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Volumn 84, Issue 5, 2003, Pages 2981-2989

Comparison of the TIM and TOM channel activities of the mitochondrial protein import complexes

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; PROTEIN TIM; PROTEIN TOM; SIGNAL PEPTIDE; UNCLASSIFIED DRUG; VOLTAGE GATED CHANNEL FORMING PROTEIN;

EID: 0038637773     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)70024-1     Document Type: Article
Times cited : (48)

References (44)
  • 1
    • 0032762996 scopus 로고    scopus 로고
    • Microsecond time-scale discrimination among polycytidylic acid, polyadenylic acid, and polyuridylic acid as homopolymers or as segments within single RNA molecules
    • Akeson, M., D. Branton, J. J. Kasianowicz, E. Brandin, and D. W. Deamer. 1999. Microsecond time-scale discrimination among polycytidylic acid, polyadenylic acid, and polyuridylic acid as homopolymers or as segments within single RNA molecules. Biophys. J. 77:3227-3233.
    • (1999) Biophys. J. , vol.77 , pp. 3227-3233
    • Akeson, M.1    Branton, D.2    Kasianowicz, J.J.3    Brandin, E.4    Deamer, D.W.5
  • 2
  • 3
    • 0001777212 scopus 로고    scopus 로고
    • Protein translocation into mitochondria: The role of TIM complexes
    • Bauer, M. F., S. Hofmann, W. Neupert, and M. Brunner. 2000. Protein translocation into mitochondria: the role of TIM complexes. Trends Cell Biol. 10:25-31.
    • (2000) Trends Cell Biol. , vol.10 , pp. 25-31
    • Bauer, M.F.1    Hofmann, S.2    Neupert, W.3    Brunner, M.4
  • 4
    • 0025355620 scopus 로고
    • Selectivity changes in site-directed mutants of the VDAC ion channel: Structural implications
    • Blachly-Dyson, E., S. Peng, M. Colombini, and M. Forte. 1990. Selectivity changes in site-directed mutants of the VDAC ion channel: Structural implications. Science. 247:1233-1236.
    • (1990) Science , vol.247 , pp. 1233-1236
    • Blachly-Dyson, E.1    Peng, S.2    Colombini, M.3    Forte, M.4
  • 5
    • 0030873947 scopus 로고    scopus 로고
    • Multicopy suppressors of phenotypes resulting from the absence of yeast VDAC encode a VDAC-like protein
    • Blachly-Dyson, E., J. M. Song, W. J. Wolfgang, M. Colombini, and M. Forte. 1997. Multicopy suppressors of phenotypes resulting from the absence of yeast VDAC encode a VDAC-like protein. Mol. Cell. Biol. 10:5727-5738.
    • (1997) Mol. Cell. Biol. , vol.10 , pp. 5727-5738
    • Blachly-Dyson, E.1    Song, J.M.2    Wolfgang, W.J.3    Colombini, M.4    Forte, M.5
  • 6
    • 0016753216 scopus 로고
    • Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma
    • Blobel, G., and B. Dobberstein. 1975. Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. J. Cell Biol. 67:835-851.
    • (1975) J. Cell Biol. , vol.67 , pp. 835-851
    • Blobel, G.1    Dobberstein, B.2
  • 7
    • 0017647639 scopus 로고
    • Ultrastructural and biochemical studies of mitoplasts and outer membranes derived from French-pressed mitochondria
    • Decker, G. L., and J. W. Greenawalt. 1977. Ultrastructural and biochemical studies of mitoplasts and outer membranes derived from French-pressed mitochondria. J. Ultrastr. Res. 59:44-56.
    • (1977) J. Ultrastr. Res. , vol.59 , pp. 44-56
    • Decker, G.L.1    Greenawalt, J.W.2
  • 9
    • 0025309392 scopus 로고
    • Localization of a synthetic presequence that blocks protein import into mitochondria
    • Glaser, S. M., and M. G. Cumsky. 1990. Localization of a synthetic presequence that blocks protein import into mitochondria. J. Biol. Chem. 265:8817-8822.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8817-8822
    • Glaser, S.M.1    Cumsky, M.G.2
  • 10
    • 0019441262 scopus 로고
    • Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches
    • Hamill, O. P., A. Marty, E. Neher, B. Sakmann, and F. J. Sigworth. 1981. Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches. Pflügers Arch-Eur J Physiol. 381:85-100.
