메뉴 건너뛰기




Volumn 9, Issue 1, 1999, Pages 102-110

Principles of protein folding in the cellular environment

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; CHAPERONE;

EID: 0032822103     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(99)80013-X     Document Type: Article
Times cited : (273)

References (66)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen CB 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
    • 0031703811 scopus 로고    scopus 로고
    • Forty years under the central dogma
    • A fascinating account of the origin of the central dogma and its current status, marred only by the incorrect suggestion in the penultimate paragraph that chaperonins determine protein conformation.
    • Thieffry D, Sarkar S Forty years under the central dogma. Trends Biochem Sci. 23:1998;312-316. A fascinating account of the origin of the central dogma and its current status, marred only by the incorrect suggestion in the penultimate paragraph that chaperonins determine protein conformation.
    • (1998) Trends Biochem Sci , vol.23 , pp. 312-316
    • Thieffry, D.1    Sarkar, S.2
  • 4
    • 0024314918 scopus 로고
    • Molecular chaperones: Proteins essential for the biogenesis of some macromolecular structures
    • Ellis RJ, Hemmingsen SM Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures. Trends Biochem Sci. 14:1989;339-342.
    • (1989) Trends Biochem Sci , vol.14 , pp. 339-342
    • Ellis, R.J.1    Hemmingsen, S.M.2
  • 5
    • 0032489016 scopus 로고    scopus 로고
    • The hsp70 and hsp60 chaperone machines
    • An excellent account of recent research findings.
    • Bukau B, Horwich AL The hsp70 and hsp60 chaperone machines. Cell. 92:1998;351-366. An excellent account of recent research findings.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 6
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl FU Molecular chaperones in cellular protein folding. Nature. 381:1996;571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 7
    • 0031590293 scopus 로고    scopus 로고
    • Do molecular chaperones have to be proteins?
    • A survey of the current status of the general concept of molecular chaperones and their definition, and recent suggestions that the term should be extended to RNA and phospholipids.
    • Ellis RJ Do molecular chaperones have to be proteins? Biochem Biophys Res Commun. 238:1997;687-692. A survey of the current status of the general concept of molecular chaperones and their definition, and recent suggestions that the term should be extended to RNA and phospholipids.
    • (1997) Biochem Biophys Res Commun , vol.238 , pp. 687-692
    • Ellis, R.J.1
  • 8
    • 0031883764 scopus 로고    scopus 로고
    • Steric chaperones
    • ••] is discussed in terms of the suggested division of molecular chaperones into two categories, termed steric and nonsteric.
    • ••] is discussed in terms of the suggested division of molecular chaperones into two categories, termed steric and nonsteric.
    • (1998) Trends Biochem Sci , vol.23 , pp. 43-45
    • Ellis, R.J.1
  • 9
    • 0030756534 scopus 로고    scopus 로고
    • Protein memory through altered folding mediated by intramolecular chaperones
    • The first evidence that a mutation in a prosequence affects the conformation of the remainder of the chain in a manner that persists after its removal.
    • Shinde UP, Liu JJ, Inouye M Protein memory through altered folding mediated by intramolecular chaperones. Nature. 389:1997;520-522. The first evidence that a mutation in a prosequence affects the conformation of the remainder of the chain in a manner that persists after its removal.
    • (1997) Nature , vol.389 , pp. 520-522
    • Shinde, U.P.1    Liu, J.J.2    Inouye, M.3
  • 10
    • 0032169518 scopus 로고    scopus 로고
    • Proregion C-terminus: Protease active site interactions are critical in catalysing the folding of α-lytic protease
    • Peters RJ, Shiau AK, Sohl JL, Anderson DE, Tang G, Silen JL, Agard DA Proregion C-terminus: protease active site interactions are critical in catalysing the folding of α-lytic protease. Biochemistry. 37:1998;12058-12067.
    • (1998) Biochemistry , vol.37 , pp. 12058-12067
    • Peters, R.J.1    Shiau, A.K.2    Sohl, J.L.3    Anderson, D.E.4    Tang, G.5    Silen, J.L.6    Agard, D.A.7
  • 11
    • 0032558779 scopus 로고    scopus 로고
    • Unfolded conformations of α-lytic protease are more stable than its native state
    • Both the unfolded and partially folded forms of α-lytic protease are more stable than the native form, with the unusual result that the stability of the native form is not as a consequence of a lower free energy but of the size of the kinetic barrier to its unfolding. The prosequence lowers this barrier.
