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Volumn 22, Issue 19, 2003, Pages 5230-5240

TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes

Author keywords

Chaperonin assisted folding; GimC; Ssb type Hsp70; TRiC; WD40 proteins

Indexed keywords

ACTIN; CHAPERONE; CHAPERONIN; HEAT SHOCK PROTEIN 70; TUBULIN;

EID: 0141613640     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdg483     Document Type: Article
Times cited : (88)

References (51)
  • 1
    • 0025969670 scopus 로고
    • Staining of actin with fluorochrome-conjugated phalloidin
    • Adams, A.E. and Pringle, J.R. (1991) Staining of actin with fluorochrome-conjugated phalloidin. Methods Enzymol., 194, 729-731.
    • (1991) Methods Enzymol. , vol.194 , pp. 729-731
    • Adams, A.E.1    Pringle, J.R.2
  • 2
    • 0025303147 scopus 로고
    • Interaction of Hsp70 with newly synthesised proteins: Implications for protein folding and assembly
    • Beckmann, R.P., Mizzen, L.E. and Welch, W.J. (1990) Interaction of Hsp70 with newly synthesised proteins: implications for protein folding and assembly. Science, 248, 850-854.
    • (1990) Science , vol.248 , pp. 850-854
    • Beckmann, R.P.1    Mizzen, L.E.2    Welch, W.J.3
  • 3
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau, B. and Horwich, A.L. (1998) The Hsp70 and Hsp60 chaperone machines. Cell, 92, 351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 4
    • 0034646515 scopus 로고    scopus 로고
    • Getting newly synthesised proteins into shape
    • Bukau, B., Deuerling, E., Pfund, C. and Craig, E.A. (2000) Getting newly synthesised proteins into shape. Cell, 101, 119-122.
    • (2000) Cell , vol.101 , pp. 119-122
    • Bukau, B.1    Deuerling, E.2    Pfund, C.3    Craig, E.A.4
  • 5
    • 0034636716 scopus 로고    scopus 로고
    • Exploring redundancy in the yeast genome: An improved strategy for use of the cre-loxP system
    • Delneri, D., Tomlin, G.C., Wixon, J.L., Hutter, A., Sefton, M., Louis, E.J. and Oliver, S.G. (2000) Exploring redundancy in the yeast genome: an improved strategy for use of the cre-loxP system. Gene, 252, 127-135.
    • (2000) Gene , vol.252 , pp. 127-135
    • Delneri, D.1    Tomlin, G.C.2    Wixon, J.L.3    Hutter, A.4    Sefton, M.5    Louis, E.J.6    Oliver, S.G.7
  • 6
    • 0033549770 scopus 로고    scopus 로고
    • Trigger factor and DnaK cooperate in folding of newly synthesised proteins
    • Deuerling, E., Schulze-Specking, A., Tomoyasu, T., Mogk, A. and Bukau, B. (1999) Trigger factor and DnaK cooperate in folding of newly synthesised proteins. Nature, 400, 693-696.
    • (1999) Nature , vol.400 , pp. 693-696
    • Deuerling, E.1    Schulze-Specking, A.2    Tomoyasu, T.3    Mogk, A.4    Bukau, B.5
  • 7
    • 0030750584 scopus 로고    scopus 로고
    • In vivo observation of polypeptide flux through the bacterial chaperonin system
    • Ewalt, K.L., Hendrick, J.P., Houry, W.A. and Hartl, F.U. (1997) In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell, 90, 491-500.
    • (1997) Cell , vol.90 , pp. 491-500
    • Ewalt, K.L.1    Hendrick, J.P.2    Houry, W.A.3    Hartl, F.U.4
  • 8
    • 0030730821 scopus 로고    scopus 로고
    • Chaperonin-mediated folding in the eukaryotic cytosol proceeds through rounds of release of native and nonnative forms
    • Farr, G.W., Scharl, E.C., Schumacher, R.J., Sondek, S. and Horwich, A.L. (1997) Chaperonin-mediated folding in the eukaryotic cytosol proceeds through rounds of release of native and nonnative forms. Cell, 89, 927-937.
