메뉴 건너뛰기




Volumn 18, Issue 1, 1999, Pages 75-84

Compartmentation of protein folding in vivo: Sequestration of non-native polypeptide by the chaperonin-GimC system

Author keywords

Actin; Chaperonin assisted folding; GimC; TRiC; Yeast

Indexed keywords

ACTIN; CHAPERONE; CHAPERONIN;

EID: 0033521523     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.1.75     Document Type: Article
Times cited : (179)

References (51)
  • 2
    • 0030598919 scopus 로고    scopus 로고
    • Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding
    • Buchberger, A., Schröder, H., Hesterkamp, T., Schönfeld, H.-J. and Bukau, B. (1996) Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding. J. Mol. Biol., 261, 328-333.
    • (1996) J. Mol. Biol. , vol.261 , pp. 328-333
    • Buchberger, A.1    Schröder, H.2    Hesterkamp, T.3    Schönfeld, H.-J.4    Bukau, B.5
  • 3
    • 0028586011 scopus 로고
    • Two yeast genes with similarity to TCP-1 are required for microtubule and actin function in vivo
    • Chen, X., Sullivan, D.S. and Huffaker, T.C. (1994) Two yeast genes with similarity to TCP-1 are required for microtubule and actin function in vivo. Proc. Natl Acad. Sci. USA, 91, 9111-9115.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 9111-9115
    • Chen, X.1    Sullivan, D.S.2    Huffaker, T.C.3
  • 4
    • 0032478545 scopus 로고    scopus 로고
    • Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT
    • Ditzel, L., Löwe, J., Stock, D., Stetter, K.O., Huber, H., Huber, R. and Steinbacher, S. (1998) Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Cell, 93, 125-138.
    • (1998) Cell , vol.93 , pp. 125-138
    • Ditzel, L.1    Löwe, J.2    Stock, D.3    Stetter, K.O.4    Huber, H.5    Huber, R.6    Steinbacher, S.7
  • 5
    • 25744477821 scopus 로고
    • A novel protein Nup133p with distinct roles in poly (A)+ RNA transport and nuclear pore distribution
    • Doye, V., Wepf, R. and Hurt, E.C. (1994) A novel protein Nup133p with distinct roles in poly (A)+ RNA transport and nuclear pore distribution. EMBO J., 14, 76-87.
    • (1994) EMBO J. , vol.14 , pp. 76-87
    • Doye, V.1    Wepf, R.2    Hurt, E.C.3
  • 6
    • 0030928059 scopus 로고    scopus 로고
    • Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells
    • Eggers, D.K., Welch, W.J. and Hansen, W.J. (1997) Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells. Mol. Biol. Cell. 8, 1559-1573.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 1559-1573
    • Eggers, D.K.1    Welch, W.J.2    Hansen, W.J.3
  • 7
    • 0023668329 scopus 로고
    • Proteins as molecular chaperones
    • Ellis, J. (1987) Proteins as molecular chaperones. Nature, 328, 378-379.
    • (1987) Nature , vol.328 , pp. 378-379
    • Ellis, J.1
  • 8
    • 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
  • 9
    • 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., Sondeck, 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    Sondeck, S.4    Horwich, A.L.5
  • 10
    • 0030910349 scopus 로고    scopus 로고
    • GroEL-mediated protein folding
    • Fenton, W.A. and Horwich, A.L. (1997) GroEL-mediated protein folding. Protein Sci., 6, 743-760.
    • (1997) Protein Sci. , vol.6 , pp. 743-760
    • Fenton, W.A.1    Horwich, A.L.2
  • 11
    • 0029980091 scopus 로고    scopus 로고
    • Principles of chaperone-assisted protein folding: Differences between in vitro and in vivo mechanisms
    • Frydman, J. and Hartl, F.U. (1996) Principles of chaperone-assisted protein folding: differences between in vitro and in vivo mechanisms. Science, 272, 1497-1502.
    • (1996) Science , vol.272 , pp. 1497-1502
    • Frydman, J.1    Hartl, F.U.2
  • 12
    • 0028361309 scopus 로고
    • Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
    • Frydman, J., Nimmesgern, E., Ohtsuka, K. and Hanl, 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    Hanl, F.U.4
  • 13
    • 0026776331 scopus 로고
    • A cytoplasmic chaperonin that catalyzes β-actin folding
    • Gao, Y., Thomas, J.O., Chow, R.L., Lee, G.H. and Cowan, N.J. (1992) A cytoplasmic chaperonin that catalyzes β-actin folding. Cell, 69, 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
  • 14
    • 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
  • 15
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M.-J. and Sambrook, J. (1992) Protein folding in the cell. Nature, 355, 33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.-J.1    Sambrook, J.2
  • 17
