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Volumn 16, Issue 3, 2006, Pages 221-229

Convergent evolution of receptors for protein import into mitochondria

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; TOM TRANSLOCASE;

EID: 31944448611     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2005.12.034     Document Type: Article
Times cited : (101)

References (51)
  • 1
    • 0033525788 scopus 로고    scopus 로고
    • Mitochondrial evolution
    • M.W. Gray, G. Burger, and B.F. Lang 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
  • 2
    • 0034443285 scopus 로고    scopus 로고
    • Origin and evolution of the mitochondrial proteome
    • C.G. Kurland, and S.G. Andersson Origin and evolution of the mitochondrial proteome Microbiol. Mol. Biol. Rev. 64 2000 786 820
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 786-820
    • Kurland, C.G.1    Andersson, S.G.2
  • 3
    • 2942568227 scopus 로고    scopus 로고
    • A molecular timescale of eukaryote evolution and the rise of complex multicellular life
    • S.B. Hedges, J.E. Blair, M.L. Venturi, and J.L. Shoe A molecular timescale of eukaryote evolution and the rise of complex multicellular life BMC Evol. Biol. 4 2004 2
    • (2004) BMC Evol. Biol. , vol.4 , pp. 2
    • Hedges, S.B.1    Blair, J.E.2    Venturi, M.L.3    Shoe, J.L.4
  • 4
    • 1842505245 scopus 로고    scopus 로고
    • Bacterial proteins predisposed for targeting to mitochondria
    • R. Lucattini, V.A. Likić, and T. Lithgow Bacterial proteins predisposed for targeting to mitochondria Mol. Biol. Evol. 21 2004 652 658
    • (2004) Mol. Biol. Evol. , vol.21 , pp. 652-658
    • Lucattini, R.1    Likić, V.A.2    Lithgow, T.3
  • 5
    • 3242761606 scopus 로고    scopus 로고
    • Tom22′, an 8-kDa trans-site receptor in plants and protozoans, is a conserved feature of the TOM complex that appeared early in the evolution of eukaryotes
    • D. Maćašev, J. Whelan, E. Newbigin, M.C. Silva-Filho, T.D. Mulhern, and T. Lithgow Tom22′, an 8-kDa trans-site receptor in plants and protozoans, is a conserved feature of the TOM complex that appeared early in the evolution of eukaryotes Mol. Biol. Evol. 21 2004 1557 1564
    • (2004) Mol. Biol. Evol. , vol.21 , pp. 1557-1564
    • Maćašev, D.1    Whelan, J.2    Newbigin, E.3    Silva-Filho, M.C.4    Mulhern, T.D.5    Lithgow, T.6
  • 6
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • W. Neupert Protein import into mitochondria Annu. Rev. Biochem. 66 1997 863 917
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 863-917
    • Neupert, W.1
  • 7
    • 0037009087 scopus 로고    scopus 로고
    • Functions of outer membrane receptors in mitochondrial protein import
    • T. Endo, and D. Kohda Functions of outer membrane receptors in mitochondrial protein import Biochim. Biophys. Acta 1592 2002 3 14
    • (2002) Biochim. Biophys. Acta , vol.1592 , pp. 3-14
    • Endo, T.1    Kohda, D.2
  • 8
    • 2442555970 scopus 로고    scopus 로고
    • The protein import machinery of mitochondria
    • N. Wiedemann, A.E. Frazier, and N. Pfanner The protein import machinery of mitochondria J. Biol. Chem. 279 2004 14473 14476
    • (2004) J. Biol. Chem. , vol.279 , pp. 14473-14476
    • Wiedemann, N.1    Frazier, A.E.2    Pfanner, N.3
  • 9
    • 0024801086 scopus 로고
    • MOM19, an import receptor for mitochondrial precursor proteins
    • T. Söllner, T.G. Griffiths, R. Pfaller, N. Pfanner, and W. Neupert MOM19, an import receptor for mitochondrial precursor proteins Cell 59 1989 1061 1070
    • (1989) Cell , vol.59 , pp. 1061-1070
    • Söllner, T.1    Griffiths, T.G.2    Pfaller, R.3    Pfanner, N.4    Neupert, W.5
  • 10
    • 0027434076 scopus 로고
    • Functional cooperation of mitochondrial protein import receptors in yeast
    • L. Ramage, T. Junne, K. Hahne, T. Lithgow, and G. Schatz Functional cooperation of mitochondrial protein import receptors in yeast EMBO J. 12 1993 4115 4123
    • (1993) EMBO J. , vol.12 , pp. 4115-4123