    • (1997) Cell , vol.89 , pp. 927-937
    • Farr, G.W.1    Scharl, E.C.2    Schumacher, R.J.3    Sondek, S.4    Horwich, A.L.5
  • 9
    • 0033400674 scopus 로고    scopus 로고
    • Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC
    • Feldman, D.E., Thulasiraman, V., Ferreyra, R.G. and Frydman, J. (1999) Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC. Mol. Cell, 4, 1051-1061.
    • (1999) Mol. Cell , vol.4 , pp. 1051-1061
    • Feldman, D.E.1    Thulasiraman, V.2    Ferreyra, R.G.3    Frydman, J.4
  • 10
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: The role of molecular chaperones
    • Frydman, J. (2001) Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu. Rev. Biochem., 70, 603-647.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 603-647
    • Frydman, J.1
  • 11
    • 0028361309 scopus 로고
    • Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
    • Frydman, J., Nimmesgern, E., Ohtsuka, K. and Hartl, F.U. (1994) Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature, 370, 111-117.
    • (1994) Nature , vol.370 , pp. 111-117
    • Frydman, J.1    Nimmesgern, E.2    Ohtsuka, K.3    Hartl, F.U.4
  • 12
    • 0343330935 scopus 로고    scopus 로고
    • Nascent polypeptide-associated complex stimulates protein import into yeast mitochondria
    • Funfschilling, U. and Rospert, S. (1999) Nascent polypeptide-associated complex stimulates protein import into yeast mitochondria. Mol. Biol. Cell, 10, 3289-3299.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3289-3299
    • Funfschilling, U.1    Rospert, S.2
  • 15
    • 0032481303 scopus 로고    scopus 로고
    • A novel protein complex promoting formation of functional α- and γ-tubulin
    • Geissler, S., Siegers, K. and Schiebel, E. (1998) A novel protein complex promoting formation of functional α- and γ-tubulin. EMBO J., 17, 952-966.
    • (1998) EMBO J. , vol.17 , pp. 952-966
    • Geissler, S.1    Siegers, K.2    Schiebel, E.3
  • 16
    • 0032478067 scopus 로고    scopus 로고
    • The yeast nascent polypeptide-associated complex initiates protein targeting to mitochondria in vivo
    • George, R., Beddoe, T., Landl, K. and Lithgow, T. (1998) The yeast nascent polypeptide-associated complex initiates protein targeting to mitochondria in vivo. Proc. Natl Acad. Sci. USA, 95, 2296-2301.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2296-2301
    • George, R.1    Beddoe, T.2    Landl, K.3    Lithgow, T.4
  • 17
    • 0034661466 scopus 로고    scopus 로고
    • CYP2E1 degradation by in vitro reconstituted systems: Role of the molecular chaperone Hsp90
    • Goasduff, T. and Cederbaum, A.I. (2000) CYP2E1 degradation by in vitro reconstituted systems: role of the molecular chaperone Hsp90. Arch. Biochem. Biophys., 379, 321-330.
    • (2000) Arch. Biochem. Biophys. , vol.379 , pp. 321-330
    • Goasduff, T.1    Cederbaum, A.I.2
  • 18
    • 0037115711 scopus 로고    scopus 로고
    • Assembly of the SMRT-histone deacetylase 3 repression complex requires the TCP-1 ring complex
    • Guenther, M.G., Yu, J.J., Kao, G.D., Yen, T.J. and Lazar, M.A. (2002) Assembly of the SMRT-histone deacetylase 3 repression complex requires the TCP-1 ring complex. Genes Dev., 16, 3130-3135.
    • (2002) Genes Dev. , vol.16 , pp. 3130-3135
    • Guenther, M.G.1    Yu, J.J.2    Kao, G.D.3    Yen, T.J.4    Lazar, M.A.5
  • 19
    • 0025994140 scopus 로고
    • Guide to yeast genetics and molecular biology
    • Guthrie, C. and Fink, G.R. (1991) Guide to yeast genetics and molecular biology. Methods Enzymol., 194, 1-933.
