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Volumn 82, Issue 1, 2012, Pages 61-69

Reconstitution of the human chaperonin CCT by co-expression of the eight distinct subunits in mammalian cells

Author keywords

CCT; Chaperonin; Protein complex; Protein folding; Reconstitution; Vaccinia virus

Indexed keywords

CHAPERONIN CONTAINING TCP1; RECOMBINANT PROTEIN;

EID: 84855458799     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2011.11.010     Document Type: Article
Times cited : (19)

References (34)
  • 1
    • 0023668329 scopus 로고
    • Proteins as molecular chaperones
    • J. Ellis Proteins as molecular chaperones Nature 328 1987 378 379
    • (1987) Nature , vol.328 , pp. 378-379
    • Ellis, J.1
  • 2
    • 0026596223 scopus 로고
    • DnaJ and GroEL along the pathway of chaperone-mediated protein folding
    • T. Langer, C. Lu, H. Echols, J. Flanagan, M.K. Hayer, and F.U. Hartl DnaJ and GroEL along the pathway of chaperone-mediated protein folding Nature 356 1992 683 689
    • (1992) Nature , vol.356 , pp. 683-689
    • Langer, T.1    Lu, C.2    Echols, H.3    Flanagan, J.4    Hayer, M.K.5    Hartl, F.U.6
  • 3
    • 0027184721 scopus 로고
    • Molecular chaperone functions of heat-shock proteins
    • J.P. Hendrick, and F.U. Hartl Molecular chaperone functions of heat-shock proteins Annu. Rev. Biochem. 62 1993 349 384 (Pubitemid 23237875)
    • (1993) Annual Review of Biochemistry , vol.62 , pp. 349-384
    • Hendrick, J.P.1    Hartl, F.-U.2
  • 4
    • 0026776331 scopus 로고
    • A cytoplasmic chaperonin that catalyzes beta-actin folding
    • Y. Gao, J.O. Thomas, R.L. Chow, G.H. Lee, and N.J. Cowan A cytoplasmic chaperonin that catalyzes beta-actin folding Cell 69 1992 1043 1050
    • (1992) Cell , vol.69 , pp. 1043-1050
    • Gao, Y.1    Thomas, J.O.2    Chow, R.L.3    Lee, G.H.4    Cowan, N.J.5
  • 5
    • 0027077442 scopus 로고
    • Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits
    • J. Frydman, E. Nimmesgern, H. Erdjument-Bromage, J.S. Wall, P. Tempst, and F.U. Hartl Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits EMBO J. 11 1992 4767 4778 (Pubitemid 23023419)
    • (1992) EMBO Journal , vol.11 , Issue.13 , pp. 4767-4778
    • Frydman, J.1    Nimmesgern, E.2    Erdjument-Bromage, H.3    Wall, J.S.4    Tempst, P.5    Hartl, F.-U.6
  • 6
    • 0026683609 scopus 로고
    • T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol
    • V.A. Lewis, G.M. Hynes, D. Zheng, H. Saibil, and K. Willison T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol Nature 358 1992 249 252
    • (1992) Nature , vol.358 , pp. 249-252
    • Lewis, V.A.1    Hynes, G.M.2    Zheng, D.3    Saibil, H.4    Willison, K.5
  • 7
    • 0025748752 scopus 로고
    • A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1
    • J.D. Trent, E. Nimmesgern, J.S. Wall, F.U. Hartl, and A.L. Horwich A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1 Nature 354 1991 490 493 (Pubitemid 21896866)
    • (1991) Nature , vol.354 , Issue.6353 , pp. 490-493
    • Trent, J.D.1    Nimmesgern, E.2    Wall, J.S.3    Hartl, F.-U.4    Horwich, A.L.5
  • 8
    • 0027992757 scopus 로고
    • Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains
    • DOI 10.1016/0968-0004(94)90058-2
    • S. Kim, K.R. Willison, and A.L. Horwich Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains Trends Biochem. Sci. 19 1994 543 548 (Pubitemid 24361780)
    • (1994) Trends in Biochemical Sciences , vol.19 , Issue.12 , pp. 543-548
    • Kim, S.1    Willison, K.R.2    Horwich, A.L.3
  • 9
    • 0030910349 scopus 로고    scopus 로고
    • GroEL-mediated protein folding