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F.U. (1996) Molecular chaperones in cellular protein folding. Nature, 381, 571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 18
    • 0027214204 scopus 로고
    • Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL
    • Horwich, A.L., Low, K.B., Fenton, W.A., Hirshfield, I.N. and Furtak, K. (1993) Folding in vivo of bacterial cytoplasmic proteins: role of GroEL. Cell, 74, 909-917.
    • (1993) Cell , vol.74 , pp. 909-917
    • Horwich, A.L.1    Low, K.B.2    Fenton, W.A.3    Hirshfield, I.N.4    Furtak, K.5
  • 19
    • 0031016469 scopus 로고    scopus 로고
    • Functional specificity among Hsp70 molecular chaperones
    • James, P., Pfund, C. and Craig, E.A. (1997) Functional specificity among Hsp70 molecular chaperones. Science, 275, 387-389.
    • (1997) Science , vol.275 , pp. 387-389
    • James, P.1    Pfund, C.2    Craig, E.A.3
  • 20
    • 0030809270 scopus 로고    scopus 로고
    • Protein folding in vivo: Unraveling complex pathways
    • Johnson, J.L. and Craig, E.A. (1997) Protein folding in vivo: unraveling complex pathways. Cell, 90, 201-204.
    • (1997) Cell , vol.90 , pp. 201-204
    • Johnson, J.L.1    Craig, E.A.2
  • 22
    • 0029591856 scopus 로고
    • Actin filaments in yeast are unstable in the absence of capping protein or fimbrin
    • Karpova, T.S., Tatchell, K. and Cooper, J.A. (1995) Actin filaments in yeast are unstable in the absence of capping protein or fimbrin. J. Cell Biol., 131, 1483-1493.
    • (1995) J. Cell Biol. , vol.131 , pp. 1483-1493
    • Karpova, T.S.1    Tatchell, K.2    Cooper, J.A.3
  • 23
    • 0030668929 scopus 로고    scopus 로고
    • Structure of the substrate binding domain of the thermosome, an Archaeal Group II chaperonin
    • Klumpp, M., Baumeister, W. and Essen, L.-O. (1997) Structure of the substrate binding domain of the thermosome, an Archaeal Group II chaperonin. Cell, 91, 263-270.
    • (1997) Cell , vol.91 , pp. 263-270
    • Klumpp, M.1    Baumeister, W.2    Essen, L.-O.3
  • 24
    • 0029062216 scopus 로고
    • The chaperonin containing t-complex polypeptide 1 (TCP-1) - Multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol
    • Kubota, H., Hynes, G. and Willison, K. (1995) The chaperonin containing t-complex polypeptide 1 (TCP-1) - multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol. Eur. J. Biochem., 230, 3-16.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 3-16
    • Kubota, H.1    Hynes, G.2    Willison, K.3
  • 25
    • 0016361516 scopus 로고
    • Actin is the naturally occuring inhibitor of deoxyribonuclease I
    • Lazarides, E. and Lindberg, U. (1974) Actin is the naturally occuring inhibitor of deoxyribonuclease I. Proc. Natl Acad. Sci. USA, 71, 4742-4746.
    • (1974) Proc. Natl Acad. Sci. USA , vol.71 , pp. 4742-4746
    • Lazarides, E.1    Lindberg, U.2
  • 27
    • 0030842428 scopus 로고    scopus 로고
    • Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT micro-complexes
    • Liou, A.K. and Willison, K.R. (1997) Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT micro-complexes. EMBO J., 16, 4311-1316.
    • (1997) EMBO J. , vol.16 , pp. 4311-11316
    • Liou, A.K.1    Willison, K.R.2
  • 28
    • 0032562815 scopus 로고    scopus 로고
    • ATP binding induces large conformational changes in the apical and equatorial domains of the eukaryotic chaperonin containing TCP-1 complex
    • Llorca, O., Smyth, M.G., Marco, S., Carrascosa, J.L., Willison, K.R. and Valpuesta, J.M. (1998) ATP binding induces large conformational changes in the apical and equatorial domains of the eukaryotic chaperonin containing TCP-1 complex. J. Biol. Chem., 273, 10091-10094.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10091-10094
    • Llorca, O.1    Smyth, M.G.2    Marco, S.3    Carrascosa, J.L.4    Willison, K.R.5    Valpuesta, J.M.6
  • 29
    • 0029935849 scopus 로고    scopus 로고
    • Construction of a CUP1 promotor-based vector to modulate gene expression in Saccharomyces cerevisiae
    • Mascorro-Gallardo, J.O., Covarrubias, A.A. and Gaxiola, R. (1996) Construction of a CUP1 promotor-based vector to modulate gene expression in Saccharomyces cerevisiae. Gene, 172, 169-170.
    • (1996) Gene , vol.172 , pp. 169-170
    • Mascorro-Gallardo, J.O.1    Covarrubias, A.A.2    Gaxiola, R.3
  • 30
    • 0028196813 scopus 로고
    • Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates
    • Melki, R. and Cowan, N.J. (1994) Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates. Mol. Cell. Biol., 14, 2895-2904.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2895-2904