    • (1981) Pflügers Arch-Eur. J. Physiol. , vol.381 , pp. 85-100
    • Hamill, O.P.1    Marty, A.2    Neher, E.3    Sakmann, B.4    Sigworth, F.J.5
  • 11
    • 0032188847 scopus 로고    scopus 로고
    • Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins
    • Hill, K., K. Model, M. T. Ryan, K. Dietmeier, F. Martin, R. Wagner, and K. Pfanner. 1998. Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins. Nature. 395:516-521.
    • (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, K.7
  • 13
    • 0035190881 scopus 로고    scopus 로고
    • Opening the door to mitochondrial protein import
    • Jensen, R. E., and A. E. Johnson. 2001. Opening the door to mitochondrial protein import. Nat. Struct. Biol. 8:1008-1010.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 1008-1010
    • Jensen, R.E.1    Johnson, A.E.2
  • 14
    • 0031058486 scopus 로고    scopus 로고
    • Relationship between the peptide-sensitive channel and the mitochondrial outer membrane protein translocation machinery
    • Juin, P., M. Thieffry, J. Henry, and F. M. Vallette. 1997. Relationship between the peptide-sensitive channel and the mitochondrial outer membrane protein translocation machinery. J. Biol. Chem. 272:6044-6050.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6044-6050
    • Juin, P.1    Thieffry, M.2    Henry, J.3    Vallette, F.M.4
  • 15
    • 0030465241 scopus 로고    scopus 로고
    • Characterization of individual polynucleotide molecules using a membrane channel
    • Kasianowicz, J. J., E. Brandin, D. Branton, and D. W. Deamer. 1996. Characterization of individual polynucleotide molecules using a membrane channel. Proc. Natl. Acad. Sci. USA. 93:13770-13773.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13770-13773
    • Kasianowicz, J.J.1    Brandin, E.2    Branton, D.3    Deamer, D.W.4
  • 16
    • 0026607021 scopus 로고
    • Modulation of inner mitochondrial membrane channel activity
    • Kinnally, K. W., Y. N. Antonenko, and D. B. Zorov. 1992. Modulation of inner mitochondrial membrane channel activity. J. Bioenerg. Biomembr. 24:99-110.
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 99-110
    • Kinnally, K.W.1    Antonenko, Y.N.2    Zorov, D.B.3
  • 18
    • 0034011972 scopus 로고    scopus 로고
    • MCC and PSC, the putative protein import channels of mitochondria
    • Kinnally, K. W., C. Muro, and M. L. Campo. 2000. MCC and PSC, the putative protein import channels of mitochondria. J. Bioenerg. Biomembr. 32:47-54.
    • (2000) J. Bioenerg. Biomembr. , vol.32 , pp. 47-54
    • Kinnally, K.W.1    Muro, C.2    Campo, M.L.3
  • 20
    • 0036154083 scopus 로고    scopus 로고
    • Transport of maltodextrins through maltoporin: A single-channel study
    • Kullman, L., M. Winterhalter, and S. M. Bezrukov. 2002. Transport of maltodextrins through maltoporin: a single-channel study. Biophys. J. 82:803-812.
    • (2002) Biophys. J. , vol.82 , pp. 803-812
    • Kullman, L.1    Winterhalter, M.2    Bezrukov, S.M.3
  • 23
    • 0033150885 scopus 로고    scopus 로고
    • Signal presequences increase mitochondrial permeability and open the multiple conductance channel
    • Kushnareva, Y. E., M. L. Campo, K. W. Kinnally, and P. M. Sokolove. 1999. Signal presequences increase mitochondrial permeability and open the multiple conductance channel. Arch. Biochem. Biophys. 366:107-115.