    • Ramage, L.1    Junne, T.2    Hahne, K.3    Lithgow, T.4    Schatz, G.5
  • 12
    • 0034598904 scopus 로고    scopus 로고
    • Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20
    • Y. Abe, T. Shodai, T. Muto, K. Mihara, H. Torii, S.-I. Nishikawa, T. Endo, and D. Kohda Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20 Cell 100 2000 551 560
    • (2000) Cell , vol.100 , pp. 551-560
    • Abe, Y.1    Shodai, T.2    Muto, T.3    Mihara, K.4    Torii, H.5    Nishikawa, S.-I.6    Endo, T.7    Kohda, D.8
  • 14
    • 0030160495 scopus 로고    scopus 로고
    • A receptor for protein import into potato mitochondria
    • L. Heins, and U.K. Schmitz A receptor for protein import into potato mitochondria Plant J. 9 1996 829 839
    • (1996) Plant J. , vol.9 , pp. 829-839
    • Heins, L.1    Schmitz, U.K.2
  • 15
    • 0035115121 scopus 로고    scopus 로고
    • Purification and characterization of the preprotein translocase of the outer mitochondrial membrane from Arabidopsis. Identification of multiple forms of TOM20
    • W. Werhahn, A. Niemeyer, L. Jänsch, V. Kruft, U.K. Schmitz, and H.-P. Braun Purification and characterization of the preprotein translocase of the outer mitochondrial membrane from Arabidopsis. Identification of multiple forms of TOM20 Plant Physiol. 125 2001 943 954
    • (2001) Plant Physiol. , vol.125 , pp. 943-954
    • Werhahn, W.1    Niemeyer, A.2    Jänsch, L.3    Kruft, V.4    Schmitz, U.K.5    Braun, H.-P.6
  • 17
    • 0027983037 scopus 로고
    • Convergent evolution: The need to be explicit
    • R.F. Doolittle Convergent evolution: The need to be explicit Trends Biochem. Sci. 19 1994 15 18
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 15-18
    • Doolittle, R.F.1
  • 18
    • 0025159176 scopus 로고
    • A repeating amino acid motif in CDC23 defines a family of proteins and a new relationship among genes required for mitosis and RNA synthesis
    • R.S. Sikorski, M.S. Boguski, M. Goebl, and P.A. Hieter A repeating amino acid motif in CDC23 defines a family of proteins and a new relationship among genes required for mitosis and RNA synthesis Cell 60 1990 307 317
    • (1990) Cell , vol.60 , pp. 307-317
    • Sikorski, R.S.1    Boguski, M.S.2    Goebl, M.3    Hieter, P.A.4
  • 19
    • 0037648552 scopus 로고    scopus 로고
    • Design of stable alpha-helical arrays from an idealized TPR motif
    • E.R.G. Main, Y. Xiong, M.J. Cocco, L. D'Andrea, and L. Regan Design of stable alpha-helical arrays from an idealized TPR motif Structure 11 2003 497 508
    • (2003) Structure , vol.11 , pp. 497-508
    • Main, E.R.G.1    Xiong, Y.2    Cocco, M.J.3    D'Andrea, L.4    Regan, L.5
  • 20
    • 0029785147 scopus 로고    scopus 로고
    • Mapping the protein universe
    • L. Holm, and C. Sander Mapping the protein universe Science 273 1996 595 603
    • (1996) Science , vol.273 , pp. 595-603
    • Holm, L.1    Sander, C.2
  • 21
    • 0032473425 scopus 로고    scopus 로고
    • The structure of the tetratricopeptide repeats of protein phosphatase 5: Implications for TPR-mediated protein-protein interactions
    • K. Das, P.T.W. Cohen, and D. Barford The structure of the tetratricopeptide repeats of protein phosphatase 5: Implications for TPR-mediated protein-protein interactions EMBO J. 17 1998 1192 1199
    • (1998) EMBO J. , vol.17 , pp. 1192-1199
    • Das, K.1    Cohen, P.T.W.2    Barford, D.3
  • 22
    • 0002218484 scopus 로고    scopus 로고
    • Rate4Site: An algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologues
    • T. Pupko, R.E. Bell, I. Mayrose, F. Glaser, and N. Ben-Tal Rate4Site: An algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologues Bioinformatics 18 2002 S71 S77
    • (2002) Bioinformatics , vol.18
    • Pupko, T.1    Bell, R.E.2    Mayrose, I.3    Glaser, F.4    Ben-Tal, N.5
  • 23
    • 4143051195 scopus 로고    scopus 로고
    • Comparison of site-specific rate-inference methods for protein sequences: Empirical Bayesian methods are superior
