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Structural analysis of substrate binding by the molecular chaperone Dnak
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of outstanding interest. A landmark paper that reports the crystal structure of the DnaK substrate-binding domain with a bound synthetic heptapeptide. The presence of a helical subdomain, which does not contact the peptide directly but may form a removable lid on the peptide-binding cleft, hints at an elegant mechanism for the regulation of binding and release of substrate, induced by conformational changes in the ATPase domain.
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Zhu X, Zhao X, Burkholder F, Gragerov A, Ogata CM, Gottesman ME, Hendrickson WA. Structural analysis of substrate binding by the molecular chaperone Dnak. of outstanding interest Science. 272:1996;1606-1614 A landmark paper that reports the crystal structure of the DnaK substrate-binding domain with a bound synthetic heptapeptide. The presence of a helical subdomain, which does not contact the peptide directly but may form a removable lid on the peptide-binding cleft, hints at an elegant mechanism for the regulation of binding and release of substrate, induced by conformational changes in the ATPase domain.
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Science
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Zhu, X.1
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The peptide-binding domain of the chaperone protein Hsc70 has an unusual secondary structure topology
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Morshauser RC, Wang H, Flynn GC, Zuiderweg ERP. The peptide-binding domain of the chaperone protein Hsc70 has an unusual secondary structure topology. Biochemistry. 34:1994;6261-6266.
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A hypothetical model for the peptide binding domain of Hsp70 based on the peptide binding domain of HLA
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Rippmann F, Taylor WR, Rothbard JB, Green NM. A hypothetical model for the peptide binding domain of Hsp70 based on the peptide binding domain of HLA. EMBO J. 10:1991;1053-1059.
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Gottesman, M.E.5
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Peptide-binding specificity of the molecular chaperone BiP
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Flynn GC, Rohl J, Flocco MT, Rothman JE. Peptide-binding specificity of the molecular chaperone BiP. Nature. 353:1991;726-730.
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Flynn, G.C.1
Rohl, J.2
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0027484417
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Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP
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Blond-Elguindi S, Cwirla SE, Dower WJ, Lipshutz RJ, Sprang SR, Sambrook JF, Gething MJ. Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP. Cell. 75:1993;717-729.
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Fourie AM, Sambrook JF, Gething MJ. Common and divergent peptide binding specificities of Hsp70 molecular chaperones. J Biol Chem. 269:1994;30470-30478.
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Fourie, A.M.1
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0029876864
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Conformational characterization of DnaK and its complexes by small-angle X-ray scattering
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of special interest. The data reported in this study suggest that the ATPase and peptide-binding domains of DnaK are connected by a short hinge region or are just in contact with each other. ATP binding causes conformational changes, including an increase in radius of gyration by 1-2 Å, and an increase by 5-10 Å in the longitudinal dimension of the dumbbell-shaped structure.
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Shi L, Kataoka M, Fink AL. Conformational characterization of DnaK and its complexes by small-angle X-ray scattering. of special interest Biochem. 35:1996;3297-3308 The data reported in this study suggest that the ATPase and peptide-binding domains of DnaK are connected by a short hinge region or are just in contact with each other. ATP binding causes conformational changes, including an increase in radius of gyration by 1-2 Å, and an increase by 5-10 Å in the longitudinal dimension of the dumbbell-shaped structure.
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Biochem
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Shi, L.1
Kataoka, M.2
Fink, A.L.3
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16
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0027987996
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NMR structure determination of the Escherichia coli DnaJ molecular chaperone: Secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J domain
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Szyperski T, Pellecchia M, Wall D, Georgopoulos C, Wüthrich K. NMR structure determination of the Escherichia coli DnaJ molecular chaperone: secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J domain. Proc Natl Acad Sci USA. 91:1994;11343-11347.
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Szyperski, T.1
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Wüthrich, K.5
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17
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0029651968
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15N magnetic resonance assignments, secondary structure, and tertiary fold of Escherichia coli DnaJ(1-78)
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15N magnetic resonance assignments, secondary structure, and tertiary fold of Escherichia coli DnaJ(1-78). Biochem. 34:1995;5587-5596.
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Biochem
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Hill, R.B.1
Flanagan, J.M.2
Prestegard, J.H.3
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Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain
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Quian YQ, Patel D, Hartl F-U, McColl DJ. Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain. J Mol Biol. 260:1996;224-235.
