메뉴 건너뛰기




Volumn 10, Issue 1, 2000, Pages 26-33

Protein folding in vivo: The importance of molecular chaperones

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 70; PROTEIN; PROTEIN DNAK;

EID: 0033953974     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(99)00044-5     Document Type: Review
Times cited : (174)

References (69)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen C.B. Principles that govern the folding of protein chains. Science. 181:1973;223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 2
    • 0031923551 scopus 로고    scopus 로고
    • Protein self-organization in-vitro and in-vivo: Partitioning between physical biochemistry and cell biology
    • Jaenicke R. Protein self-organization in-vitro and in-vivo: partitioning between physical biochemistry and cell biology. Biol Chem. 379:1998;237-243.
    • (1998) Biol Chem , vol.379 , pp. 237-243
    • Jaenicke, R.1
  • 3
    • 0031239894 scopus 로고    scopus 로고
    • Molecular chaperones: Avoiding the crowd
    • Ellis R.J. Molecular chaperones: avoiding the crowd. Curr Biol. 7:1997;531-533.
    • (1997) Curr Biol , vol.7 , pp. 531-533
    • Ellis, R.J.1
  • 4
    • 0028361309 scopus 로고
    • Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
    • Frydman J., Nimmesgern E., Ohtsuka K., Hartl F.U. Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature. 370:1994;111-117.
    • (1994) Nature , vol.370 , pp. 111-117
    • Frydman, J.1    Nimmesgern, E.2    Ohtsuka, K.3    Hartl, F.U.4
  • 5
    • 0030844281 scopus 로고    scopus 로고
    • Recombination of protein domains facilitated by co-translational folding in eukaryotes
    • Netzer W., Hartl F.U. Recombination of protein domains facilitated by co-translational folding in eukaryotes. Nature. 388:1997;343-349.
    • (1997) Nature , vol.388 , pp. 343-349
    • Netzer, W.1    Hartl, F.U.2
  • 6
    • 0032983520 scopus 로고    scopus 로고
    • Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase
    • This study used a multidomain protein to demonstrate that folding during translation and refolding from denaturant occur through different folding pathways
    • Frydman J., Erdjument-Bromage H., Tempst P., Hartl F.U. Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase. Nat Struct Biol. 6:1999;697-705. This study used a multidomain protein to demonstrate that folding during translation and refolding from denaturant occur through different folding pathways.
    • (1999) Nat Struct Biol , vol.6 , pp. 697-705
    • Frydman, J.1    Erdjument-Bromage, H.2    Tempst, P.3    Hartl, F.U.4
  • 7
    • 0033203533 scopus 로고    scopus 로고
    • Co-translational folding of an alphavirus capsid protein in the cytosol of living cells
    • Nicola A.V., Chen W., Helenius A. Co-translational folding of an alphavirus capsid protein in the cytosol of living cells. Nat Cell Biol. 1:1999;341-345.
    • (1999) Nat Cell Biol , vol.1 , pp. 341-345
    • Nicola, A.V.1    Chen, W.2    Helenius, A.3
  • 8
    • 0028889120 scopus 로고
    • Contribution of cotranslational folding to the rate of formation of native protein structure
    • Fedorov A.N., Baldwin T.O. Contribution of cotranslational folding to the rate of formation of native protein structure. Proc Natl Acad Sci USA. 92:1995;1227-1231.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1227-1231
    • Fedorov, A.N.1    Baldwin, T.O.2
  • 9
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething M.J., Sambrook J. Protein folding in the cell. Nature. 355:1992;33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 10
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • An excellent review of the mechanism and function of the Hsp70 and chaperonin systems
    • Bukau B., Horwich A.L. The Hsp70 and Hsp60 chaperone machines. Cell. 92:1998;351-366. An excellent review of the mechanism and function of the Hsp70 and chaperonin systems.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 11
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl F.U. Molecular chaperones in cellular protein folding. Nature. 381:1996;571-579.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 12
    • 0026649409 scopus 로고
    • The translation machinery and 70 kd heat shock protein cooperate in protein synthesis
    • Nelson R.J., Ziegelhoffer T., Nicolet C., Werner-Washburne M., Craig E.A. The translation machinery and 70 kd heat shock protein cooperate in protein synthesis. Cell. 71:1992;97-105.
