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Volumn 395, Issue 6701, 1998, Pages 516-521

Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; LIPOSOME;

EID: 0032188847     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/26780     Document Type: Article
Times cited : (419)

References (30)
  • 1
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz, G. & Dobberstein, B. Common principles of protein translocation across membranes. Science 271, 1519-1526 (1996).
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 2
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Neupert, W. Protein import into mitochondria. Annu. Rev. Biochem. 66, 863-917 (1997).
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 863-917
    • Neupert, W.1
  • 4
    • 0025176934 scopus 로고
    • Electrophysiological characterization of contact sites in brain mitochondria
    • Moran, O., Sandri, G., Panfili, E., Stühmer, W. & Sorgato, C. Electrophysiological characterization of contact sites in brain mitochondria. J. Biol. Chem. 265, 908-913 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 908-913
    • Moran, O.1    Sandri, G.2    Panfili, E.3    Stühmer, W.4    Sorgato, C.5
  • 5
    • 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. & 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, 377-386 (1997).
    • (1997) J. Cell Biol. , vol.137 , pp. 377-386
    • Lohret, T.A.1    Jensen, R.E.2    Kinnally, K.W.3
  • 6
    • 0031058486 scopus 로고    scopus 로고
    • Relationship between the peptide-sensitive channel and the mitochondrial outer membrane protein translocation machinery
    • Juin, P., Thieffry, M., Henry, J.-P. & Vallette, F. M. Relationship between the peptide-sensitive channel and the mitochondrial outer membrane protein translocation machinery. J. Biol. Chem. 272, 6044-6050 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 6044-6050
    • Juin, P.1    Thieffry, M.2    Henry, J.-P.3    Vallette, F.M.4
  • 7
    • 0024409765 scopus 로고
    • Identification of a new pore in the mitochondrial outer membrane of a porin-deficient yeast mutant
    • Dihanich, M., Schmidt, A., Oppliger, W. & Benz, R. Identification of a new pore in the mitochondrial outer membrane of a porin-deficient yeast mutant. Eur. J. Biochem. 181, 703-708 (1989).
    • (1989) Eur. J. Biochem. , vol.181 , pp. 703-708
    • Dihanich, M.1    Schmidt, A.2    Oppliger, W.3    Benz, R.4
  • 8
    • 0025597095 scopus 로고
    • A yeast mitochondrial outer membrane protein essential for protein import and cell viability
    • Baker, K. P., Schaniel, A., Vestweber, D. & Schatz, G. A yeast mitochondrial outer membrane protein essential for protein import and cell viability. Nature 348, 605-609 (1990).
    • (1990) Nature , vol.348 , pp. 605-609
    • Baker, K.P.1    Schaniel, A.2    Vestweber, D.3    Schatz, G.4
  • 9
    • 0029971312 scopus 로고    scopus 로고
    • Detection of likely transmembrane β-strand regions in sequences of mitochondrial pore proteins using the Gibbs sampler
    • Mannella, C. A., Neuwald, A. F. & Lawrence, C. E. Detection of likely transmembrane β-strand regions in sequences of mitochondrial pore proteins using the Gibbs sampler. J. Bioenerg. Biomembr. 28, 163-169 (1996).
    • (1996) J. Bioenerg. Biomembr. , vol.28 , pp. 163-169
    • Mannella, C.A.1    Neuwald, A.F.2    Lawrence, C.E.3
  • 10
    • 18744422713 scopus 로고    scopus 로고
    • Expression of porin from Rhodopseudomonas blastica in Escherichia coli inclusion bodies and folding into exact native structure
    • Schmid, B., Krömer, M. & Schulz, G. E. Expression of porin from Rhodopseudomonas blastica in Escherichia coli inclusion bodies and folding into exact native structure. FEBS Lett. 381, 111-114 (1996).
    • (1996) FEBS Lett. , vol.381 , pp. 111-114
    • Schmid, B.1    Krömer, M.2    Schulz, G.E.3
  • 11
    • 0027988296 scopus 로고
    • Protein secondary structure from circular dichroism spectroscopy: Combining variable selection principle and cluster analysis with neural network, ridge regression and self-consistent methods
    • Sreerama, N. & Woody, R. W. Protein secondary structure from circular dichroism spectroscopy: combining variable selection principle and cluster analysis with neural network, ridge regression and self-consistent methods. J. Mol. Biol. 242, 497-507 (1994).