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Quian, Y.Q.1
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McColl, D.J.4
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19
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0030581175
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NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone
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Pellecchia M, Szyperski T, Wall D, Georgopoulos C, Wüthrich K. NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone. J Mol Biol. 260:1996;236-250.
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Pellecchia, M.1
Szyperski, T.2
Wall, D.3
Georgopoulos, C.4
Wüthrich, K.5
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20
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0028170215
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The NH2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for λ replication
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Wall D, Zylicz M, Georgopoulos C. The NH2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for λ replication. J Biol Chem. 269:1994;5446-5451.
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Wall, D.1
Zylicz, M.2
Georgopoulos, C.3
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0029871766
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A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct form substrate binding
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Tsai J, Douglas MG. A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct form substrate binding. J Biol Chem. 271:1996;9347-9354.
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Tsai, J.1
Douglas, M.G.2
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22
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Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK
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Liberek K, Marszalek J, Ang D, Georgopoulos C, Zylicz M. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc Natl Acad Sci USA. 88:1991;2874-2878.
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Liberek, K.1
Marszalek, J.2
Ang, D.3
Georgopoulos, C.4
Zylicz, M.5
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23
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0028930540
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The conserved G/F motif of the DnaJ chaperone is necessary for the activation of the substrate binding properties of the DnaK chaperone
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Wall D, Zylicz M, Georgopoulos C. The conserved G/F motif of the DnaJ chaperone is necessary for the activation of the substrate binding properties of the DnaK chaperone. J Biol Chem. 270:1995;2139-2144.
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J Biol Chem
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Wall, D.1
Zylicz, M.2
Georgopoulos, C.3
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24
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15844372190
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A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein
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Karzai AW, McMacken R. A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein. J Biol Chem. 271:1996;11236-11246.
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Karzai, A.W.1
McMacken, R.2
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25
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0029741321
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Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog Hsp40
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Minami Y, Höhfeld J, Ohtsuka K, Hart F-U. Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog Hsp40. J Biol Chem. 271:1996;19617-19624.
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Minami, Y.1
Höhfeld, J.2
Ohtsuka, K.3
Hart, F.-U.4
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26
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0030030946
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A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates
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of special interest. DnaJ is shown to contain a zinc-finger-like domain which probably fulfills a structural role and is required for the chaperone's ability to bind denatured proteins. Furthermore, evidence is presented that only full length DnaJ can cooperate with DnaK and GrpE in the refolding of denatured luciferase, although its interaction with DnaK is mediated (primarily) by the J-domain and the adjacent glycine/phenylalanine region.
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Szabo A, Korszun R, Hartl FU, Flanagan J. A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates. of special interest EMBO J. 15:1996;408-417 DnaJ is shown to contain a zinc-finger-like domain which probably fulfills a structural role and is required for the chaperone's ability to bind denatured proteins. Furthermore, evidence is presented that only full length DnaJ can cooperate with DnaK and GrpE in the refolding of denatured luciferase, although its interaction with DnaK is mediated (primarily) by the J-domain and the adjacent glycine/phenylalanine region.
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EMBO J
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Szabo, A.1
Korszun, R.2
Hartl, F.U.3
Flanagan, J.4
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27
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15844404388
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Structure - function analysis of the zinc finger region of the DnaJ molecular chaperone
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of special interest. An internal deletion of the cysteine-rich zinc-finger domain of DnaJ is shown to affect the interaction of DnaJ with some but not all of its substrate proteins.
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Banecki B, Liberek K, Wall D, Wawrzynúw A, Georgopoulos C, Bertoli E, Tanfani F, Zylicz M. Structure - function analysis of the zinc finger region of the DnaJ molecular chaperone. of special interest J Biol Chem. 271:1996;14840-14848 An internal deletion of the cysteine-rich zinc-finger domain of DnaJ is shown to affect the interaction of DnaJ with some but not all of its substrate proteins.
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J Biol Chem
, vol.271
, pp. 14840-14848
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Banecki, B.1
Liberek, K.2
Wall, D.3
Wawrzynúw, A.4
Georgopoulos, C.5
Bertoli, E.6
Tanfani, F.7
Zylicz, M.8
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0029051966
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Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1
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Freeman BC, Myers MP, Schumacher R, Morimoto RI. Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1. EMBO J. 14:1995;2281-2292.