    • I. Mayrose, D. Graur, N. Ben-Tal, and T. Pupko Comparison of site-specific rate-inference methods for protein sequences: Empirical Bayesian methods are superior Mol. Biol. Evol. 21 2004 1781 1791
    • (2004) Mol. Biol. Evol. , vol.21 , pp. 1781-1791
    • Mayrose, I.1    Graur, D.2    Ben-Tal, N.3    Pupko, T.4
  • 24
    • 4744341309 scopus 로고    scopus 로고
    • The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin alpha
    • 10.1038/nsmb833
    • M. Jinek, J. Rehwindel, B.D. Lazarus, E. Izaurralde, J.A. Hanover, and E. Conti The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin alpha Nat. Struct. Mol. Biol. 11 2004 1001 1007 10.1038/nsmb833 Published online September 12, 2004
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 1001-1007
    • Jinek, M.1    Rehwindel, J.2    Lazarus, B.D.3    Izaurralde, E.4    Hanover, J.A.5    Conti, E.6
  • 25
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • C. Scheufler, A. Brinker, G. Bourenkov, S. Pegoraro, L. Moroder, H. Bartunik, F.U. Hartl, and I. Moarefi Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine Cell 101 2000 199 210
    • (2000) Cell , vol.101 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6    Hartl, F.U.7    Moarefi, I.8
  • 26
  • 27
    • 0037447049 scopus 로고    scopus 로고
    • Mechanisms of protein import into mitochondria
    • K.N. Truscott, K. Brandner, and N. Pfanner Mechanisms of protein import into mitochondria Curr. Biol. 13 2003 R326 R337
    • (2003) Curr. Biol. , vol.13
    • Truscott, K.N.1    Brandner, K.2    Pfanner, N.3
  • 28
    • 18844421618 scopus 로고    scopus 로고
    • Protein import into mitochondria: Origins and functions today
    • R. Lister, J.M. Hulett, T. Lithgow, and J. Whelan Protein import into mitochondria: Origins and functions today Mol. Membr. Biol. 22 2005 87 100
    • (2005) Mol. Membr. Biol. , vol.22 , pp. 87-100
    • Lister, R.1    Hulett, J.M.2    Lithgow, T.3    Whelan, J.4
  • 29
    • 0028239372 scopus 로고
    • Yeast mitochondria lacking the two import receptors Mas20p and Mas70p can efficiently and specifically import precursor proteins
    • T. Lithgow, T. Junne, C. Wachter, and G. Schatz Yeast mitochondria lacking the two import receptors Mas20p and Mas70p can efficiently and specifically import precursor proteins J. Biol. Chem. 269 1994 15325 15330
    • (1994) J. Biol. Chem. , vol.269 , pp. 15325-15330
    • Lithgow, T.1    Junne, T.2    Wachter, C.3    Schatz, G.4
  • 30
    • 0028046512 scopus 로고
    • The mitochondrial outer membrane protein Mas22p is essential for protein import and viability of yeast
    • T. Lithgow, T. Junne, K. Suda, S. Gratzer, and G. Schatz The mitochondrial outer membrane protein Mas22p is essential for protein import and viability of yeast Proc. Natl. Acad. Sci. USA 91 1994 11973 11977
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11973-11977
    • Lithgow, T.1    Junne, T.2    Suda, K.3    Gratzer, S.4    Schatz, G.5
  • 31
  • 32
    • 24944591095 scopus 로고    scopus 로고
    • The missing link between hydrogenosomes and mitochondria
    • W. Martin The missing link between hydrogenosomes and mitochondria Trends Microbiol. 13 2005 457 459
    • (2005) Trends Microbiol. , vol.13 , pp. 457-459
    • Martin, W.1
  • 33
    • 0020479721 scopus 로고
    • Import of proteins into mitochondria. Energy-dependent, two-step processing of the intermembrane space enzyme cytochrome b2 by isolated yeast mitochondria
    • G. Daum, S.M. Gasser, and G. Schatz Import of proteins into mitochondria. Energy-dependent, two-step processing of the intermembrane space enzyme cytochrome b2 by isolated yeast mitochondria J. Biol. Chem. 257 1982 13075 13080
    • (1982) J. Biol. Chem. , vol.257 , pp. 13075-13080
    • Daum, G.1    Gasser, S.M.2    Schatz, G.3
  • 34
    • 0030691041 scopus 로고    scopus 로고
    • Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR
    • J.R. Huth, C.A. Bewley, B.M. Jackson, A.G. Hinnebusch, G.M. Clore, and A.M. Gronenborn Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR Protein Sci. 6 1997 2359 2364
    • (1997) Protein Sci. , vol.6 , pp. 2359-2364
    • Huth, J.R.1    Bewley, C.A.2    Jackson, B.M.3    Hinnebusch, A.G.4    Clore, G.M.5    Gronenborn, A.M.6
  • 35
    • 0034992645 scopus 로고    scopus 로고
    • A method for efficient isotopic labeling of recombinant proteins
    • J. Marley, M. Lu, and C. Bracken A method for efficient isotopic labeling of recombinant proteins J. Biomol. NMR 20 2001 71 75
    • (2001) J. Biomol. NMR , vol.20 , pp. 71-75
    • Marley, J.1    Lu, M.2    Bracken, C.3
  • 36
    • 31444434621 scopus 로고    scopus 로고
    • (1)H, (13)C and (15)N resonance assignments of the cytosolic domain of Tom20 from Arabidopsis thaliana
    • A.J. Perry, J.M. Hulett, T. Lithgow, and P.R. Gooley (1)H, (13)C and (15)N resonance assignments of the cytosolic domain of Tom20 from Arabidopsis thaliana J. Biomol. NMR 33 2005 198
    • (2005) J. Biomol. NMR , vol.33 , pp. 198
    • Perry, A.J.1    Hulett, J.M.2    Lithgow, T.3    Gooley, P.R.4
  • 39
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • P. Güntert, C. Mumenthaler, and K. Wüthrich Torsion angle dynamics for NMR structure calculation with the new program DYANA J. Mol. Biol. 273 1997 283 298
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 40
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • T. Herrmann, P. Güntert, and K. Wüthrich Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA J. Mol. Biol. 319 2002 209 227
    • (2002) J. Mol. Biol. , vol.319 , pp. 209-227
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 41
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • G. Cornilescu, F. Delaglio, and A. Bax Protein backbone angle restraints from searching a database for chemical shift and sequence homology J. Biomol. NMR 13 1999 289 302
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 42
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • R.A. Laskowski, J.A. Rullmann, M.W. MacArthur, R. Kaptein, and J.M. Thornton AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR J. Biomol. NMR 8 1996 477 486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmann, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 43
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • R. Koradi, M. Billeter, and K. Wuthrich MOLMOL: A program for display and analysis of macromolecular structures J. Mol. Graph. 14 1996 51 55
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 45
    • 0032512801 scopus 로고    scopus 로고
    • A symmetric-iterated multiple alignment of protein sequences
    • L. Brocchieri, and S. Karlin A symmetric-iterated multiple alignment of protein sequences J. Mol. Biol. 276 1998 249 264
    • (1998) J. Mol. Biol. , vol.276 , pp. 249-264
    • Brocchieri, L.1    Karlin, S.2
  • 46
  • 47
    • 0031743421 scopus 로고    scopus 로고
    • Profile hidden Markov models
    • S.R. Eddy Profile hidden Markov models Bioinformatics 14 1998 755 763
    • (1998) Bioinformatics , vol.14 , pp. 755-763
    • Eddy, S.R.1
  • 48
    • 0037566814 scopus 로고    scopus 로고
    • Tom40, the import channel of the mitochondrial outer membrane, plays an active role in sorting imported proteins
    • K. Gabriel, B. Egan, and T. Lithgow Tom40, the import channel of the mitochondrial outer membrane, plays an active role in sorting imported proteins EMBO J. 22 2003 2380 2386
    • (2003) EMBO J. , vol.22 , pp. 2380-2386
    • Gabriel, K.1    Egan, B.2    Lithgow, T.3
  • 49
    • 0142179050 scopus 로고    scopus 로고
    • The geometry and efficacy of cation-π interactions in a diagonal position of a designed beta-hairpin
    • C.D. Tatko, and M.L. Waters The geometry and efficacy of cation-π interactions in a diagonal position of a designed beta-hairpin Protein Sci. 12 2003 2443 2452
    • (2003) Protein Sci. , vol.12 , pp. 2443-2452
    • Tatko, C.D.1    Waters, M.L.2


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