    • Sohl JL, Jaswal SS, Agard DA Unfolded conformations of α-lytic protease are more stable than its native state. Nature. 395:1998;817-819. Both the unfolded and partially folded forms of α-lytic protease are more stable than the native form, with the unusual result that the stability of the native form is not as a consequence of a lower free energy but of the size of the kinetic barrier to its unfolding. The prosequence lowers this barrier.
    • (1998) Nature , vol.395 , pp. 817-819
    • Sohl, J.L.1    Jaswal, S.S.2    Agard, D.A.3
  • 12
    • 0031925150 scopus 로고    scopus 로고
    • Hsp70 chaperone systems: Diversity of cellular functions and mechanism of action
    • A useful review of the variety of hsp70 chaperones and their regulatory co-chaperones in different types of cell.
    • Mayer MP, Bukau B Hsp70 chaperone systems: diversity of cellular functions and mechanism of action. Biol Chem. 379:1998;261-268. A useful review of the variety of hsp70 chaperones and their regulatory co-chaperones in different types of cell.
    • (1998) Biol Chem , vol.379 , pp. 261-268
    • Mayer, M.P.1    Bukau, B.2
  • 13
    • 0038217763 scopus 로고    scopus 로고
    • Regulation of the heat shock cognate hsc70 in the mammalian cell: The characterization of the anti-apoptic protein BAG-1 provides novel insights
    • A review of the evidence that a protein known for its ability to inhibit apoptosis also acts as a nucleotide exchange factor in the Hsc70 ATPase cycle.
    • Hohfeld J Regulation of the heat shock cognate hsc70 in the mammalian cell: the characterization of the anti-apoptic protein BAG-1 provides novel insights. Biol Chem. 379:1998;269-274. A review of the evidence that a protein known for its ability to inhibit apoptosis also acts as a nucleotide exchange factor in the Hsc70 ATPase cycle.
    • (1998) Biol Chem , vol.379 , pp. 269-274
    • Hohfeld, J.1
  • 14
    • 0032103439 scopus 로고    scopus 로고
    • The J-domain family and the recruitment of chaperone power
    • Kelley WL 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
  • 16
    • 0032005913 scopus 로고    scopus 로고
    • Structural aspects of GroEL function
    • Horovitz A Structural aspects of GroEL function. Curr Opin Struct Biol. 8:1998;93-100.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 93-100
    • Horovitz, A.1
  • 17
    • 0004167360 scopus 로고    scopus 로고
    • R.J. Ellis. San Diego: Academic Press
    • Ellis RJ The Chaperonins. 1996;Academic Press, San Diego.
    • (1996) The Chaperonins
  • 18
    • 0031239894 scopus 로고    scopus 로고
    • Avoiding the crowd
    • An argument is presented that the occurrence of the two types of molecular chaperone in the cytosol can be rationalised in terms of the enhancing effects of macromolecular crowding on the aggregation of nascent and partially folded proteins.
    • Ellis RJ Avoiding the crowd. Curr Biol. 7:1997;R531-R533. An argument is presented that the occurrence of the two types of molecular chaperone in the cytosol can be rationalised in terms of the enhancing effects of macromolecular crowding on the aggregation of nascent and partially folded proteins.
    • (1997) Curr Biol , vol.7
    • Ellis, R.J.1
  • 19
    • 0016206102 scopus 로고    scopus 로고
    • Renaturation of Escherichia coli tryptophanase after exposure to 8M urea
    • London J, Skrzynia C, Goldberg ME: Renaturation of Escherichia coli tryptophanase after exposure to 8M urea. Eur J Biochem 47:409-415.
    • Eur J Biochem , vol.47 , pp. 409-415
    • London, J.1    Skrzynia, C.2    Goldberg, M.E.3
  • 20
    • 0027318513 scopus 로고
    • Macromolecular crowding: Biochemical, biophysical and physiological consequences
    • Zimmermann SB, Minton AP Macromolecular crowding: biochemical, biophysical and physiological consequences. Annu Rev Biophys Biomol Struct. 22:1993;27-65.