    • (1991) Methods Enzymol. , vol.194 , pp. 1-933
    • Guthrie, C.1    Fink, G.R.2
  • 20
    • 0345518025 scopus 로고    scopus 로고
    • Prefoldin-nascent chain complexes in the folding of cytoskeletal proteins
    • Hansen, W.J., Cowan, N.J. and Welch, W.J. (1999) Prefoldin-nascent chain complexes in the folding of cytoskeletal proteins. J. Cell Biol., 145, 265-277.
    • (1999) J. Cell Biol. , vol.145 , pp. 265-277
    • Hansen, W.J.1    Cowan, N.J.2    Welch, W.J.3
  • 21
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl, F.U. and Hayer-Hartl, M. (2002) Molecular chaperones in the cytosol: from nascent chain to folded protein. Science, 295, 1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 22
    • 0026091769 scopus 로고
    • CDC55, a Saccharomyces cerevisiae gene involved in cellular morphogenesis: Identification, characterization, and homology to the B subunit of mammalian type 2A protein phosphatase
    • Healy, A.M., Zolnierowicz, S., Stapleton, A.E., Goebl, M., DePaoli-Roach, A.A. and Pringle, J.R. (1991) CDC55, a Saccharomyces cerevisiae gene involved in cellular morphogenesis: identification, characterization, and homology to the B subunit of mammalian type 2A protein phosphatase. Mol. Cell. Biol., 11, 5767-5780.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 5767-5780
    • Healy, A.M.1    Zolnierowicz, S.2    Stapleton, A.E.3    Goebl, M.4    DePaoli-Roach, A.A.5    Pringle, J.R.6
  • 23
    • 0037050004 scopus 로고    scopus 로고
    • Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
    • Ho, Y. et al. (2002) Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature, 415, 180-183.
    • (2002) Nature , vol.415 , pp. 180-183
    • Ho, Y.1
  • 24
    • 0032775010 scopus 로고    scopus 로고
    • Epitope tagging of yeast genes using a PCR-based strategy: More tags and improved practical routines
    • Knop, M., Siegers, K., Pereira, G., Zachariae, W., Winsor, B., Nasmyth, K. and Schiebel, E. (1999) Epitope tagging of yeast genes using a PCR-based strategy: More tags and improved practical routines. Yeast, 15, 963-972.
    • (1999) Yeast , vol.15 , pp. 963-972
    • Knop, M.1    Siegers, K.2    Pereira, G.3    Zachariae, W.4    Winsor, B.5    Nasmyth, K.6    Schiebel, E.7
  • 27
    • 0034193525 scopus 로고    scopus 로고
    • The interaction of the chaperonin tailless complex polypeptide 1 (TCP1) ring complex (TRiC) with ribosome-bound nascent chains examined using photo-cross-linking
    • McCallum, C.D., Do, H., Johnson, A.E. and Frydman, J. (2000) The interaction of the chaperonin tailless complex polypeptide 1 (TCP1) ring complex (TRiC) with ribosome-bound nascent chains examined using photo-cross-linking. J. Cell Biol., 149, 591-601.
    • (2000) J. Cell Biol. , vol.149 , pp. 591-601
    • McCallum, C.D.1    Do, H.2    Johnson, A.E.3    Frydman, J.4
  • 28
    • 0037404423 scopus 로고    scopus 로고
    • The Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to assemble the von Hippel-Lindau tumor suppressor complex
    • Melville, M.W., McClellan, A.J., Meyer, A.S., Darveau, A. and Frydman, J. (2003) The Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to assemble the von Hippel-Lindau tumor suppressor complex. Mol. Cell. Biol., 23, 3141-3151.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3141-3151
    • Melville, M.W.1    McClellan, A.J.2    Meyer, A.S.3    Darveau, A.4    Frydman, J.5
  • 29
    • 0038737003 scopus 로고    scopus 로고
    • Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis
    • Meyer, A.S., Gillespie, J.R., Walther, D., Millet, I.S., Doniach, S. and Frydman, J. (2003) Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis. Cell, 113, 369-381.