    • Melki, R.1    Cowan, N.J.2
  • 31
    • 0028355543 scopus 로고
    • Primary structure and function of a second essential member of the heterooligomeric TCP1 chaperonin complex of yeast, TCP1 β
    • Miklos, D. et al. (1994) Primary structure and function of a second essential member of the heterooligomeric TCP1 chaperonin complex of yeast, TCP1 β. Proc. Natl Acad. Sci. USA, 91, 2743-2747.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 2743-2747
    • Miklos, D.1
  • 33
    • 0030667932 scopus 로고    scopus 로고
    • In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone
    • Nathan, D.F., Vos, M.H. and Lindquist, S. (1997) In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone. Proc. Natl Acad. Sci. USA, 94, 12949-12956.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 12949-12956
    • Nathan, D.F.1    Vos, M.H.2    Lindquist, S.3
  • 34
    • 0030844281 scopus 로고    scopus 로고
    • Recombination of protein domains facilitated by co-translational folding in eukaryotes
    • Netzer, W.J. and Hartl, F.U. (1997) Recombination of protein domains facilitated by co-translational folding in eukaryotes. Nature, 388, 343-349.
    • (1997) Nature , vol.388 , pp. 343-349
    • Netzer, W.J.1    Hartl, F.U.2
  • 35
    • 0032005026 scopus 로고    scopus 로고
    • Protein folding in the cytosol: Chaperonin-dependent and -independent mechanisms
    • Netzer, W.J. and Hartl, F.U. (1998) Protein folding in the cytosol: chaperonin-dependent and -independent mechanisms. Trends Biochem. Sci., 23, 68-73.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 68-73
    • Netzer, W.J.1    Hartl, F.U.2
  • 36
    • 0032528301 scopus 로고    scopus 로고
    • The molecular chaperone ssb of S.Cerevisiae is a component of the ribosome-nascent chain complex
    • Pfund, C., Lopez-Hoyo, N., Ziegelhoffer, T., Schilke, B.A., Lopez-Buesa, P., Walter,W.A., Wiedmann, M. and Craig, E.A. (1998) The molecular chaperone Ssb of S.cerevisiae is a component of the ribosome-nascent chain complex. EMBO J., 17, 3981-3989.
    • (1998) EMBO J. , vol.17 , pp. 3981-3989
    • Pfund, C.1    Lopez-Hoyo, N.2    Ziegelhoffer, T.3    Schilke, B.A.4    Lopez-Buesa, P.5    Wiedmann, M.6    Craig, E.A.7
  • 37
    • 0024456399 scopus 로고
    • Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells
    • Rothman, J.E. (1989) Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells. Cell, 59, 591-601.
    • (1989) Cell , vol.59 , pp. 591-601
    • Rothman, J.E.1
  • 38
    • 0027410046 scopus 로고
    • The pRSET family of T7 promoter expression vectors for Escherichia coli
    • Schoepfer, R. (1993) The pRSET family of T7 promoter expression vectors for Escherichia coli. Gene, 124, 83-85.
    • (1993) Gene , vol.124 , pp. 83-85
    • Schoepfer, R.1
  • 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
  • 44
    • 0026345831 scopus 로고
    • The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes
    • Ursic, D. and Culbertson, M.R. (1991) The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes. Mol. Cell. Biol., 11, 2629-2640.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2629-2640
    • Ursic, D.1    Culbertson, M.R.2
  • 45
    • 0027988048 scopus 로고
    • The essential yeast Tcp1 protein affects actin and microtubules
    • Ursic, D., Sedbrook, J.C., Himmel, K.L. and Culbertson, M.R. (1994) The essential yeast Tcp1 protein affects actin and microtubules. Mol. Biol. Cell, 5, 1065-1080.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 1065-1080
    • Ursic, D.1    Sedbrook, J.C.2    Himmel, K.L.3    Culbertson, M.R.4
  • 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 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
    • 0027933369 scopus 로고
    • GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms
    • Weissman, J.S., Kashi, Y., Fenton, W.A. and Horwich, A.L. (1994) GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms. Cell, 78, 693-702.
    • (1994) Cell , vol.78 , pp. 693-702
    • Weissman, J.S.1    Kashi, Y.2    Fenton, W.A.3    Horwich, A.L.4
  • 50
    • 0027980239 scopus 로고
    • A protein complex required for signal-sequence-specific sorting and translocation
    • Wiedmann, B., Sakai, H., Davis, T.A. and Wiedmann, M. (1994) A protein complex required for signal-sequence-specific sorting and translocation. Nature, 370, 434-440.
    • (1994) Nature , vol.370 , pp. 434-440
    • Wiedmann, B.1    Sakai, H.2    Davis, T.A.3    Wiedmann, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.