    • (1993) Annu Rev Biophys Biomol Struct , vol.22 , pp. 27-65
    • Zimmermann, S.B.1    Minton, A.P.2
  • 21
    • 0030870719 scopus 로고    scopus 로고
    • 7 chaperonin complex
    • A major achievement in the chaperonin field. The detailed structure of this complex is consistent with the idea that it is essentially an Anfinsen cage, inside which individual partially folded chains are first bound by hydrophobic residues and then released in a hydrophilic environment to continue to fold in isolation from other folding chains.
    • 7 chaperonin complex. Nature. 388:1997;741-750. A major achievement in the chaperonin field. The detailed structure of this complex is consistent with the idea that it is essentially an Anfinsen cage, inside which individual partially folded chains are first bound by hydrophobic residues and then released in a hydrophilic environment to continue to fold in isolation from other folding chains.
    • (1997) Nature , vol.388 , pp. 741-750
    • Xu, Z.1    Horwich, A.L.2    Sigler, P.B.3
  • 22
    • 0032478521 scopus 로고    scopus 로고
    • Recognition of protein substrates by the prolyl isomerase trigger factor is independent of proline residues
    • Scholz C, Mucke M, Rape M, Pecht A, Pahl A, Bang H, Schmid FX Recognition of protein substrates by the prolyl isomerase trigger factor is independent of proline residues. J Mol Biol. 277:1998;723-732.
    • (1998) J Mol Biol , vol.277 , pp. 723-732
    • Scholz, C.1    Mucke, M.2    Rape, M.3    Pecht, A.4    Pahl, A.5    Bang, H.6    Schmid, F.X.7
  • 23
    • 0030928059 scopus 로고    scopus 로고
    • Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells
    • This paper reports the use of puromycin antibodies in precipitating nascent chain-hsp70 complexes truncated in vivo by the addition of puromycin to HeLa cells. Whether the properties of these puromycyl peptides accurately reflect those of true nascent chains remains to be established.
    • Eggers DK, Welch WJ, Hansen WJ Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells. Mol Biol Cell. 8:1997;1559-1573. This paper reports the use of puromycin antibodies in precipitating nascent chain-hsp70 complexes truncated in vivo by the addition of puromycin to HeLa cells. Whether the properties of these puromycyl peptides accurately reflect those of true nascent chains remains to be established.
    • (1997) Mol Biol Cell , vol.8 , pp. 1559-1573
    • Eggers, D.K.1    Welch, W.J.2    Hansen, W.J.3
  • 24
    • 0032528301 scopus 로고    scopus 로고
    • The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosome-nascent chain complex
    • The hsp70 homologues in yeast associate with both ribosomes and polysomes and can be cross-linked to nascent chains in an ATP-independent manner.
    • Pfund C, Lopez-Hoyo N, Ziegelhoffer T, Schilke BA, Lopez-Buesa P, Walter WA, Wiedmann M, Craig EA The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosome-nascent chain complex. EMBO J. 17:1998;3981-3989. The hsp70 homologues in yeast associate with both ribosomes and polysomes and can be cross-linked to nascent chains in an ATP-independent manner.
    • (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    Walter, W.A.6    Wiedmann, M.7    Craig, E.A.8
  • 25
    • 0032541489 scopus 로고    scopus 로고
    • Zuotin, a ribosome-associated DnaJ molecular chaperone
    • This report strongly supports the significance of the hsp70-hsp40 system as part of the translation and folding machinery, demonstrating that the DnaJ homologue zuotin, presumably a regulator of Ssb, interacts directly with the ribosome.
    • Yan W, Schilke B, Pfund C, Walter W, Kim S, Craig EA Zuotin, a ribosome-associated DnaJ molecular chaperone. EMBO J. 17:1998;4809-4817. This report strongly supports the significance of the hsp70-hsp40 system as part of the translation and folding machinery, demonstrating that the DnaJ homologue zuotin, presumably a regulator of Ssb, interacts directly with the ribosome.
    • (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
  • 26
    • 0030862486 scopus 로고    scopus 로고
    • In vitro evidence that hsp90 contains two independent chaperone sites
    • Young J, Schneider C, Hartl FU In vitro evidence that hsp90 contains two independent chaperone sites. FEBS Lett. 418:1997;139-143.