    • (1992) Cell , vol.71 , pp. 97-105
    • Nelson, R.J.1    Ziegelhoffer, T.2    Nicolet, C.3    Werner-Washburne, M.4    Craig, E.A.5
  • 13
    • 0025303147 scopus 로고
    • Interaction of Hsp 70 with newly synthesized proteins: Implications for protein folding and assembly
    • Beckmann R.P., Mizzen L.A., Welch W.J. Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly. Science. 248:1990;850-854.
    • (1990) Science , vol.248 , pp. 850-854
    • Beckmann, R.P.1    Mizzen, L.A.2    Welch, W.J.3
  • 14
    • 0028068961 scopus 로고
    • Stabilization of protein synthesis in thermotolerant cells during heat shock. Association of heat shock protein-72 with ribosomal subunits of polysomes
    • Beck S.C., De Maio A. Stabilization of protein synthesis in thermotolerant cells during heat shock. Association of heat shock protein-72 with ribosomal subunits of polysomes. J Biol Chem. 269:1994;21803-21811.
    • (1994) J Biol Chem , vol.269 , pp. 21803-21811
    • Beck, S.C.1    De Maio, A.2
  • 15
    • 0028125299 scopus 로고
    • Complex environment of nascent polypeptide chains
    • Hansen W.J., Lingappa V.R., Welch W.J. Complex environment of nascent polypeptide chains. J Biol Chem. 269:1994;26610-26613.
    • (1994) J Biol Chem , vol.269 , pp. 26610-26613
    • Hansen, W.J.1    Lingappa, V.R.2    Welch, W.J.3
  • 16
    • 0026070260 scopus 로고
    • Sequential action of mitochondrial chaperones in protein import into the matrix
    • Manning-Krieg U., Scherer P.E., Schatz G. Sequential action of mitochondrial chaperones in protein import into the matrix. EMBO J. 10:1991;3273-3280.
    • (1991) EMBO J , vol.10 , pp. 3273-3280
    • Manning-Krieg, U.1    Scherer, P.E.2    Schatz, G.3
  • 17
    • 0027759380 scopus 로고
    • A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome
    • Brodsky J.L., Schekman R. A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome. J Cell Biol. 123:1993;1355-1363.
    • (1993) J Cell Biol , vol.123 , pp. 1355-1363
    • Brodsky, J.L.1    Schekman, R.2
  • 18
    • 0023375806 scopus 로고
    • Complex interactions among members of an essential subfamily of hsp70 genes in Saccharomyces cerevisiae
    • Werner-Washburne M., Stone D.E., Craig E.A. Complex interactions among members of an essential subfamily of hsp70 genes in Saccharomyces cerevisiae. Mol Cell Biol. 7:1987;2568-2577.
    • (1987) Mol Cell Biol , vol.7 , pp. 2568-2577
    • Werner-Washburne, M.1    Stone, D.E.2    Craig, E.A.3
  • 19
    • 0032573163 scopus 로고    scopus 로고
    • Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins
    • This study confirms the important role of the yeast Hsp70 Ssa in the folding of at least some cytosolic proteins by showing that Ssa2 is required for ornithine transcarbamoylase biogenesis in vivo
    • Kim S., Schilke B., Craig E.A., Horwich A.L. Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins. Proc Natl Acad Sci USA. 95:1998;12860-12865. This study confirms the important role of the yeast Hsp70 Ssa in the folding of at least some cytosolic proteins by showing that Ssa2 is required for ornithine transcarbamoylase biogenesis in vivo.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12860-12865
    • Kim, S.1    Schilke, B.2    Craig, E.A.3    Horwich, A.L.4
  • 20
    • 0032528301 scopus 로고    scopus 로고
    • The molecular chaperone Ssb from Saccharomyces-cerevisiae is a component of the ribosome nascent chain complex
    • This study demonstrates, through the use of a photoactivatable cross-linker incorporated into the nascent polypeptide, that the yeast Hsp70 Ssb associates directly with ribosome-bound polypeptide chains
    • Pfund C., Lopezhoyo N., Ziegelhoffer T., Schilke B.A., Lopezbuesa P., Walter W.A., Wiedmann M., Craig E.A. The molecular chaperone Ssb from Saccharomyces-cerevisiae is a component of the ribosome nascent chain complex. EMBO J. 17:1998;3981-3989. This study demonstrates, through the use of a photoactivatable cross-linker incorporated into the nascent polypeptide, that the yeast Hsp70 Ssb associates directly with ribosome-bound polypeptide chains.