    • W.A. Fenton, and A.L. Horwich GroEL-mediated protein folding Protein Sci. 6 1997 743 760 (Pubitemid 27154801)
    • (1997) Protein Science , vol.6 , Issue.4 , pp. 743-760
    • Fenton, W.A.1    Horwich, A.L.2
  • 10
    • 0030056969 scopus 로고    scopus 로고
    • Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction
    • DOI 10.1016/S0092-8674(00)81293-3
    • J.S. Weissman, H.S. Rye, W.A. Fenton, J.M. Beechem, and A.L. Horwich Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction Cell 84 1996 481 490 (Pubitemid 26058572)
    • (1996) Cell , vol.84 , Issue.3 , pp. 481-490
    • Weissman, J.S.1    Rye, H.S.2    Fenton, W.A.3    Beechem, J.M.4    Horwich, A.L.5
  • 12
    • 0027427326 scopus 로고
    • The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding
    • DOI 10.1038/366228a0
    • J. Martin, M. Mayhew, T. Langer, and F.U. Hartl The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding Nature 366 1993 228 233 (Pubitemid 23359705)
    • (1993) Nature , vol.366 , Issue.6452 , pp. 228-233
    • Martin, J.1    Mayhew, M.2    Langer, T.3    Hartl, F.U.4
  • 13
    • 43749113194 scopus 로고    scopus 로고
    • Hydrophilic residues 526 KNDAAD 531 in the flexible C-terminal region of the chaperonin GroEL are critical for substrate protein folding within the central cavity
    • K. Machida, A. Kono-Okada, K. Hongo, T. Mizobata, and Y. Kawata Hydrophilic residues 526 KNDAAD 531 in the flexible C-terminal region of the chaperonin GroEL are critical for substrate protein folding within the central cavity J. Biol. Chem. 283 2008 6886 6896
    • (2008) J. Biol. Chem. , vol.283 , pp. 6886-6896
    • MacHida, K.1    Kono-Okada, A.2    Hongo, K.3    Mizobata, T.4    Kawata, Y.5
  • 14
    • 0027092285 scopus 로고
    • Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity
    • T. Langer, G. Pfeifer, J. Martin, W. Baumeister, and F.U. Hartl Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity EMBO J. 11 1992 4757 4765 (Pubitemid 23023418)
    • (1992) EMBO Journal , vol.11 , Issue.13 , pp. 4757-4765
    • Langer, T.1    Pfeifer, G.2    Martin, J.3    Baumeister, W.4    Hartl, F.-U.5
  • 16
    • 69249229765 scopus 로고    scopus 로고
    • Gly192 at hinge 2 site in the chaperonin GroEL plays a pivotal role in the dynamic apical domain movement that leads to GroES binding and efficient encapsulation of substrate proteins
    • K. Machida, R. Fujiwara, T. Tanaka, I. Sakane, K. Hongo, T. Mizobata, and Y. Kawata Gly192 at hinge 2 site in the chaperonin GroEL plays a pivotal role in the dynamic apical domain movement that leads to GroES binding and efficient encapsulation of substrate proteins Biochim. Biophys. Acta 1794 2009 1344 1354
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 1344-1354
    • MacHida, K.1    Fujiwara, R.2    Tanaka, T.3    Sakane, I.4    Hongo, K.5    Mizobata, T.6    Kawata, Y.7
  • 17
    • 0028370512 scopus 로고
    • Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin
    • H. Kubota, G. Hynes, A. Carne, A. Ashworth, and K. Willison Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin Curr. Biol. 4 1994 89 99
    • (1994) Curr. Biol. , vol.4 , pp. 89-99
    • Kubota, H.1    Hynes, G.2    Carne, A.3    Ashworth, A.4    Willison, K.5
  • 18
    • 0028938750 scopus 로고
    • The eighth Cct gene, Cctq, encoding the theta subunit of the cytosolic chaperonin containing TCP-1
    • H. Kubota, G. Hynes, and K. Willison The eighth Cct gene, Cctq, encoding the theta subunit of the cytosolic chaperonin containing TCP-1 Gene 154 1995 231 236
    • (1995) Gene , vol.154 , pp. 231-236
    • Kubota, H.1    Hynes, G.2    Willison, K.3
  • 19
    • 54049139149 scopus 로고    scopus 로고