    • (1997) FEBS Lett , vol.418 , pp. 139-143
    • Young, J.1    Schneider, C.2    Hartl, F.U.3
  • 27
    • 0032539709 scopus 로고    scopus 로고
    • Two chaperone sites in hsp90 differing in substrate specificity and ATP-dependence
    • Schleibel T, Weikl T, Buchner J Two chaperone sites in hsp90 differing in substrate specificity and ATP-dependence. Proc Natl Acad Sci USA. 95:1998;1495-1499.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 1495-1499
    • Schleibel, T.1    Weikl, T.2    Buchner, J.3
  • 28
    • 0032541344 scopus 로고    scopus 로고
    • ATP binding and hydrolysis are essential to the function of the hsp90 molecular chaperone in vivo
    • Panaretou B, Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, Pearl LH ATP binding and hydrolysis are essential to the function of the hsp90 molecular chaperone in vivo. EMBO J. 17:1998;4829-4836.
    • (1998) EMBO J , vol.17 , pp. 4829-4836
    • Panaretou, B.1    Prodromou, C.2    Roe, S.M.3    O'Brien, R.4    Ladbury, J.E.5    Piper, P.W.6    Pearl, L.H.7
  • 29
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterisation of the ATP/ADP binding site in the hsp90 molecular chaperone
    • Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper RW, Pearl LH Identification and structural characterisation of the ATP/ADP binding site in the hsp90 molecular chaperone. Cell. 90:1997;65-75.
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1    Roe, S.M.2    O'Brien, R.3    Ladbury, J.E.4    Piper, R.W.5    Pearl, L.H.6
  • 30
    • 0032538995 scopus 로고    scopus 로고
    • In vivo function of hsp90 is dependent on ATP binding and hydrolysis
    • Obermann W, Sondermann H, Hartl FU In vivo function of hsp90 is dependent on ATP binding and hydrolysis. J Cell Biol. 143:1998;901-910.
    • (1998) J Cell Biol , vol.143 , pp. 901-910
    • Obermann, W.1    Sondermann, H.2    Hartl, F.U.3
  • 31
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an hsp90-geldanamycin complex - Targeting of a protein chaperone by an antitumour agent
    • Stebbins CE, Russo AA, Schneider C, Rosen N, Hartl FU, Pavletich NP Crystal structure of an hsp90-geldanamycin complex - targeting of a protein chaperone by an antitumour agent. Cell. 89:1997;239-250.
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.U.5    Pavletich, N.P.6
  • 33
    • 0033521588 scopus 로고    scopus 로고
    • In vivo newly translated polypeptides are sequestered in a protected folding environment
    • The expression of trap GroEL to 3-6% of the soluble protein in CHO cells fails to trap any newly synthesised chains or inhibit actin folding, supporting the chaperone pathway model. Controls establish that trap GroEL can bind unfolded proteins in vivo.
    • Thulasiraman V, Yang C-F, Frydman J In vivo newly translated polypeptides are sequestered in a protected folding environment. EMBO J. 18:1999;85-95. The expression of trap GroEL to 3-6% of the soluble protein in CHO cells fails to trap any newly synthesised chains or inhibit actin folding, supporting the chaperone pathway model. Controls establish that trap GroEL can bind unfolded proteins in vivo.
    • (1999) EMBO J , vol.18 , pp. 85-95
    • Thulasiraman, V.1    Yang, C.-F.2    Frydman, J.3
  • 34
    • 0032541496 scopus 로고    scopus 로고
    • Role of the DnaK and HscA homologs of hsp70 chaperones in protein folding in E. coli
    • 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.
    • (1998) EMBO J , vol.17 , pp. 4818-4828
    • Hesterkamp, T.1    Bukau, B.2
  • 36
    • 0032514615 scopus 로고    scopus 로고
    • GroEL-GroES-mediated protein folding requires an intact central cavity
    • •], describes a series of in vivo and in vitro experiments demonstrating that the apical polypeptide domain of GroEL is insufficient to mediate the folding of aggregation-prone chaperonin substrates such as rhodanese, malate dehydrogenase and citrate synthase. See also [39].