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EMBO J
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Freeman, B.C.1
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0029013908
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The role of ATP in the functional cycle of the DnaK chaperone system
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McCarty JS, Buchberger A, Reinstein J, Bukau B. The role of ATP in the functional cycle of the DnaK chaperone system. J Mol Biol. 249:1995;126-137.
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McCarty, J.S.1
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Reinstein, J.3
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Analysis of three DnaK mutant proteins suggests that progression through the ATPase cycle requires conformational changes
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Kamath-Loeb AS, Lu CZ, Lonetto MA, Gross CA. Analysis of three DnaK mutant proteins suggests that progression through the ATPase cycle requires conformational changes. J Biol Chem. 270:1995;30051-30059.
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J Biol Chem
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Kamath-Loeb, A.S.1
Lu, C.Z.2
Lonetto, M.A.3
Gross, C.A.4
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31
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0028151509
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The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system: DnaK, DnaJ, and GrpE
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Szabo A, Langer T, Schröder H, Flanagan J, Bukau B, Hartl F-U. The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system: DnaK, DnaJ, and GrpE. Proc Natl Acad Sci USA. 91:1994;10345-10349.
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Proc Natl Acad Sci USA
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Szabo, A.1
Langer, T.2
Schröder, H.3
Flanagan, J.4
Bukau, B.5
Hartl, F.-U.6
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32
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0028921261
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The dissociation of ATP from Hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates
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Ziegelhoffer T, Lopez-Buesa P, Craig EA. The dissociation of ATP from Hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates. J Biol Chem. 270:1995;10412-10419.
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Ziegelhoffer, T.1
Lopez-Buesa, P.2
Craig, E.A.3
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33
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0028842615
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Hip, a novel chaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
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of special interest. of outstanding interest. Hip was identified in a yeast two hybrid screen for proteins that interact with the ATPase domain of rat Hsc70. Hip belongs to the family of tetratricopeptide repeat proteins. It has chaperone activity, and by binding to the Hsc70 ATPase domain, it stabilizes the ADP state of Hsc70. Functional characterization of Hsc70, in context with Hip and Hsp40 suggests that the ATPase cycle of eukaryotic Hsc70 is independent of a GrpE-like nucleotide-exchange factor. Hip is identical to p48, a component of Hsp90 heterocomplexes (see also [34,35,36].
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of special interest Höhfeld J, Minami Y, Hartl F-U. Hip, a novel chaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle. of outstanding interest Cell. 83:1995;589-598 Hip was identified in a yeast two hybrid screen for proteins that interact with the ATPase domain of rat Hsc70. Hip belongs to the family of tetratricopeptide repeat proteins. It has chaperone activity, and by binding to the Hsc70 ATPase domain, it stabilizes the ADP state of Hsc70. Functional characterization of Hsc70, in context with Hip and Hsp40 suggests that the ATPase cycle of eukaryotic Hsc70 is independent of a GrpE-like nucleotide-exchange factor. Hip is identical to p48, a component of Hsp90 heterocomplexes (see also [34,35,36].
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(1995)
Cell
, vol.83
, pp. 589-598
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Höhfeld, J.1
Minami, Y.2
Hartl, F.-U.3
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34
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0029833573
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Mutational analysis of the Hsp70-interacting protein Hip
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of special interest. Several mutant constructs of Hip are tested for their ability to bind to Hsp70. The tetratricopeptide domain of Hip is shown to be required for this interaction; the N-terminal region of Hip is necessary for homo-oligomerization.
-
Prapaparich V, Chen S, Toran EJ, Rimerman RA, Smith DF. Mutational analysis of the Hsp70-interacting protein Hip. of special interest Mol Cell Biol. 16:1996;6200-6207 Several mutant constructs of Hip are tested for their ability to bind to Hsp70. The tetratricopeptide domain of Hip is shown to be required for this interaction; the N-terminal region of Hip is necessary for homo-oligomerization.
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Mol Cell Biol
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Prapaparich, V.1
Chen, S.2
Toran, E.J.3
Rimerman, R.A.4
Smith, D.F.5
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35
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0031029286
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Characterization of functional domains of the eukaryotic co-chaperone Hip
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of special interest By employing the yeast two hybrid system and biochemical binding assays, the Hsc70-binding site of Hip was mapped to a domain that comprises multiple tetratricopeptide repeats and that flanks charged α helices. A domain required for homo-oligomerization at the extreme N terminus of Hip is identified
-
Irmer H, Höhfeld J. Characterization of functional domains of the eukaryotic co-chaperone Hip. of special interest J Biol Chem. 1997; By employing the yeast two hybrid system and biochemical binding assays, the Hsc70-binding site of Hip was mapped to a domain that comprises multiple tetratricopeptide repeats and that flanks charged α helices. A domain required for homo-oligomerization at the extreme N terminus of Hip is identified.