    • A human cell-derived in vitro coupled transcription/translation system optimized for production of recombinant proteins
    • S. Mikami, T. Kobayashi, M. Masutani, S. Yokoyama, and H. Imataka A human cell-derived in vitro coupled transcription/translation system optimized for production of recombinant proteins Protein Expr. Purif. 62 2008 190 198
    • (2008) Protein Expr. Purif. , vol.62 , pp. 190-198
    • Mikami, S.1    Kobayashi, T.2    Masutani, M.3    Yokoyama, S.4    Imataka, H.5
  • 20
    • 33746870434 scopus 로고    scopus 로고
    • Rescue system for measles virus from cloned cDNA driven by vaccinia virus Lister vaccine strain
    • DOI 10.1016/j.jviromet.2006.05.029, PII S0166093406001856
    • Y. Nakatsu, M. Takeda, M. Kidokoro, M. Kohara, and Y. Yanagi Rescue system for measles virus from cloned cDNA driven by vaccinia virus Lister vaccine strain J. Virol. Methods 137 2006 152 155 (Pubitemid 44189501)
    • (2006) Journal of Virological Methods , vol.137 , Issue.1 , pp. 152-155
    • Nakatsu, Y.1    Takeda, M.2    Kidokoro, M.3    Kohara, M.4    Yanagi, Y.5
  • 21
    • 33750295885 scopus 로고    scopus 로고
    • Transfection of mammalian cells using linear polyethylenimine is a simple and effective means of producing recombinant adeno-associated virus vectors
    • DOI 10.1016/j.jviromet.2006.07.024, PII S0166093406002771
    • S.E. Reed, E.M. Staley, J.P. Mayginnes, D.J. Pintel, and G.E. Tullis Transfection of mammalian cells using linear polyethylenimine is a simple and effective means of producing recombinant adeno-associated virus vectors J. Virol. Methods 138 2006 85 98 (Pubitemid 44633451)
    • (2006) Journal of Virological Methods , vol.138 , Issue.1-2 , pp. 85-98
    • Reed, S.E.1    Staley, E.M.2    Mayginnes, J.P.3    Pintel, D.J.4    Tullis, G.E.5
  • 22
    • 33846204799 scopus 로고    scopus 로고
    • A hybridoma-based in vitro translation system that efficiently synthesizes glycoproteins
    • DOI 10.1016/j.jbiotec.2006.06.018, PII S0168165606005359
    • S. Mikami, T. Kobayashi, S. Yokoyama, and H. Imataka A hybridoma-based in vitro translation system that efficiently synthesizes glycoproteins J. Biotechnol. 127 2006 65 78 (Pubitemid 46107129)
    • (2006) Journal of Biotechnology , vol.127 , Issue.1 , pp. 65-78
    • Mikami, S.1    Kobayashi, T.2    Yokoyama, S.3    Imataka, H.4
  • 23
    • 33745272858 scopus 로고    scopus 로고
    • Quantitative Actin Folding Reactions using Yeast CCT Purified via an Internal Tag in the CCT3/γ Subunit
    • DOI 10.1016/j.jmb.2006.05.003, PII S0022283606005699
    • G. Pappenberger, E.A. McCormack, and K.R. Willison Quantitative actin folding reactions using yeast CCT purified via an internal tag in the CCT3/gamma subunit J. Mol. Biol. 360 2006 484 496 (Pubitemid 43927828)
    • (2006) Journal of Molecular Biology , vol.360 , Issue.2 , pp. 484-496
    • Pappenberger, G.1    McCormack, E.A.2    Willison, K.R.3
  • 24
    • 0032478545 scopus 로고    scopus 로고
    • Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT
    • DOI 10.1016/S0092-8674(00)81152-6
    • L. Ditzel, J. Lowe, D. Stock, K.O. Stetter, H. Huber, R. Huber, and S. Steinbacher Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT Cell 93 1998 125 138 (Pubitemid 28173558)
    • (1998) Cell , vol.93 , Issue.1 , pp. 125-138
    • Ditzel, L.1    Lowe, J.2    Stock, D.3    Stetter, K.-O.4    Huber, H.5    Huber, R.6    Steinbacher, S.7
  • 28
    • 33846049519 scopus 로고    scopus 로고
    • Limiting factors governing protein expression following polyethylenimine-mediated gene transfer in HEK293-EBNA1 cells
    • DOI 10.1016/j.jbiotec.2006.10.014, PII S0168165606008984