    • •], describes a series of in vivo and in vitro experiments demonstrating that the apical polypeptide domain of GroEL is insufficient to mediate the folding of aggregation-prone chaperonin substrates such as rhodanese, malate dehydrogenase and citrate synthase. See also [39].
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12163-12168
    • Wang, J.D.1    Michelitsch, D.2    Weissman, J.S.3
  • 38
    • 0030750584 scopus 로고    scopus 로고
    • In vivo observation of polypeptide flux through the bacterial chaperonin system
    • The first report into the rates of transit and the sizes of newly synthesised proteins that bind to GroEL in uninfected E. coli cells.
    • Ewalt KL, Hendrick JP, Houry WA, Hartl FU In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell. 90:1997;491-500. The first report into the rates of transit and the sizes of newly synthesised proteins that bind to GroEL in uninfected E. coli cells.
    • (1997) Cell , vol.90 , pp. 491-500
    • Ewalt, K.L.1    Hendrick, J.P.2    Houry, W.A.3    Hartl, F.U.4
  • 40
    • 0032113635 scopus 로고    scopus 로고
    • A single ring is sufficient for productive chaperonin-mediated folding in vivo
    • Nielsen KL, Cowan NJ A single ring is sufficient for productive chaperonin-mediated folding in vivo. Mol Cell. 2:1998;93-99.
    • (1998) Mol Cell , vol.2 , pp. 93-99
    • Nielsen, K.L.1    Cowan, N.J.2
  • 41
    • 0030668929 scopus 로고    scopus 로고
    • Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin
    • The structure of the apical domain of the archaeal thermosome has an α-helical protrusion that is not present in the otherwise homologous domain of GroEL. It is suggested that this protrusion takes over a GroES-like role in closing and opening the cage of the group II chaperonin.
    • Klumpp M, Baumeister W, Essen LO Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin. Cell. 91:1997;263-270. The structure of the apical domain of the archaeal thermosome has an α-helical protrusion that is not present in the otherwise homologous domain of GroEL. It is suggested that this protrusion takes over a GroES-like role in closing and opening the cage of the group II chaperonin.
    • (1997) Cell , vol.91 , pp. 263-270
    • Klumpp, M.1    Baumeister, W.2    Essen, L.O.3
  • 42
    • 0032478545 scopus 로고    scopus 로고
    • Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT
    • A landmark paper reporting the 2.6 Å resolution crystal structure determination of the thermosome (chaperonin) from the archaean T. acidophilum. The central cavity has 74% of the volume of the GroEL-GroES cavity and a polar internal surface, suggesting that this crystal form represents the closed conformation.
    • Ditzel L, Lowe J, Stock D, Stetter KO, Huber H, Huber R, Steinbacher S Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Cell. 93:1998;125-138. A landmark paper reporting the 2.6 Å resolution crystal structure determination of the thermosome (chaperonin) from the archaean T. acidophilum. The central cavity has 74% of the volume of the GroEL-GroES cavity and a polar internal surface, suggesting that this crystal form represents the closed conformation.
    • (1998) Cell , vol.93 , 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
  • 44
    • 0031945917 scopus 로고    scopus 로고
    • The thermosome: Chaperonin with a built-in lid
    • Horwich AL, Saibil HR The thermosome: chaperonin with a built-in lid. Nat Struct Biol. 5:1998;333-336.
    • (1998) Nat Struct Biol , vol.5 , pp. 333-336
    • Horwich, A.L.1    Saibil, H.R.2
  • 45
    • 0032481303 scopus 로고    scopus 로고
    • A novel protein complex promoting formation of functional α- And τ-tubulin
    • Geissler S, Siegers K, Schiebel E A novel protein complex promoting formation of functional α- and τ-tubulin. EMBO J. 17:1998;952-966.
    • (1998) EMBO J , vol.17 , pp. 952-966
    • Geissler, S.1    Siegers, K.2    Schiebel, E.3
  • 46
    • 0032577573 scopus 로고    scopus 로고
    • Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin
    • This paper reports the discovery of a hetero-oligomer of six different subunits (prefoldin) in yeast and animal cells that binds unfolded β-actin and transfers it to TriC, even in the presence of a sixfold excess of hsp60
    • Vainberg IE, Lewis SA, Rommelaere H, Ampe C, Vandekerckhove J, Klein HL, Cowan NJ Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin. Cell. 93:1998;863-873. This paper reports the discovery of a hetero-oligomer of six different subunits (prefoldin) in yeast and animal cells that binds unfolded β-actin and transfers it to TriC, even in the presence of a sixfold excess of hsp60.