    • (1999) Arch. Biochem. Biophys. , vol.366 , pp. 107-115
    • Kushnareva, Y.E.1    Campo, M.L.2    Kinnally, K.W.3    Sokolove, P.M.4
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature (Lond.). 227:680-685.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 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
    • Lohret, T. A., R. E. Jensen, and K. W. Kinnally. 1997. Tim23, a protein import component of the mitochondrial inner membrane, is required for normal activity of the multiple conductance channel, MCC. J. Cell Biol. 137:377-386.
    • (1997) MCC. J. Cell Biol. , vol.137 , pp. 377-386
    • Lohret, T.A.1    Jensen, R.E.2    Kinnally, K.W.3
  • 26
    • 0029024668 scopus 로고
    • Multiple conductance channel activity of wild-type and voltage-dependent anion-selective channel (VDAC)-less yeast mitochondria
    • Lohret, T. A., and K. W. Kinnally. 1995a. Multiple conductance channel activity of wild-type and voltage-dependent anion-selective channel (VDAC)-less yeast mitochondria. Biophys. J. 68:2299-2309.
    • (1995) Biophys. J. , vol.68 , pp. 2299-2309
    • Lohret, T.A.1    Kinnally, K.W.2
  • 27
    • 0029005757 scopus 로고
    • Targeting peptides transiently block a mitochondrial channel
    • Lohret, T. A., and K. W. Kinnally. 1995b. Targeting peptides transiently block a mitochondrial channel. J. Biol. Chem. 270:15950-15953.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15950-15953
    • Lohret, T.A.1    Kinnally, K.W.2
  • 28
    • 0029981386 scopus 로고    scopus 로고
    • Activity of the mitochondrial multiple conductance channel is independent of the adenine nucleotide translocator
    • Lohret, T. A., R. C. Murphy, T. Drgon, and K. W. Kinnally. 1996. Activity of the mitochondrial multiple conductance channel is independent of the adenine nucleotide translocator. J. Biol. Chem. 271:4846-4849.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4846-4849
    • Lohret, T.A.1    Murphy, R.C.2    Drgon, T.3    Kinnally, K.W.4
  • 29
    • 0020450839 scopus 로고
    • Structure of the outer mitochondrial membrane: Ordered arrays of porelike subunits in outer membrane fractions from Neurospora crassa mitochondria
    • Mannella, C. A. 1982. Structure of the outer mitochondrial membrane: ordered arrays of porelike subunits in outer membrane fractions from Neurospora crassa mitochondria. J. Cell Biol. 94:680-687.
    • (1982) J. Cell Biol. , vol.94 , pp. 680-687
    • Mannella, C.A.1
  • 30
    • 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., T. Prinz, T. Ruiz, M. Radermacher, T. Krimmer, W. Kuhlbrandt, N. Pfanner, and C. Meisinger. 2002. Protein translocase of the outer mitochondrial membrane: role of import receptors in the structural organization of the TOM complex. J. Mol. Biol. 316:657-666.
    • (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
  • 31
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Neupert, W. 1997. Protein import into mitochondria. Annu. Rev. Biochem. 66:867-917.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 867-917
    • Neupert, W.1
  • 33
    • 0035344460 scopus 로고    scopus 로고
    • Versatility of the mitochondrial protein import machinery
    • Pfanner, N., and A. Geissler. 2001. Versatility of the mitochondrial protein import machinery. Nat. Rev. Mol. Cell Biol. 2:339-349.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 339-349
    • Pfanner, N.1    Geissler, A.2
  • 34
    • 0036213690 scopus 로고    scopus 로고
    • Powering mitochondrial protein import
    • Pfanner, N., and K. N. Truscott. 2002. Powering mitochondrial protein import. Nat. Struct. Biol. 9:234-236.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 234-236
    • Pfanner, N.1    Truscott, K.N.2
  • 35
    • 0031967829 scopus 로고    scopus 로고
    • ATP transport through a single mitochondrial channel, VDAC, studied by current fluctuation analysis
    • Rostovtseva, T. K., and S. M. Bezrukov. 1998. ATP transport through a single mitochondrial channel, VDAC, studied by current fluctuation analysis. Biophys. J. 74:2365-2373.