    • (1994) J. Mol. Biol. , vol.242 , pp. 497-507
    • Sreerama, N.1    Woody, R.W.2
  • 13
    • 0031464541 scopus 로고    scopus 로고
    • Reconstitution of a chloroplast protein import channel
    • Hinnah, S., Hill, K., Wagner, R., Schlicher, T. & Soll, J. Reconstitution of a chloroplast protein import channel. EMBO J. 16, 7351-7360 (1997).
    • (1997) EMBO J. , vol.16 , pp. 7351-7360
    • Hinnah, S.1    Hill, K.2    Wagner, R.3    Schlicher, T.4    Soll, J.5
  • 14
    • 0031042584 scopus 로고    scopus 로고
    • A novel method for structure-based prediction of ion channel conductance properties
    • Smart, O. S., Breed, J., Smith, G. R. & Sansom, M. S. A novel method for structure-based prediction of ion channel conductance properties. Biophys. J. 72, 1109-1126 (1997).
    • (1997) Biophys. J. , vol.72 , pp. 1109-1126
    • Smart, O.S.1    Breed, J.2    Smith, G.R.3    Sansom, M.S.4
  • 16
    • 0028856032 scopus 로고
    • Mitochondrial receptor complex from Neurospora crassa and Saccharomyces cerevisiae
    • Alconada, A., Gärtner, F., Hönlinger, A., Kübrich, M. & Pfanner, N. Mitochondrial receptor complex from Neurospora crassa and Saccharomyces cerevisiae. Methods Enzymol. 260, 263-286 (1995).
    • (1995) Methods Enzymol. , vol.260 , pp. 263-286
    • Alconada, A.1    Gärtner, F.2    Hönlinger, A.3    Kübrich, M.4    Pfanner, N.5
  • 17
    • 1842329159 scopus 로고    scopus 로고
    • Tom5 functionally links mitochondrial preprotein receptors to the general import pore
    • Dietmeier, K. et al. Tom5 functionally links mitochondrial preprotein receptors to the general import pore. Nature 388, 195-200 (1997).
    • (1997) Nature , vol.388 , pp. 195-200
    • Dietmeier, K.1
  • 18
    • 0030845840 scopus 로고    scopus 로고
    • The Tim core complex defines the number of mitochondrial translocation contact sites and can hold arrested preproteins in the absence of matrix Hsp70-Tim44
    • Dekker, P. J. T. et al. The Tim core complex defines the number of mitochondrial translocation contact sites and can hold arrested preproteins in the absence of matrix Hsp70-Tim44. EMBO J. 16, 5408-5419 (1997).
    • (1997) EMBO J. , vol.16 , pp. 5408-5419
    • Dekker, P.J.T.1
  • 19
    • 0342301720 scopus 로고
    • Artificial mitochondrial presequences
    • Allison, D. S. & Schatz, G. Artificial mitochondrial presequences. Proc. Natl Acad. Sci. USA 83, 9011-9015 (1986).
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 9011-9015
    • Allison, D.S.1    Schatz, G.2
  • 20
    • 0030769419 scopus 로고    scopus 로고
    • Differential recognition of preproteins by the purified cytosolic domains of the mitochondrial import receptors Tom20, Tom22, and Tom70
    • Brix, J., Dietmeier, K. & Pfanner, N. Differential recognition of preproteins by the purified cytosolic domains of the mitochondrial import receptors Tom20, Tom22, and Tom70. J. Biol. Chem. 272, 20730-20735 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 20730-20735
    • Brix, J.1    Dietmeier, K.2    Pfanner, N.3
  • 21
    • 0030872409 scopus 로고    scopus 로고
    • Mitochondrial protein import: Tom40 plays a major role in targeting and translocation of preproteins by forming a specific binding site for the presequence
    • Rapaport, D., Neupert, W. & Lill, R. Mitochondrial protein import: Tom40 plays a major role in targeting and translocation of preproteins by forming a specific binding site for the presequence. J. Biol. Chem. 272, 18725-18731 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 18725-18731
    • Rapaport, D.1    Neupert, W.2    Lill, R.3
  • 22
    • 0028796617 scopus 로고
    • Mitochondrial protein import: Reversible binding of the presequence at the trans side of the outer membrane drives partial translocation and unfolding
    • Mayer, A., Neupert, W. & Lill, R. Mitochondrial protein import: reversible binding of the presequence at the trans side of the outer membrane drives partial translocation and unfolding. Cell 80, 127-137 (1995).