    • (2003) Cell , vol.113 , pp. 369-381
    • Meyer, A.S.1    Gillespie, J.R.2    Walther, D.3    Millet, I.S.4    Doniach, S.5    Frydman, J.6
  • 30
    • 0030464317 scopus 로고    scopus 로고
    • Protein phosphatase 2A regulates MPF activity and sister chromatid cohesion in budding yeast
    • Minshull, J., Straight, A., Rudner, A.D., Demburg, A.F., Belmont, A. and Murray, A.W. (1996) Protein phosphatase 2A regulates MPF activity and sister chromatid cohesion in budding yeast. Curr. Biol., 6, 1609-1620.
    • (1996) Curr. Biol. , vol.6 , pp. 1609-1620
    • Minshull, J.1    Straight, A.2    Rudner, A.D.3    Demburg, A.F.4    Belmont, A.5    Murray, A.W.6
  • 31
    • 0028076764 scopus 로고    scopus 로고
    • The ancient regulatory-protein family of WD-repeat proteins
    • Neer, E.J., Schmidt, C.J., Nambudripad, R. and Smith, T.F. (1994) The ancient regulatory-protein family of WD-repeat proteins [erratum appears in Nature (2003), 371, 812]. Nature, 371, 297-300.
    • (1994) Nature , vol.371 , pp. 297-300
    • Neer, E.J.1    Schmidt, C.J.2    Nambudripad, R.3    Smith, T.F.4
  • 32
    • 0028076764 scopus 로고    scopus 로고
    • erratum appears
    • Neer, E.J., Schmidt, C.J., Nambudripad, R. and Smith, T.F. (1994) The ancient regulatory-protein family of WD-repeat proteins [erratum appears in Nature (2003), 371, 812]. Nature, 371, 297-300.
    • (2003) Nature , vol.371 , pp. 812
  • 33
    • 0026649409 scopus 로고
    • The translation machinery and 70 kd heat shock protein cooperate in protein synthesis
    • Nelson, R.L, Ziegelhoffer, T., Nicolet, C., Werner-Washburne, M. and Craig, E.A. (1992) The translation machinery and 70 kd heat shock protein cooperate in protein synthesis. Cell, 71, 97-105.
    • (1992) Cell , vol.71 , pp. 97-105
    • Nelson, R.L.1    Ziegelhoffer, T.2    Nicolet, C.3    Werner-Washburne, M.4    Craig, E.A.5
  • 34
  • 36
  • 38
    • 0033521523 scopus 로고    scopus 로고
    • Compartmentation of protein folding in vivo: Sequestration of non-native polypeptide by the chaperonin-GimC system
    • Siegers, K., Waldmann, T., Leroux, M.R., Grein, K., Shevchenko, A., Schiebel, E. and Hartl, F.U. (1999) Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J., 18, 75-84.
    • (1999) EMBO J. , vol.18 , pp. 75-84
    • Siegers, K.1    Waldmann, T.2    Leroux, M.R.3    Grein, K.4    Shevchenko, A.5    Schiebel, E.6    Hartl, F.U.7
  • 39
    • 0033680802 scopus 로고    scopus 로고
    • Structure of the molecular chaperone prefoldin: Unique interaction of multiple coiled coil tentacles with unfolded proteins
    • Siegert, R., Leroux, M.R., Scheufler, C., Hartl, F.U. and Moarefi, I. (2000) Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins. Cell, 103, 621-632.