    • (1998) EMBO J , vol.17 , pp. 3981-3989
    • Pfund, C.1    Lopezhoyo, N.2    Ziegelhoffer, T.3    Schilke, B.A.4    Lopezbuesa, P.5    Walter, W.A.6    Wiedmann, M.7    Craig, E.A.8
  • 21
    • 0033521588 scopus 로고    scopus 로고
    • In vivo newly translated polypeptides are sequestered in a protected folding environment
    • ••] using yeast cells
    • ••] using yeast cells.
    • (1999) EMBO J , vol.18 , pp. 85-95
    • Thulasiraman, V.1    Yang, C.F.2    Frydman, J.3
  • 22
    • 0023123175 scopus 로고
    • Escherichia coli dnaK null mutants are inviable at high temperature
    • Paek K.H., Walker G.C. Escherichia coli dnaK null mutants are inviable at high temperature. J Bacteriol. 169:1987;283-290.
    • (1987) J Bacteriol , vol.169 , pp. 283-290
    • Paek, K.H.1    Walker, G.C.2
  • 23
    • 0032541496 scopus 로고    scopus 로고
    • Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E. coli
    • This paper investigates the possibility that DnaK cooperates with a closely related protein, Hsc66, and finds that bacterial strains harboring deletions of both genes are viable
    • Hesterkamp T., Bukau B. Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E. coli. EMBO J. 17:1998;4818-4828. This paper investigates the possibility that DnaK cooperates with a closely related protein, Hsc66, and finds that bacterial strains harboring deletions of both genes are viable.
    • (1998) EMBO J , vol.17 , pp. 4818-4828
    • Hesterkamp, T.1    Bukau, B.2
  • 25
    • 0033549770 scopus 로고    scopus 로고
    • Trigger factor and DnaK cooperate in folding of newly synthesized proteins
    • ••], describes the in vivo role of DnaK in chaperoning nascent chains and characterizes the substrate repertoire of DnaK. In addition, these studies reveal that DnaK cooperates with trigger factor (TF) in de novo protein folding. The overexpression of GroEL decreased the transit time of substrates on DnaK, implying directionality in the transfer of folding substrates from DnaK to GroEL
    • ••], describes the in vivo role of DnaK in chaperoning nascent chains and characterizes the substrate repertoire of DnaK. In addition, these studies reveal that DnaK cooperates with trigger factor (TF) in de novo protein folding. The overexpression of GroEL decreased the transit time of substrates on DnaK, implying directionality in the transfer of folding substrates from DnaK to GroEL.
    • (1999) Nature , vol.400 , pp. 693-696
    • Deuerling, E.1    Schulze-Specking, A.2    Tomoyasu, T.3    Mogk, A.4    Bukau, B.5
  • 26
    • 0028864461 scopus 로고
    • A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor
    • Stoller G., Rucknagel K.P., Nierhaus K.H., Schmid F.X., Fischer G., Rahfeld J.U. A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor. EMBO J. 14:1995;4939-4948.
    • (1995) EMBO J , vol.14 , pp. 4939-4948
    • Stoller, G.1    Rucknagel, K.P.2    Nierhaus, K.H.3    Schmid, F.X.4    Fischer, G.5    Rahfeld, J.U.6
  • 27
    • 0025003789 scopus 로고
    • Trigger factor depletion or overproduction causes defective cell division but does not block protein export
    • Guthrie B., Wickner W. Trigger factor depletion or overproduction causes defective cell division but does not block protein export. J Bacteriol. 172:1990;5555-5562.
    • (1990) J Bacteriol , vol.172 , pp. 5555-5562
    • Guthrie, B.1    Wickner, W.2
  • 28
    • 0029112391 scopus 로고
    • NAC covers ribosome-associated nascent chains thereby forming a protective environment for regions of nascent chains just emerging from the peptidyl transferase center
    • Wang S., Sakai H., Wiedmann M. NAC covers ribosome-associated nascent chains thereby forming a protective environment for regions of nascent chains just emerging from the peptidyl transferase center. J Cell Biol. 130:1995;519-528.