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(1997)
J Biol Chem
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Irmer, H.1
Höhfeld, J.2
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36
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0029964506
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Human p48, a transient component of progesterone receptor complexes and an Hsp70-binding protein
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of outstanding interest. of special interest. See annotation [33].
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of outstanding interest Prapapanich V, Chen S, Nair SC, Rimerman RA, Smith DF. Human p48, a transient component of progesterone receptor complexes and an Hsp70-binding protein. of special interest Mol Endocrinol. 10:1995;420-431 See annotation [33].
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Mol Endocrinol
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, pp. 420-431
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Prapapanich, V.1
Chen, S.2
Nair, S.C.3
Rimerman, R.A.4
Smith, D.F.5
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37
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0027943510
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The crystal structure of the bacterial chaperonin GroEL at 2.8 Å
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Braig K, Otwinowski Z, Hegde R, Boisvert DC, Joachimiak A, Horwich AL, Sigler PB. The crystal structure of the bacterial chaperonin GroEL at 2.8 Å Nature. 371:1994;578-586.
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(1994)
Nature
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Braig, K.1
Otwinowski, Z.2
Hegde, R.3
Boisvert, D.C.4
Joachimiak, A.5
Horwich, A.L.6
Sigler, P.B.7
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38
-
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0030067634
-
The crystal structure of the GroES co-chaperonin at 2.8 Å resolution
-
of outstanding interest. The X-ray crystallographic analysis of the smaller chaperonin cofactor from E. coli reveals a flexible, dome-shaped heptamer composed of β sheets. The 8 Å orifice in the roof is surrounded by negatively charged residues, and is thought to have a metastable structure. The flexible-loop regions which make contact with GroEL protrude from each GroES subunit at the base of the dome. Except for one loop region, these segments are not resolved in the crystal structure.
-
Hunt JF, Weaver AJ, Landry SJ, Gierasch L, Deisenhofer J. The crystal structure of the GroES co-chaperonin at 2.8 Å resolution. of outstanding interest Nature. 379:1996;37-45 The X-ray crystallographic analysis of the smaller chaperonin cofactor from E. coli reveals a flexible, dome-shaped heptamer composed of β sheets. The 8 Å orifice in the roof is surrounded by negatively charged residues, and is thought to have a metastable structure. The flexible-loop regions which make contact with GroEL protrude from each GroES subunit at the base of the dome. Except for one loop region, these segments are not resolved in the crystal structure.
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(1996)
Nature
, vol.379
, pp. 37-45
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-
Hunt, J.F.1
Weaver, A.J.2
Landry, S.J.3
Gierasch, L.4
Deisenhofer, J.5
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39
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0030024540
-
Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae
-
of outstanding interest. The structure of mycobacterial chaperonin 10 (GroES) is at lower resolution than that of E. coli GroES. The two structures are very similar. See annotation [38].
-
Mande SC, Mehra V, Bloom BR, Hol WGJ. Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae. of outstanding interest Science. 271:1996;203-207 The structure of mycobacterial chaperonin 10 (GroES) is at lower resolution than that of E. coli GroES. The two structures are very similar. See annotation [38].
