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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.
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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.
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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.
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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.
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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.
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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.
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Eggers, D.K.1
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The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosome-nascent chain complex
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The hsp70 homologues in yeast associate with both ribosomes and polysomes and can be cross-linked to nascent chains in an ATP-independent manner.
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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.
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Craig, E.A.8
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25
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Zuotin, a ribosome-associated DnaJ molecular chaperone
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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.
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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.
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ATP binding and hydrolysis are essential to the function of the hsp90 molecular chaperone in vivo
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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.
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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.
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In vivo newly translated polypeptides are sequestered in a protected folding environment
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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.
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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.
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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.
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Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL
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Rye, H.S.1
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0030750584
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In vivo observation of polypeptide flux through the bacterial chaperonin system
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The first report into the rates of transit and the sizes of newly synthesised proteins that bind to GroEL in uninfected E. coli cells.
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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.
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Cell
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Ewalt, K.L.1
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A single ring is sufficient for productive chaperonin-mediated folding in vivo
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Mol Cell
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41
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0030668929
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Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin
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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.
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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.
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0032478545
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Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT
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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.
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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.
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Cell
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Ditzel, L.1
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Stetter, K.O.4
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43
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0031719642
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44
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The thermosome: Chaperonin with a built-in lid
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Horwich AL, Saibil HR The thermosome: chaperonin with a built-in lid. Nat Struct Biol. 5:1998;333-336.
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46
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Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin
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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
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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.
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Vainberg, I.E.1
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