    • (1995) J Cell Biol , vol.130 , pp. 519-528
    • Wang, S.1    Sakai, H.2    Wiedmann, M.3
  • 29
    • 0032481303 scopus 로고    scopus 로고
    • A novel protein complex promoting formation of functional alpha- And gamma-tubulin
    • This paper reports the identification of yeast GimC, a novel chaperone complex
    • Geissler S., Siegers K., Schiebel E. A novel protein complex promoting formation of functional alpha- and gamma-tubulin. EMBO J. 17:1998;952-966. This paper reports the identification of yeast GimC, a novel chaperone complex.
    • (1998) EMBO J , vol.17 , pp. 952-966
    • Geissler, S.1    Siegers, K.2    Schiebel, E.3
  • 32
    • 0033521523 scopus 로고    scopus 로고
    • Compartmentation of protein folding in vivo: Sequestration of non-native polypeptide by the chaperonin-GimC system
    • ••], assessing the effects of trap GroEL expression on growth and protein folding in the budding yeast S. cerevisiae. Again, cell growth is unaffected by trap GroEL and most newly made polypeptides are not detectably bound by the trap; however, mutants of TRiC or its putative co-chaperone GimC do cause many newly made polypeptides to be exposed to the trap. These important findings also suggest that GimC and TRiC make essential contributions to the compartmentation of protein folding in the eukaryotic cytosol. Kinetic analysis of actin folding and chaperone interactions indicate that GimC acts on or after TRiC in the folding pathway
    • ••], assessing the effects of trap GroEL expression on growth and protein folding in the budding yeast S. cerevisiae. Again, cell growth is unaffected by trap GroEL and most newly made polypeptides are not detectably bound by the trap; however, mutants of TRiC or its putative co-chaperone GimC do cause many newly made polypeptides to be exposed to the trap. These important findings also suggest that GimC and TRiC make essential contributions to the compartmentation of protein folding in the eukaryotic cytosol. Kinetic analysis of actin folding and chaperone interactions indicate that GimC acts on or after TRiC in the folding pathway.
    • (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
  • 33
    • 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., Willison K. The chaperonin containing T-complex polypeptide-1 (Tcp-1): multisubunit machinery assisting in protein-folding and assembly in the eukaryotic cytosol. Eur J Biochem. 230:1995;3-16.
    • (1995) Eur J Biochem , vol.230 , pp. 3-16
    • Kubota, H.1    Hynes, G.2    Willison, K.3
  • 34
    • 0032701797 scopus 로고    scopus 로고
    • Group II chaperonins: New TRiC(k)s and turns of a protein folding machine
    • An up-to-date review of current knowledge of group II chaperonin function
    • Gutsche I., Essen L.O., Baumeister W. Group II chaperonins: new TRiC(k)s and turns of a protein folding machine. J Mol Biol. 293:1999;295-312. An up-to-date review of current knowledge of group II chaperonin function.
    • (1999) J Mol Biol , vol.293 , pp. 295-312
    • Gutsche, I.1    Essen, L.O.2    Baumeister, W.3
  • 35
    • 0033574162 scopus 로고    scopus 로고
    • The cytosolic class II chaperonin CCT recognizes delineated hydrophobic sequences in its target proteins
    • This paper describes a deletion analysis to identify chaperonin-binding determinants of actin. The authors found that three separate regions in actin are required for binding to TRiC/CCT. This study provides support for the idea the interaction of the actin substrate with this chaperonin is polyvalent and occurs through multiple contacts
    • Rommelaere H., De Neve M., Melki R., Vandekerckhove J., Ampe C. The cytosolic class II chaperonin CCT recognizes delineated hydrophobic sequences in its target proteins. Biochemistry. 38:1999;3246-3257. This paper describes a deletion analysis to identify chaperonin-binding determinants of actin. The authors found that three separate regions in actin are required for binding to TRiC/CCT. This study provides support for the idea the interaction of the actin substrate with this chaperonin is polyvalent and occurs through multiple contacts.