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(1996)
Science
, vol.271
, pp. 203-207
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-
Mande, S.C.1
Mehra, V.2
Bloom, B.R.3
Hol, W.G.J.4
-
40
-
-
0030045870
-
Protein folding in the central cavity of the GroEL-GroES chaperonin complex
-
of outstanding interest. This study provides direct evidence that chaperonin-bound proteins, in this case DHFR, can reach their native state by folding in the central cavity of the GroEL cylinder. Folding requires bonding of GroES to the GroEL ring that contains the substrate polypeptide (cis topology), resulting in the release of polypeptide into the cavity, and precluding the premature exit of protein from the cavity. Folded polypeptide emerges into the bulk solution upon GroES dissociation from GroEL, which is triggered by ATP hydrolysis in the trans GroEL ring. Incompletely folded polypeptide rebinds GroEL at this stage. In addition, each reaction cycle is associated with the release of a fraction of bound polypeptide (~ 25% in the case of rhodanese)into the bulk solution in a non-native state. These molecules either rebind to another chaperonin for a new folding trial in the GroEL cavity or can be trapped by noncycling mutant GroEL, which explains the inhibition of folding
-
Mayhew M, Da Silva ARC, Martin J, Erdjument-Bromage H, Tempst P, Hartl FU. Protein folding in the central cavity of the GroEL-GroES chaperonin complex. of outstanding interest Nature. 379:1996;420-426 This study provides direct evidence that chaperonin-bound proteins, in this case DHFR, can reach their native state by folding in the central cavity of the GroEL cylinder. Folding requires bonding of GroES to the GroEL ring that contains the substrate polypeptide (cis topology), resulting in the release of polypeptide into the cavity, and precluding the premature exit of protein from the cavity. Folded polypeptide emerges into the bulk solution upon GroES dissociation from GroEL, which is triggered by ATP hydrolysis in the trans GroEL ring. Incompletely folded polypeptide rebinds GroEL at this stage. In addition, each reaction cycle is associated with the release of a fraction of bound polypeptide (~ 25% in the case of rhodanese)into the bulk solution in a non-native state. These molecules either rebind to another chaperonin for a new folding trial in the GroEL cavity or can be trapped by noncycling mutant GroEL, which explains the inhibition of folding by mutant GroEL reported previously [63].
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Nature
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Mayhew, M.1
Da Silva, A.R.C.2
Martin, J.3
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Tempst, P.5
Hartl, F.U.6
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41
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0030056969
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Characterization of the active intermediate of a GroEL - GroES-mediated protein folding reaction
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of outstanding interest. This paper presents convincing evidence for rhodanese and for green fluorescent protein that folding to the native state occurs in the GroEL cavity beneath the cap of GroES. Evidence from fluorescence anisotropy measurements (in the presence of ATP) indicates that folding initiates when the protein is enclosed in the GroEL cavity by GroES. (For comparison see annotation [68].)
-
Weissman JS, Rye HS, Fenton WA, Beechem JM, Horwich AL. Characterization of the active intermediate of a GroEL - GroES-mediated protein folding reaction. of outstanding interest Cell. 84:1996;481-490 This paper presents convincing evidence for rhodanese and for green fluorescent protein that folding to the native state occurs in the GroEL cavity beneath the cap of GroES. Evidence from fluorescence anisotropy measurements (in the presence of ATP) indicates that folding initiates when the protein is enclosed in the GroEL cavity by GroES. (For comparison see annotation [68].).
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(1996)
Cell
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, pp. 481-490
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Weissman, J.S.1
Rye, H.S.2
Fenton, W.A.3
Beechem, J.M.4
Horwich, A.L.5
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42
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Residues in chaperonin GroEL required for polypeptide binding and release
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Fenton WA, Kashi Y, Furtak K, Horwich AL. Residues in chaperonin GroEL required for polypeptide binding and release. Nature. 371:1994;614-619.
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Nature
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Fenton, W.A.1
Kashi, Y.2
Furtak, K.3
Horwich, A.L.4
-
43
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0030592538
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The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL
-
of outstanding interest. Cryo-electron microscopy is used to generate three-dimensional reconstructions of GroEL and GroEL - GroES complexes in different nucleotide-bound states. Rotations in the apical GroEL subunit domains, induced by nucleotide and GroES binding, result in the burial of the hydrophobic polypeptide-binding sites within the domain interface, and thereby regulate the affinity of GroEL for polypeptide substrate.
-
Roseman AM, Chen S, White H, Braig K, Saibil HR. The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. of outstanding interest Cell. 87:1996;241-251 Cryo-electron microscopy is used to generate three-dimensional reconstructions of GroEL and GroEL - GroES complexes in different nucleotide-bound states. Rotations in the apical GroEL subunit domains, induced by nucleotide and GroES binding, result in the burial of the hydrophobic polypeptide-binding sites within the domain interface, and thereby regulate the affinity of GroEL for polypeptide substrate.
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(1996)
Cell
, vol.87
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Roseman, A.M.1
Chen, S.2
White, H.3
Braig, K.4
Saibil, H.R.5
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44
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0028117314
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Molecular chaperones in protein folding: The art of avoiding sticky situations
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Hartl FU, Hlodan R, Langer T. Molecular chaperones in protein folding: the art of avoiding sticky situations. Trends Biochem Sci. 19:1994;20-25.
