijne, G.1
  • 196
    • 0037428132 scopus 로고    scopus 로고
    • Role of a highly conserved bacterial protein in outer membrane protein assembly
    • Voulhoux R., Bos M.P., Geurtsen J., Mols M., and Tommassen J. Role of a highly conserved bacterial protein in outer membrane protein assembly. Science 299 (2003) 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
  • 197
    • 0142242210 scopus 로고    scopus 로고
    • Signal-anchor domains of proteins of the outer membrane of mitochondria: Structural and functional characteristics
    • Waizenegger T., Stan T., Neupert W., and Rapaport D. Signal-anchor domains of proteins of the outer membrane of mitochondria: Structural and functional characteristics. J. Biol. Chem. 278 (2003) 42064-42071
    • (2003) J. Biol. Chem. , vol.278 , pp. 42064-42071
    • Waizenegger, T.1    Stan, T.2    Neupert, W.3    Rapaport, D.4
  • 199
    • 21444448704 scopus 로고    scopus 로고
    • Mim1, a protein required for the assembly of the TOM complex of mitochondria
    • Waizenegger T., Schmitt S., Zivkovic J., Neupert W., and Rapaport D. Mim1, a protein required for the assembly of the TOM complex of mitochondria. EMBO Rep. 6 (2005) 57-62
    • (2005) EMBO Rep. , vol.6 , pp. 57-62
    • Waizenegger, T.1    Schmitt, S.2    Zivkovic, J.3    Neupert, W.4    Rapaport, D.5
  • 200
    • 4344590764 scopus 로고    scopus 로고
    • The J-protein family: Modulating protein assembly, disassembly and translocation
    • Walsh P., Bursac D., Law Y.C., Cyr D., and Lithgow T. The J-protein family: Modulating protein assembly, disassembly and translocation. EMBO Rep. 5 (2004) 567-571
    • (2004) EMBO Rep. , vol.5 , pp. 567-571
    • Walsh, P.1    Bursac, D.2    Law, Y.C.3    Cyr, D.4    Lithgow, T.5
  • 201
    • 0035102443 scopus 로고    scopus 로고
    • Targeting of C-terminal (tail)-anchored proteins: Understanding how cytoplasmic activities are anchored to intracellular membranes
    • Wattenberg B., and Lithgow T. Targeting of C-terminal (tail)-anchored proteins: Understanding how cytoplasmic activities are anchored to intracellular membranes. Traffic 2 (2001) 66-71
    • (2001) Traffic , vol.2 , pp. 66-71
    • Wattenberg, B.1    Lithgow, T.2
  • 202
    • 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
  • 203
    • 0031551576 scopus 로고    scopus 로고
    • Mdj2p, a novel DnaJ homolog in the mitochondrial inner membrane of the yeast Saccharomyces cerevisiae
    • Westermann B., and Neupert W. Mdj2p, a novel DnaJ homolog in the mitochondrial inner membrane of the yeast Saccharomyces cerevisiae. J. Mol. Biol. 272 (1997) 477-483
    • (1997) J. Mol. Biol. , vol.272 , pp. 477-483
    • Westermann, B.1    Neupert, W.2
  • 204
  • 205
    • 0035283084 scopus 로고    scopus 로고
    • The three modules of ADP/ATP carrier cooperate in receptor recruitment and translocation into mitochondria
    • Wiedemann N., Pfanner N., and Ryan M.T. The three modules of ADP/ATP carrier cooperate in receptor recruitment and translocation into mitochondria. EMBO J. 20 (2001) 951-960
    • (2001) EMBO J. , vol.20 , pp. 951-960
    • Wiedemann, N.1    Pfanner, N.2    Ryan, M.T.3
  • 207
    • 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
  • 208
    • 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
  • 209
    • 0041428149 scopus 로고    scopus 로고
    • The versatile beta-barrel membrane protein
    • Wimley W.C. The versatile beta-barrel membrane protein. Curr. Opin. Struct. Biol. 13 (2003) 404-411
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 404-411
    • Wimley, W.C.1
  • 210
    • 17444381980 scopus 로고    scopus 로고
    • Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli
    • Wu T., Malinverni J., Ruiz N., Kim S., Silhavy T.J., and Kahne D. Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli. Cell 121 (2005) 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
  • 211
    • 33749352547 scopus 로고    scopus 로고
    • Differential protein distributions define two sub-compartments of the mitochondrial inner membrane in yeast
    • Wurm C.A., and Jakobs S. Differential protein distributions define two sub-compartments of the mitochondrial inner membrane in yeast. FEBS Lett. 580 (2006) 5628-5634
    • (2006) FEBS Lett. , vol.580 , pp. 5628-5634
    • Wurm, C.A.1    Jakobs, S.2
  • 212
    • 0024818131 scopus 로고
    • The major 45-kDa protein of the yeast mitochondrial outer membrane is not essential for cell growth or mitochondrial function
    • Yaffe M.P., Jensen R.E., and Guido E.C. The major 45-kDa protein of the yeast mitochondrial outer membrane is not essential for cell growth or mitochondrial function. J. Biol. Chem. 264 (1989) 21091-21096
    • (1989) J. Biol. Chem. , vol.264 , pp. 21091-21096
    • Yaffe, M.P.1    Jensen, R.E.2    Guido, E.C.3
  • 213
    • 0037111988 scopus 로고    scopus 로고
    • Tim50 is a subunit of the TIM23 complex that links protein translocation across the outer and inner mitochondrial membranes
    • Yamamoto H., Esaki M., Kanamori T., Tamura Y., Nishikawa S., and Endo T. Tim50 is a subunit of the TIM23 complex that links protein translocation across the outer and inner mitochondrial membranes. Cell 111 (2002) 519-528
    • (2002) Cell , vol.111 , pp. 519-528
    • Yamamoto, H.1    Esaki, M.2    Kanamori, T.3    Tamura, Y.4    Nishikawa, S.5    Endo, T.6
  • 214
    • 0035856567 scopus 로고    scopus 로고
    • Phylogenetic and structural analyses of the oxa1 family of protein translocases
    • Yen M.R., Harley K.T., Tseng Y.H., and Saier Jr. M.H. Phylogenetic and structural analyses of the oxa1 family of protein translocases. FEMS Microbiol. Lett. 204 (2001) 223-231
    • (2001) FEMS Microbiol. Lett. , vol.204 , pp. 223-231
    • Yen, M.R.1    Harley, K.T.2    Tseng, Y.H.3    Saier Jr., M.H.4
  • 215
    • 0037428164 scopus 로고    scopus 로고
    • Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70
    • Young J.C., Hoogenraad N.J., and Hartl F.U. Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. Cell 112 (2003) 41-50
    • (2003) Cell , vol.112 , pp. 41-50
    • Young, J.C.1    Hoogenraad, N.J.2    Hartl, F.U.3
  • 217
    • 1442309968 scopus 로고    scopus 로고
    • Mmm2p, a mitochondrial outer membrane protein required for yeast mitochondrial shape and maintenance of mtDNA nucleoids
    • Youngman M.J., Hobbs A.E., Burgess S.M., Srinivasan M., and Jensen R.E. Mmm2p, a mitochondrial outer membrane protein required for yeast mitochondrial shape and maintenance of mtDNA nucleoids. J. Cell Biol. 164 (2004) 677-688
    • (2004) J. Cell Biol. , vol.164 , pp. 677-688
    • Youngman, M.J.1    Hobbs, A.E.2    Burgess, S.M.3    Srinivasan, M.4    Jensen, R.E.5


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