    • (1999) Biochemistry , vol.38 , pp. 3246-3257
    • Rommelaere, H.1    De Neve, M.2    Melki, R.3    Vandekerckhove, J.4    Ampe, C.5
  • 36
    • 0028334547 scopus 로고
    • Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha-lactalbumin
    • Hayer-Hartl M.K., Ewbank J.J., Creighton T.E., Hartl F.U. Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha-lactalbumin. EMBO J. 13:1994;3192-3202.
    • (1994) EMBO J , vol.13 , pp. 3192-3202
    • Hayer-Hartl, M.K.1    Ewbank, J.J.2    Creighton, T.E.3    Hartl, F.U.4
  • 37
    • 0030050614 scopus 로고    scopus 로고
    • A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo
    • Lorimer G.H. A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo. FASEB J. 10:1996;5-9.
    • (1996) FASEB J , vol.10 , pp. 5-9
    • Lorimer, G.H.1
  • 38
    • 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., Furtak K. Folding in vivo of bacterial cytoplasmic proteins: role of GroEL. Cell. 74:1993;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
  • 39
    • 0030750584 scopus 로고    scopus 로고
    • In-vivo observation of polypeptide flux through the bacterial chaperonin system
    • Ewalt K., Hendrick J.P., Houry W.A., Hartl F.U. In-vivo observation of polypeptide flux through the bacterial chaperonin system. Cell. 90:1997;491-500.
    • (1997) Cell , vol.90 , pp. 491-500
    • Ewalt, K.1    Hendrick, J.P.2    Houry, W.A.3    Hartl, F.U.4
  • 40
    • 0033547324 scopus 로고    scopus 로고
    • Identification of in vivo substrates of the chaperonin GroEL
    • A remarkable and detailed examination of the in vivo substrates of GroEL, including the identification by mass spectroscopy of over 50 abundant endogenous substrates. These proteins do not share a common consensus sequence, but instead are significantly enriched for a specific multiple α/β/α domain architecture. Another intriguing finding of this report is the identification of a number of pre-existing proteins that return continually to GroEL throughout the course of their lifetime
    • Houry W.A., Frishman D., Eckerskorn C., Lottspeich F., Hartl F.U. Identification of in vivo substrates of the chaperonin GroEL. Nature. 402:1999;147-154. A remarkable and detailed examination of the in vivo substrates of GroEL, including the identification by mass spectroscopy of over 50 abundant endogenous substrates. These proteins do not share a common consensus sequence, but instead are significantly enriched for a specific multiple α/β/α domain architecture. Another intriguing finding of this report is the identification of a number of pre-existing proteins that return continually to GroEL throughout the course of their lifetime.
    • (1999) Nature , vol.402 , pp. 147-154
    • Houry, W.A.1    Frishman, D.2    Eckerskorn, C.3    Lottspeich, F.4    Hartl, F.U.5
  • 41
    • 0032531727 scopus 로고    scopus 로고
    • Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non-identical requirement for hsp60 and hsp10
    • An analysis of yeast mitochondrial Hsp60 and Hsp10 function in protein folding using loss-of-function alleles in each gene. Interestingly, similar, but nonidentical, proteins became aggregated owing to loss of function in either Hsp60 or Hsp10
    • Dubaquie Y., Looser R., Funfschilling U., Jeno P., Rospert S. Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non-identical requirement for hsp60 and hsp10. EMBO J. 17:1998;5868-5876. An analysis of yeast mitochondrial Hsp60 and Hsp10 function in protein folding using loss-of-function alleles in each gene. Interestingly, similar, but nonidentical, proteins became aggregated owing to loss of function in either Hsp60 or Hsp10.
    • (1998) EMBO J , vol.17 , pp. 5868-5876
    • Dubaquie, Y.1    Looser, R.2    Funfschilling, U.3    Jeno, P.4    Rospert, S.5
  • 43
    • 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., Horwich A.L. Chaperonin-mediated folding in the eukaryotic cytosol proceeds through rounds of release of native and nonnative forms. Cell. 89:1997;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
  • 44
    • 0031725057 scopus 로고    scopus 로고
    • Maturation of human cyclin E requires the function of eukaryotic chaperonin CCT
    • Won K.A., Schumacher R.J., Farr G.W., Horwich A.L., Reed S.I. Maturation of human cyclin E requires the function of eukaryotic chaperonin CCT. Mol Cell Biol. 18:1998;7584-7589.