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Trends Biochem Sci
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Hartl, F.U.1
Hlodan, R.2
Langer, T.3
-
45
-
-
0029664944
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The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγS
-
of outstanding interest. The structure of GroEL with 14 molecules of ATPγS bound shows details of the ATP-binding site in the equatorial GroEL domains. Nucleotide binding does not cause the long-range conformational changes in GroEL noted in the structural analysis of the complex by electron microscopy (see annotation [43,51]).
-
Boisvert DC, Wang JM, Otwinowski Z, Horwich AL, Sigler PB. The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγS. of outstanding interest Nat Struct Biol. 3:1996;170-177 The structure of GroEL with 14 molecules of ATPγS bound shows details of the ATP-binding site in the equatorial GroEL domains. Nucleotide binding does not cause the long-range conformational changes in GroEL noted in the structural analysis of the complex by electron microscopy (see annotation [43,51]).
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Nat Struct Biol
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, pp. 170-177
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Boisvert, D.C.1
Wang, J.M.2
Otwinowski, Z.3
Horwich, A.L.4
Sigler, P.B.5
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46
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0028135063
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Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196/Ala
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Yifrach O, Horovitz A. Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196/Ala. J Mol Biol. 243:1994;397-401.
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Yifrach, O.1
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47
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The origins and consequences of asymmetry in the chaperonin reaction cycle
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Burston SG, Ranson NA, Clarke AR. The origins and consequences of asymmetry in the chaperonin reaction cycle. J Mol Biol. 249:1995;138-152.
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J Mol Biol
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Burston, S.G.1
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48
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Co-operativity in ATP hydrolysis by GroEL is increased by GroES
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Gray TE, Fersht AR. Co-operativity in ATP hydrolysis by GroEL is increased by GroES. FEBS Lett. 292:1991;254-258.
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Gray, T.E.1
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49
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0027250447
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Hydrolysis of adenosine 5' triphosphate by Escherichia coli GroEL: Effects of GroES and potassium ion
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Todd MJ, Viitanen PV, Lorimer GH. Hydrolysis of adenosine 5' triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion. Biochemistry. 32:1993;8560-8567.
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Todd, M.J.1
Viitanen, P.V.2
Lorimer, G.H.3
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50
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Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: Implications for the mechanism of assisted protein folding
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Jackson GS, Staniforth RA, Halsall DJ, Atkinson T, Holbrook JJ, Clarke AR, Burston SG. Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding. Biochemistry. 32:1993;2554-2563.
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Jackson, G.S.1
Staniforth, R.A.2
Halsall, D.J.3
Atkinson, T.4
Holbrook, J.J.5
Clarke, A.R.6
Burston, S.G.7
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51
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0029877893
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Inter-ring communication is disrupted in the GroEL mutant Arg13→Gly; Ala126→Val with known crystal structure
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Aharoni A, Horovitz A. Inter-ring communication is disrupted in the GroEL mutant Arg13→Gly; Ala126→Val with known crystal structure. J Mol Biol. 258:1996;732-735.
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Aharoni, A.1
Horovitz, A.2
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Characterization of a functionally important mobile domain of GroES
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Landry SJ, Zeilstra-Ryalls J, Fayet O, Georgopolos C, Gierasch LM. Characterization of a functionally important mobile domain of GroES. Nature. 364:1993;255-258.
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Nature
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, pp. 255-258
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Landry, S.J.1
Zeilstra-Ryalls, J.2
Fayet, O.3
Georgopolos, C.4
Gierasch, L.M.5
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54
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0028027055
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Location of a folding protein and shape changes in GroEL - GroES complexes imaged by cryo-electron microscopy
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Chen S, Roseman AM, Hunter A, Wood SP, Burston SG, Ranson N, Clarke AR, Saibil HR. Location of a folding protein and shape changes in GroEL - GroES complexes imaged by cryo-electron microscopy. Nature. 371:1994;261-264.
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Nature
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Chen, S.1
Roseman, A.M.2
Hunter, A.3
Wood, S.P.4
Burston, S.G.5
Ranson, N.6
Clarke, A.R.7
Saibil, H.R.8
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55
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0342568282
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Hydrogen exchange protection in GroEL-bound α-lactalbumin detected by mass spectrometry
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Robinson CV, Gro M, Eyles SJ, Ewbank JJ, Mayhew M, Hartl FU, Dobson CM, Radford SE. Hydrogen exchange protection in GroEL-bound α-lactalbumin detected by mass spectrometry. Nature. 372:1995;646-651.