    • (1998) Biophys. J. , vol.74 , pp. 2365-2373
    • Rostovtseva, T.K.1    Bezrukov, S.M.2
  • 36
    • 0036219774 scopus 로고    scopus 로고
    • Dynamics of nucleotides in VDAC channels: Structure-specific noise generation
    • Rostovtseva, T. K., A. Komarov, S. M. Bezrukov, and M. Colombini. 2002. Dynamics of nucleotides in VDAC channels: structure-specific noise generation. Biophys. J. 82:193-205.
    • (2002) Biophys. J. , vol.82 , pp. 193-205
    • Rostovtseva, T.K.1    Komarov, A.2    Bezrukov, S.M.3    Colombini, M.4
  • 37
    • 0028842614 scopus 로고
    • Protein translocation across mitochondrial membranes: What a long, strange trip it is
    • Ryan, K. R., and R. E. Jensen. 1995. Protein translocation across mitochondrial membranes: what a long, strange trip it is. Cell. 83:517-519.
    • (1995) Cell , vol.83 , pp. 517-519
    • Ryan, K.R.1    Jensen, R.E.2
  • 38
    • 0027399210 scopus 로고
    • The protein import machinery of mitochondria
    • Schatz, G. 1993. The protein import machinery of mitochondria. Protein Sci. 2:141-146.
    • (1993) Protein Sci. , vol.2 , pp. 141-146
    • Schatz, G.1
  • 39
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz, G., and B. Dobberstein. 1996. Common principles of protein translocation across membranes. Science. 271:1519-1526.
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 40
    • 0033529681 scopus 로고    scopus 로고
    • A multisubunit complex of outer and inner mitochondrial membrane protein translocases stabilized in vivo by translocation intermediates
    • Schulke, N., N. B. Sepuri, D. M. Gordon, S. Saxena, A. Dancis, and D. Pain. 1999. A multisubunit complex of outer and inner mitochondrial membrane protein translocases stabilized in vivo by translocation intermediates. J. Biol. Chem. 274:22847-22854.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22847-22854
    • Schulke, N.1    Sepuri, N.B.2    Gordon, D.M.3    Saxena, S.4    Dancis, A.5    Pain, D.6
  • 41
    • 0030787527 scopus 로고    scopus 로고
    • In vivo zippering of inner and outer mitochondrial membranes by a stable translocation intermediate
    • Schulke, N., N. B. V. Sepuri, and D. Pain. 1997. In vivo zippering of inner and outer mitochondrial membranes by a stable translocation intermediate. Proc. Natl. Acad. Sci. USA. 94:7314-7319.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7314-7319
    • Schulke, N.1    Sepuri, N.B.V.2    Pain, D.3
  • 42
    • 0033539505 scopus 로고    scopus 로고
    • The dimensions of the protein import channels in the outer and inner mitochondrial membranes
    • Schwartz, M. P., and A. Matouschek. 1999. The dimensions of the protein import channels in the outer and inner mitochondrial membranes. Proc. Natl. Acad. Sci. USA. 96:13086-13090.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13086-13090
    • Schwartz, M.P.1    Matouschek, A.2
  • 43
    • 0026705887 scopus 로고
    • Properties of the mitochondrial peptide-sensitive cationic channel studied in planar bilayers and patches of giant liposomes
    • Thieffry, M., J. Neyton, M. Pelleschi, F. Fèvre, and J.-P. Henry. 1992. Properties of the mitochondrial peptide-sensitive cationic channel studied in planar bilayers and patches of giant liposomes. Biophys. J. 63:333-339.
    • (1992) Biophys. J. , vol.63 , pp. 333-339
    • Thieffry, M.1    Neyton, J.2    Pelleschi, M.3    Fèvre, F.4    Henry, J.-P.5
  • 44
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins for polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins for polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3


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