    • E. Carpentier, S. Paris, A.A. Kamen, and Y. Durocher Limiting factors governing protein expression following polyethylenimine-mediated gene transfer in HEK293-EBNA1 cells J. Biotechnol. 128 2007 268 280 (Pubitemid 46074201)
    • (2007) Journal of Biotechnology , vol.128 , Issue.2 , pp. 268-280
    • Carpentier, E.1    Paris, S.2    Kamen, A.A.3    Durocher, Y.4
  • 30
    • 0039797301 scopus 로고
    • Cap-independent translation of mRNA conferred by encephalomyocarditis virus 5' sequence improves the performance of the vaccinia virus/bacteriophage T7 hybrid expression system
    • O. Elroy-Stein, T.R. Fuerst, and B. Moss Cap-independent translation of mRNA conferred by encephalomyocarditis virus 5′ sequence improves the performance of the vaccinia virus/bacteriophage T7 hybrid expression system Proc. Natl. Acad. Sci. USA 86 1989 6126 6130 (Pubitemid 19210614)
    • (1989) Proceedings of the National Academy of Sciences of the United States of America , vol.86 , Issue.16 , pp. 6126-6130
    • Elroy-Stein, O.1    Fuerst, T.R.2    Moss, B.3
  • 31
    • 0034865980 scopus 로고    scopus 로고
    • Reconstitution of recombinant TFIIH that can mediate activator-dependent transcription
    • DOI 10.1046/j.1365-2443.2001.00456.x
    • A. Fukuda, J. Yamauchi, S.Y. Wu, C.M. Chiang, M. Muramatsu, and K. Hisatake Reconstitution of recombinant TFIIH that can mediate activator-dependent transcription Genes Cells 6 2001 707 719 (Pubitemid 32791682)
    • (2001) Genes to Cells , vol.6 , Issue.8 , pp. 707-719
    • Fukuda, A.1    Yamauchi, J.2    Wu, S.-Y.3    Chiang, C.-M.4    Muramatsu, M.5    Hisatake, K.6
  • 32
    • 34547178178 scopus 로고    scopus 로고
    • Reconstitution reveals the functional core of mammalian eIF3
    • DOI 10.1038/sj.emboj.7601765, PII 7601765
    • M. Masutani, N. Sonenberg, S. Yokoyama, and H. Imataka Reconstitution reveals the functional core of mammalian eIF3 EMBO J. 26 2007 3373 3383 (Pubitemid 47123530)
    • (2007) EMBO Journal , vol.26 , Issue.14 , pp. 3373-3383
    • Masutani, M.1    Sonenberg, N.2    Yokoyama, S.3    Imataka, H.4
  • 33
    • 0035423032 scopus 로고    scopus 로고
    • The 'sequential allosteric ring' mechanism in the eukaryotic chaperonin-assisted folding of actin and tubulin
    • DOI 10.1093/emboj/20.15.4065
    • O. Llorca, J. Martin-Benito, J. Grantham, M. Ritco-Vonsovici, K.R. Willison, J.L. Carrascosa, and J.M. Valpuesta The 'sequential allosteric ring' mechanism in the eukaryotic chaperonin-assisted folding of actin and tubulin EMBO J. 20 2001 4065 4075 (Pubitemid 32751823)
    • (2001) EMBO Journal , vol.20 , Issue.15 , pp. 4065-4075
    • Llorca, O.1    Martin-Benito, J.2    Grantham, J.3    Ritco-Vonsovici, M.4    Willison, K.R.5    Carrascosa, J.L.6    Valpuesta, J.M.7
  • 34
    • 23044445800 scopus 로고    scopus 로고
    • The cotranslational contacts between ribosome-bound nascent polypeptides and the subunits of the hetero-oligomeric chaperonin TRiC probed by photocross-linking
    • DOI 10.1074/jbc.M504110200
    • S.A. Etchells, A.S. Meyer, A.Y. Yam, A. Roobol, Y. Miao, Y. Shao, M.J. Carden, W.R. Skach, J. Frydman, and A.E. Johnson The cotranslational contacts between ribosome-bound nascent polypeptides and the subunits of the hetero-oligomeric chaperonin TRiC probed by photocross-linking J. Biol. Chem. 280 2005 28118 28126 (Pubitemid 41076930)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.30 , pp. 28118-28126
    • Etchells, S.A.1    Meyer, A.S.2    Yam, A.Y.3    Roobol, A.4    Miao, Y.5    Shao, Y.6    Carden, M.J.7    Skach, W.R.8    Frydman, J.9    Johnson, A.E.10


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