    • (2000) Cell , vol.103 , pp. 621-632
    • Siegert, R.1    Leroux, M.R.2    Scheufler, C.3    Hartl, F.U.4    Moarefi, I.5
  • 40
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R.S. and Hieter, P. (1989) A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics, 122, 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 41
    • 0033133919 scopus 로고    scopus 로고
    • The WD repeat: A common architecture for diverse functions
    • Smith, T.F., Gaitatzes, C., Saxena, K. and Neer, E.J. (1999) The WD repeat: a common architecture for diverse functions. Trends Biochem. Sci., 24, 181-185.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 181-185
    • Smith, T.F.1    Gaitatzes, C.2    Saxena, K.3    Neer, E.J.4
  • 42
    • 0030034646 scopus 로고    scopus 로고
    • Crystal structure of a G-protein beta gamma dimer at 2.1 Å resolution
    • Sondek, J., Bohm, A., Lambright, D.G., Hamm, H.E. and Sigler, P.B. (1996) Crystal structure of a G-protein beta gamma dimer at 2.1 Å resolution. Nature, 379, 369-374.
    • (1996) Nature , vol.379 , pp. 369-374
    • Sondek, J.1    Bohm, A.2    Lambright, D.G.3    Hamm, H.E.4    Sigler, P.B.5
  • 43
  • 44
    • 0033521588 scopus 로고    scopus 로고
    • In vivo newly translated polypeptides are sequestered in a protected folding environment
    • Thulasiraman, V., Yang, C.F. and Frydman, J. (1999) In vivo newly translated polypeptides are sequestered in a protected folding environment. EMBO J., 18, 85-95.
    • (1999) EMBO J. , vol.18 , pp. 85-95
    • Thulasiraman, V.1    Yang, C.F.2    Frydman, J.3
  • 47
    • 0028676232 scopus 로고
    • New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae
    • Wach, A., Brachat, A., Pohlmann, R. and Philippsen, P. (1994) New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae. Yeast, 10, 1793-1808.
    • (1994) Yeast , vol.10 , pp. 1793-1808
    • Wach, A.1    Brachat, A.2    Pohlmann, R.3    Philippsen, P.4
  • 48
    • 0030840519 scopus 로고    scopus 로고
    • Heterologous HIS3 marker and GFP reporter modules for PCR-targeting in Saccharomyces cerevisiae
    • Wach, A., Brachat, A., Alberti-Segui, C., Rebischung, C. and Philippsen, P. (1997) Heterologous HIS3 marker and GFP reporter modules for PCR-targeting in Saccharomyces cerevisiae. Yeast, 13, 1065-1075.
    • (1997) Yeast , vol.13 , pp. 1065-1075
    • Wach, A.1    Brachat, A.2    Alberti-Segui, C.3    Rebischung, C.4    Philippsen, P.5
  • 49
    • 0032849794 scopus 로고    scopus 로고
    • The nascent polypeptide-associated complex (NAC) of yeast functions in the targeting process of ribosomes to the ER membrane
    • Wiedmann, B. and Prehn, S. (1999) The nascent polypeptide-associated complex (NAC) of yeast functions in the targeting process of ribosomes to the ER membrane. FEBS Lett., 458, 51-54.
    • (1999) FEBS Lett. , vol.458 , pp. 51-54
    • Wiedmann, B.1    Prehn, S.2
  • 50
    • 0024025436 scopus 로고
    • Post-translational transport of proteins into microsomal membranes of Candida maltosa
    • Wiedmann, M., Wiedmann, B., Voigt, S., Wachter, E., Muller, H.G. and Rapoport, T.A. (1988) Post-translational transport of proteins into microsomal membranes of Candida maltosa. EMBO J., 7, 1763-1768.
    • (1988) EMBO J. , vol.7 , pp. 1763-1768
    • Wiedmann, M.1    Wiedmann, B.2    Voigt, S.3    Wachter, E.4    Muller, H.G.5    Rapoport, T.A.6
  • 51
    • 0033772801 scopus 로고    scopus 로고
    • Loss of a protein phosphatase 2A regulatory subunit (Cdc55p) elicits improper regulation of Swelp degradation
    • Yang, H., Jiang, W., Gentry, M. and Hallberg, R.L. (2000) Loss of a protein phosphatase 2A regulatory subunit (Cdc55p) elicits improper regulation of Swelp degradation. Mol. Cell Biol., 20, 8143-8156.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 8143-8156
    • Yang, H.1    Jiang, W.2    Gentry, M.3    Hallberg, R.L.4


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