    • (1998) Mol Cell Biol , vol.18 , pp. 7584-7589
    • Won, K.A.1    Schumacher, R.J.2    Farr, G.W.3    Horwich, A.L.4    Reed, S.I.5
  • 45
    • 0033578722 scopus 로고    scopus 로고
    • Myosin II folding is mediated by a molecular chaperonin
    • Srikakulam R., Winkelmann D.A. Myosin II folding is mediated by a molecular chaperonin. J Biol Chem. 274:1999;27265-27273.
    • (1999) J Biol Chem , vol.274 , pp. 27265-27273
    • Srikakulam, R.1    Winkelmann, D.A.2
  • 46
    • 0030809270 scopus 로고    scopus 로고
    • Protein folding in vivo: Unraveling complex pathways
    • Johnson J.L., Craig E.A. Protein folding in vivo: unraveling complex pathways. Cell. 90:1997;201-204.
    • (1997) Cell , vol.90 , pp. 201-204
    • Johnson, J.L.1    Craig, E.A.2
  • 47
    • 0033602228 scopus 로고    scopus 로고
    • Molecular chaperones: Pathways and networks
    • Ellis R.J. Molecular chaperones: pathways and networks. Curr Biol. 9:1999;137-139.
    • (1999) Curr Biol , vol.9 , pp. 137-139
    • Ellis, R.J.1
  • 48
    • 0030560763 scopus 로고    scopus 로고
    • Growing-up in a dangerous environment: A network of multiple targeting and folding pathways for nascent polypeptides in the cytosol
    • Bukau B., Hesterkamp T., Luirink J. Growing-up in a dangerous environment: a network of multiple targeting and folding pathways for nascent polypeptides in the cytosol. Trends Cell Biol. 6:1996;480-486.
    • (1996) Trends Cell Biol , vol.6 , pp. 480-486
    • Bukau, B.1    Hesterkamp, T.2    Luirink, J.3
  • 49
    • 0030042460 scopus 로고    scopus 로고
    • Protein folding in the cell: Competing models of chaperonin function
    • Ellis R.J., Hartl F.U. Protein folding in the cell: competing models of chaperonin function. FASEB J. 10:1996;20-26.
    • (1996) FASEB J , vol.10 , pp. 20-26
    • Ellis, R.J.1    Hartl, F.U.2
  • 50
    • 0029980091 scopus 로고    scopus 로고
    • Principles of chaperone-assisted protein folding: Differences between in vitro and in vivo mechanisms
    • Frydman J., Hartl F.U. Principles of chaperone-assisted protein folding: differences between in vitro and in vivo mechanisms. Science. 272:1996;1497-1502.
    • (1996) Science , vol.272 , pp. 1497-1502
    • Frydman, J.1    Hartl, F.U.2
  • 51
    • 0030598919 scopus 로고    scopus 로고
    • Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding
    • Buchberger A., Schroder H., Hesterkamp T., Schonfeld H.J., Bukau B. Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding. J Mol Biol. 261:1996;328-333.
    • (1996) J Mol Biol , vol.261 , pp. 328-333
    • Buchberger, A.1    Schroder, H.2    Hesterkamp, T.3    Schonfeld, H.J.4    Bukau, B.5
  • 52
    • 0032103439 scopus 로고    scopus 로고
    • The J-domain family and the recruitment of chaperone power
    • Kelley W.L. The J-domain family and the recruitment of chaperone power. Trends Biochem Sci. 23:1998;222-227.
    • (1998) Trends Biochem Sci , vol.23 , pp. 222-227
    • Kelley, W.L.1
  • 53
    • 0029934520 scopus 로고    scopus 로고
    • Differential requirement for the mitochondrial Hsp70-Tim44 complex in unfolding and translocation of preproteins
    • Voos W., von Ahsen O., Muller H., Guiard B., Rassow J., Pfanner N. Differential requirement for the mitochondrial Hsp70-Tim44 complex in unfolding and translocation of preproteins. EMBO J. 15:1996;2668-2677.