    • (1998) Cell , vol.93 , pp. 863-873
    • Vainberg, I.E.1    Lewis, S.A.2    Rommelaere, H.3    Ampe, C.4    Vandekerckhove, J.5    Klein, H.L.6    Cowan, N.J.7
  • 47
    • 0033521523 scopus 로고    scopus 로고
    • Compartmentation of protein folding in vivo: Sequestration of non-native polypeptide by the chaperonin-GimC system
    • The kinetics of actin folding and its transit through the chaperonin TriC were measured in vivo in S. cerevisiae. The disruption of GimC, the novel cofactor of TriC, slows the kinetics of TriC-mediated actin folding by a factor of five and decreases the efficiency of folding by 50%. Evidence is provided that GimC intimately cooperates with TriC in folding. Newly synthesised actin is effectively shielded from the bulk cytosol by the TriC-GimC machinery.
    • Siegers K, Waldmann T, Leroux MR, Grein K, Shevchenko A, Schiebel E, Hartl FU Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J. 18:1999;75-84. The kinetics of actin folding and its transit through the chaperonin TriC were measured in vivo in S. cerevisiae. The disruption of GimC, the novel cofactor of TriC, slows the kinetics of TriC-mediated actin folding by a factor of five and decreases the efficiency of folding by 50%. Evidence is provided that GimC intimately cooperates with TriC in folding. Newly synthesised actin is effectively shielded from the bulk cytosol by the TriC-GimC machinery.
    • (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
  • 48
    • 0030050614 scopus 로고    scopus 로고
    • A quantitative assessment of the role of chaperonin proteins in protein folding in vivo
    • Lorimer GH A quantitative assessment of the role of 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
  • 49
    • 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
    • The chaperonin dependence of the folding of several mitochondrial proteins was tested using temperature sensitive yeast strains that are defective in hsp60 and hsp10. This study reveals a differential requirement by mitochondrial proteins for hsp60 and hsp10, suggesting that the two components do not always act as a single unit.
    • 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. The chaperonin dependence of the folding of several mitochondrial proteins was tested using temperature sensitive yeast strains that are defective in hsp60 and hsp10. This study reveals a differential requirement by mitochondrial proteins for hsp60 and hsp10, suggesting that the two components do not always act as a single unit.
    • (1998) EMBO J , vol.17 , pp. 5868-5876
    • Dubaquie, Y.1    Looser, R.2    Funfschilling, U.3    Jeno, P.4    Rospert, S.5
  • 50
    • 0030809270 scopus 로고    scopus 로고
    • Protein folding in vivo: Unraveling complex pathways
    • Johnson JL, Craig EA Protein folding in vivo: unraveling complex pathways. Cell. 90:1997;204-210.
    • (1997) Cell , vol.90 , pp. 204-210
    • Johnson, J.L.1    Craig, E.A.2
  • 51
    • 0030667932 scopus 로고    scopus 로고
    • In vivo chaperone functions of the Saccharomyces cerevisiae hsp90 chaperone
    • Despite the binding of hsp90 to signal transduction components, a temperature sensitive yeast hsp90 mutant does not suffer from protein aggregation, suggesting that hsp90 has no general role in protein folding in this organism.
    • Nathan DF, Vos MH, Lindquist S In vivo chaperone functions of the Saccharomyces cerevisiae hsp90 chaperone. Proc Natl Acad Sci USA. 94:1997;12949-12956. Despite the binding of hsp90 to signal transduction components, a temperature sensitive yeast hsp90 mutant does not suffer from protein aggregation, suggesting that hsp90 has no general role in protein folding in this organism.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12949-12956
    • Nathan, D.F.1    Vos, M.H.2    Lindquist, S.3
  • 52
    • 0030623528 scopus 로고    scopus 로고
    • Ribosomes and ribosomal RNAs as chaperones for folding of proteins
    • Kudlicki W, Coffman A, Kramer G, Hardesty B Ribosomes and ribosomal RNAs 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
  • 53
    • 0032496137 scopus 로고    scopus 로고
    • Chaperone properties of bacterial elongation factor EF-Tu
    • Caldas TD, 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
  • 54
    • 0026596223 scopus 로고
    • Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
    • Langer T, Lu C, Echuls H, Flanagan J, Hayer MK, Hartl FU Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature. 356:1994;683-689.