    • (1995) Cell , vol.80 , pp. 127-137
    • Mayer, A.1    Neupert, W.2    Lill, R.3
  • 23
    • 0024536726 scopus 로고
    • DNA-protein conjugates can enter mitochondria via the protein import pathway
    • Vestweber, D. & Schatz, G. DNA-protein conjugates can enter mitochondria via the protein import pathway. Nature 338, 170-172 (1989).
    • (1989) Nature , vol.338 , pp. 170-172
    • Vestweber, D.1    Schatz, G.2
  • 24
    • 0032511189 scopus 로고    scopus 로고
    • The preprotein translocation channel of the outer membrane of mitochondria
    • Künkele, K.-P. et al. The preprotein translocation channel of the outer membrane of mitochondria. Cell 93, 1009-1019 (1998).
    • (1998) Cell , vol.93 , pp. 1009-1019
    • Künkele, K.-P.1
  • 25
    • 0032488845 scopus 로고    scopus 로고
    • Protein translocation: Tunnel vision
    • Matlack, K. E. S., Mothes, W. & Rapoport, T. A. Protein translocation: tunnel vision. Cell 92, 381-390 (1998).
    • (1998) Cell , vol.92 , pp. 381-390
    • Matlack, K.E.S.1    Mothes, W.2    Rapoport, T.A.3
  • 26
    • 0024424988 scopus 로고
    • A 24K outer-membrane protein is a component of the yeast mitochondrial protein import site
    • Vestweber, D., Brunner, J., Baker, A. & Schatz, G. A 24K outer-membrane protein is a component of the yeast mitochondrial protein import site. Nature 341, 205-209 (1989).
    • (1989) Nature , vol.341 , pp. 205-209
    • Vestweber, D.1    Brunner, J.2    Baker, A.3    Schatz, G.4
  • 27
    • 0025606107 scopus 로고
    • Identification of a mitochondrial receptor complex required for recognition and membrane insertion of precursor proteins
    • Kiebler, M. et al. Identification of a mitochondrial receptor complex required for recognition and membrane insertion of precursor proteins. Nature 348, 610-616 (1990).
    • (1990) Nature , vol.348 , pp. 610-616
    • Kiebler, M.1
  • 28
    • 0026502349 scopus 로고
    • Mapping of the protein import machinery in the mitochondrial outer membrane by crosslinking of translocation intermediates
    • Söllner, T. et al. Mapping of the protein import machinery in the mitochondrial outer membrane by crosslinking of translocation intermediates. Nature 355, 84-87 (1992).
    • (1992) Nature , vol.355 , pp. 84-87
    • Söllner, T.1
  • 29
    • 0028997692 scopus 로고
    • The mitochondrial receptor complex: Mom22 is essential for cell viability and directly interacts with preproteins
    • Hönlinger, A. et al. The mitochondrial receptor complex: Mom22 is essential for cell viability and directly interacts with preproteins. Mol. Cell. Biol. 15, 3382-3389 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3382-3389
    • Hönlinger, A.1
  • 30
    • 0029619088 scopus 로고
    • Acidic receptor domains on both sides of the outer membrane mediate translocation of precursor proteins into yeast mitochondria
    • Bolliger, L., Junne, T., Schatz, G. & Lithgow, T. Acidic receptor domains on both sides of the outer membrane mediate translocation of precursor proteins into yeast mitochondria. EMBO J. 14, 6318-6326 (1995).
    • (1995) EMBO J. , vol.14 , pp. 6318-6326
    • Bolliger, L.1    Junne, T.2    Schatz, G.3    Lithgow, T.4


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