    • (1996) EMBO J , vol.15 , pp. 2668-2677
    • Voos, W.1    Von Ahsen, O.2    Muller, H.3    Guiard, B.4    Rassow, J.5    Pfanner, N.6
  • 54
    • 0032541489 scopus 로고    scopus 로고
    • Zuotin; A ribosome-associated DnaJ molecular chaperone
    • This paper describes a new member of the J-domain class of proteins, zuotin, which is ribosome associated. As zuotin deletion strains display phenotypes identical to mutants of Ssb, a ribosome-bound member of the Hsp70 family, the authors postulate that zuotin may play a role in modulating the activity or substrate binding of its putative partner Ssb proteins
    • Yan W., Schilke B., Pfund C., Walter W., Kim S., Craig E.A. Zuotin; a ribosome-associated DnaJ molecular chaperone. EMBO J. 17:1998;4809-4817. This paper describes a new member of the J-domain class of proteins, zuotin, which is ribosome associated. As zuotin deletion strains display phenotypes identical to mutants of Ssb, a ribosome-bound member of the Hsp70 family, the authors postulate that zuotin may play a role in modulating the activity or substrate binding of its putative partner Ssb proteins.
    • (1998) EMBO J , vol.17 , pp. 4809-4817
    • Yan, W.1    Schilke, B.2    Pfund, C.3    Walter, W.4    Kim, S.5    Craig, E.A.6
  • 55
    • 0029798054 scopus 로고    scopus 로고
    • Interaction of the protein import and folding machineries of the chloroplast
    • Kessler F., Blobel G. Interaction of the protein import and folding machineries of the chloroplast. Proc Natl Acad Sci USA. 93:1996;7684-7689.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 7684-7689
    • Kessler, F.1    Blobel, G.2
  • 56
    • 0031896846 scopus 로고    scopus 로고
    • Directionality of polypeptide transfer in the mitochondrial pathway of chaperone-mediated protein-folding
    • Heyrovska N., Frydman J., Hohfeld J., Hartl F.U. Directionality of polypeptide transfer in the mitochondrial pathway of chaperone-mediated protein-folding. Biol Chem. 379:1998;301-309.
    • (1998) Biol Chem , vol.379 , pp. 301-309
    • Heyrovska, N.1    Frydman, J.2    Hohfeld, J.3    Hartl, F.U.4
  • 57
    • 0027536925 scopus 로고
    • + reductase upon its import into chloroplasts
    • + reductase upon its import into chloroplasts. FEBS Lett. 320:1993;198-202.
    • (1993) FEBS Lett , vol.320 , pp. 198-202
    • Tsugeki, R.1    Nishimura, M.2
  • 58
    • 0026596223 scopus 로고
    • Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
    • Langer T., Lu C., Echols H., Flanagan J., Hayer M.K., Hartl F.U. Successive action of DnaK, 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
  • 59
    • 0028068610 scopus 로고
    • Sequential folding of UmuC by the Hsp70 and Hsp60 chaperone complexes of Escherichia coli
    • Petit M.A., Bedale W., Osipiuk J. Sequential folding of UmuC by the Hsp70 and Hsp60 chaperone complexes of Escherichia coli. J Biol Chem. 269:1994;23824-23829.
    • (1994) J Biol Chem , vol.269 , pp. 23824-23829
    • Petit, M.A.1    Bedale, W.2    Osipiuk, J.3
  • 60
    • 0031026329 scopus 로고    scopus 로고
    • Trigger factor associates with GroEL in vivo and promotes its binding to certain polypeptides
    • Kandror O., Sherman M., Moerschell R., Goldberg A.L. Trigger factor associates with GroEL in vivo and promotes its binding to certain polypeptides. J Biol Chem. 272:1997;1730-1734.
    • (1997) J Biol Chem , vol.272 , pp. 1730-1734
    • Kandror, O.1    Sherman, M.2    Moerschell, R.3    Goldberg, A.L.4
  • 61
    • 0030667932 scopus 로고    scopus 로고
    • In-vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone
    • Nathan D.F., Vos M.H., Lindquist S. In-vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone. Proc Natl Acad Sci USA. 94:1997;12949-12956.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12949-12956
    • Nathan, D.F.1    Vos, M.H.2    Lindquist, S.3
  • 62
    • 0033168520 scopus 로고    scopus 로고
    • Hsp90's secrets unfold: New insights from structural and functional studies
    • Caplan A.J. Hsp90's secrets unfold: new insights from structural and functional studies. Trends Cell Biol. 9:1999;262-268.