    • (1994) Nature , vol.356 , pp. 683-689
    • Langer, T.1    Lu, C.2    Echuls, H.3    Flanagan, J.4    Hayer, M.K.5    Hartl, F.U.6
  • 55
    • 0030598919 scopus 로고    scopus 로고
    • Substrate shuffling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding
    • Buchberger A, Schroder H, Hesterkamp T, Schonfeld HJ, Bukau B Substrate shuffling 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
  • 56
    • 0031946770 scopus 로고    scopus 로고
    • How chaperones fold proteins
    • Beissinger M, Buchner J How chaperones fold proteins. Biol Chem. 379:1998;245-259.
    • (1998) Biol Chem , vol.379 , pp. 245-259
    • Beissinger, M.1    Buchner, J.2
  • 57
    • 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 FU 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
  • 58
    • 0030730821 scopus 로고    scopus 로고
    • Chaperonin-mediated folding in the cytosol proceeds through rounds of release of native and non-native forms
    • ••]. The observed differences may be due to the use of nongrowing oocytes, which may have lower levels of GimC than growing yeast and mammalian cells.
    • ••]. The observed differences may be due to the use of nongrowing oocytes, which may have lower levels of GimC than growing yeast and mammalian cells.
    • (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
  • 59
  • 61
    • 0001747786 scopus 로고    scopus 로고
    • Genetic contributions to understanding polyketide synthases
    • Hopwood DA Genetic contributions to understanding polyketide synthases. Chem Rev. 97:1997;2465-2498.
    • (1997) Chem Rev , vol.97 , pp. 2465-2498
    • Hopwood, D.A.1
  • 62
    • 0030844281 scopus 로고    scopus 로고
    • Recombination of protein domains facilitated by co-translational folding in eukaryotes
    • Studies of the folding of artificial two-domain proteins in bacterial and eukaryote cells, and translation extracts led to the proposal that a shift in emphasis from post-translational to co-translational protein folding has occurred during the evolution of eukaryotes.
    • Netzer WJ, Hartl FU Recombination of protein domains facilitated by co-translational folding in eukaryotes. Nature. 388:1997;343-349. Studies of the folding of artificial two-domain proteins in bacterial and eukaryote cells, and translation extracts led to the proposal that a shift in emphasis from post-translational to co-translational protein folding has occurred during the evolution of eukaryotes.
    • (1997) Nature , vol.388 , pp. 343-349
    • Netzer, W.J.1    Hartl, F.U.2
  • 63
    • 0032005026 scopus 로고    scopus 로고
    • Protein folding in the cytosol: Chaperonin-dependent and chaperonin-independent mechanisms
    • Netzer WJ, Hartl FU Protein folding in the cytosol: chaperonin-dependent and chaperonin-independent mechanisms. Trends Biochem Sci. 23:1998;68-73.
    • (1998) Trends Biochem Sci , vol.23 , pp. 68-73
    • Netzer, W.J.1    Hartl, F.U.2
  • 64
    • 0001848681 scopus 로고
    • Folding of large proteins: Multidomain and multisubunit proteins
    • T.E. Creighton. New York: Freeman & Co
    • Garel JR Folding of large proteins: multidomain and multisubunit proteins. Creighton TE Protein Folding. 1992;405-454 Freeman & Co, New York.
    • (1992) Protein Folding , pp. 405-454
    • Garel, J.R.1
  • 65
    • 0031468437 scopus 로고    scopus 로고
    • Cotranslational protein folding
    • Fedorov AN, Baldwin TO Cotranslational protein folding. J Biol Chem. 272:1997;32715-32718.
    • (1997) J Biol Chem , vol.272 , pp. 32715-32718
    • Fedorov, A.N.1    Baldwin, T.O.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.