    • (1999) Trends Cell Biol , vol.9 , pp. 262-268
    • Caplan, A.J.1
  • 63
    • 0031106603 scopus 로고    scopus 로고
    • Chaperones get in touch: The Hip-Hop connection
    • Frydman J., Hohfeld J. Chaperones get in touch: the Hip-Hop connection. Trends Biochem Sci. 22:1997;87-92.
    • (1997) Trends Biochem Sci , vol.22 , pp. 87-92
    • Frydman, J.1    Hohfeld, J.2
  • 64
    • 0030623528 scopus 로고    scopus 로고
    • Ribosomes and ribosomal-RNA as chaperones for folding of proteins
    • Kudlicki W., Coffman A., Kramer G., Hardesty B. Ribosomes and ribosomal-RNA as chaperones for folding of proteins. Fold Des. 2:1997;101-108.
    • (1997) Fold des , vol.2 , pp. 101-108
    • Kudlicki, W.1    Coffman, A.2    Kramer, G.3    Hardesty, B.4
  • 65
    • 0032496137 scopus 로고    scopus 로고
    • Chaperone properties of bacterial elongation-factor EF-Tu
    • Caldas T.D., Elyaagoubi A., Richarme G. Chaperone properties of bacterial elongation-factor EF-Tu. J Biol Chem. 273:1998;11478-11482.
    • (1998) J Biol Chem , vol.273 , pp. 11478-11482
    • Caldas, T.D.1    Elyaagoubi, A.2    Richarme, G.3
  • 66
    • 0033572725 scopus 로고    scopus 로고
    • Effects of macromolecular crowding on protein folding and aggregation
    • This exciting paper provides experimental evidence that the conditions of macromolecular crowding prevalent in the cell may profoundly affect the folding process. By studying the effect of crowding agents on the refolding of the model protein lysozyme, the authors make two important observations. Firstly, that crowding essentially abolishes spontaneous folding by favoring aggregation and secondly, that crowded conditions can greatly enhance chaperone activity
    • Van den Berg B., Ellis R.J., Dobson C.M. Effects of macromolecular crowding on protein folding and aggregation. EMBO J. 18:1999;6927-6933. This exciting paper provides experimental evidence that the conditions of macromolecular crowding prevalent in the cell may profoundly affect the folding process. By studying the effect of crowding agents on the refolding of the model protein lysozyme, the authors make two important observations. Firstly, that crowding essentially abolishes spontaneous folding by favoring aggregation and secondly, that crowded conditions can greatly enhance chaperone activity.
    • (1999) EMBO J , vol.18 , pp. 6927-6933
    • Van Den Berg, B.1    Ellis, R.J.2    Dobson, C.M.3
  • 67
    • 0033400674 scopus 로고    scopus 로고
    • Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TriC
    • This paper demonstrates that the chaperonin TRiC/CCT is required for the folding of the VHL tumor suppressor protein and its assembly into a functional complex with its partner proteins elongin B and elongin C. VHL interacts with TRiC through a 55 amino acid domain that is a target of tumor-causing mutations. Some of these mutations disrupt the interaction of VHL with TRiC, suggesting that loss of protein function may arise through mutations that disrupt the chaperone-substrate interaction
    • Feldman D.E., Thulasiraman V., Ferreyra R., Frydman J. Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TriC. Mol Cell. 4:1999;1051-1061. This paper demonstrates that the chaperonin TRiC/CCT is required for the folding of the VHL tumor suppressor protein and its assembly into a functional complex with its partner proteins elongin B and elongin C. VHL interacts with TRiC through a 55 amino acid domain that is a target of tumor-causing mutations. Some of these mutations disrupt the interaction of VHL with TRiC, suggesting that loss of protein function may arise through mutations that disrupt the chaperone-substrate interaction.
    • (1999) Mol Cell , vol.4 , pp. 1051-1061
    • Feldman, D.E.1    Thulasiraman, V.2    Ferreyra, R.3    Frydman, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.