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Nature
, vol.372
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Robinson, C.V.1
Gro, M.2
Eyles, S.J.3
Ewbank, J.J.4
Mayhew, M.5
Hartl, F.U.6
Dobson, C.M.7
Radford, S.E.8
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56
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0028260023
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Destabilization of the complete protein secondary structure on binding to the chaperone GroEL
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Zahn R, Spitzfaden C, Ottiger M, Wüthrich K, Plückthun A. Destabilization of the complete protein secondary structure on binding to the chaperone GroEL. Nature. 368:1994;261-265.
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Nature
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Zahn, R.1
Spitzfaden, C.2
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Wüthrich, K.4
Plückthun, A.5
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57
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0030061845
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Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB
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of outstanding interest. The model substrate barnase is analyzed in terms of exchangeability of its amide protons when bound to the chaperones GroEL or SecB. Two-dimensional NMR data indicate that even deeply buried protons can exchange with solvent, suggesting that complete unfolding occurred during the interaction with the chaperones.
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Zahn R, Perrett S, Stenberg G, Fersht AR. Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB. of outstanding interest Science. 271:1996;642-645 The model substrate barnase is analyzed in terms of exchangeability of its amide protons when bound to the chaperones GroEL or SecB. Two-dimensional NMR data indicate that even deeply buried protons can exchange with solvent, suggesting that complete unfolding occurred during the interaction with the chaperones.
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Science
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Zahn, R.1
Perrett, S.2
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Fersht, A.R.4
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58
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0030451744
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Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling
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of outstanding interest. The conformational properties of DHFR bound to the molecular chaperone GroEL at different stages of its ATP-driven folding reaction were determined by hydrogen-exchange labeling and electrospray ionization mass spectrometry. About 20 hydrogens are protected in DHFR bound to GroEL in the absence of ATP. This remains unchanged after several rounds of substrate cycling, suggesting that GroEL-assisted folding of DHFR occurs by iterative cycling of partially folded states, rather than by complete unfolding on the chaperonin surface.
-
Groβ M, Robinson CV, Mayhew M, Hartl FU, Radford SE. Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling. of outstanding interest Protein Sci. 5:1996;2506-2513 The conformational properties of DHFR bound to the molecular chaperone GroEL at different stages of its ATP-driven folding reaction were determined by hydrogen-exchange labeling and electrospray ionization mass spectrometry. About 20 hydrogens are protected in DHFR bound to GroEL in the absence of ATP. This remains unchanged after several rounds of substrate cycling, suggesting that GroEL-assisted folding of DHFR occurs by iterative cycling of partially folded states, rather than by complete unfolding on the chaperonin surface.
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Protein Sci
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Groß, M.1
Robinson, C.V.2
Mayhew, M.3
Hartl, F.U.4
Radford, S.E.5
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59
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0026416043
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Chaperonin-mediated protein folding at the surface of GroEL through a 'molten globule'-like intermediate
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Martin J, Langer T, Boteva R, Schramel A, Horwich AL, Hartl FU. Chaperonin-mediated protein folding at the surface of GroEL through a 'molten globule'-like intermediate. Nature. 352:1991;36-42.
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Nature
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Martin, J.1
Langer, T.2
Boteva, R.3
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Horwich, A.L.5
Hartl, F.U.6
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60
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0029882517
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Determination of regions in the dihydrofolate reductase structure that interact with the molecular chaperonin GroEL
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of special interest. A detailed characterization of the structural features that determine binding of unfolded DHFR to GroEL. Distinct loop regions in the mouse enzyme, which are absent in the otherwise homologous E. coli enzyme, appear to be responsible for the much higher GroEL affinity of the eukaryotic protein in its unfolded state. How the presence or absence of these loops affects the conformation of folding intermediates that are recognized by GroEL remains to be determined.
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Clark AC, Hugo E, Frieden C. Determination of regions in the dihydrofolate reductase structure that interact with the molecular chaperonin GroEL. of special interest Biochemistry. 35:1996;5893-5901 A detailed characterization of the structural features that determine binding of unfolded DHFR to GroEL. Distinct loop regions in the mouse enzyme, which are absent in the otherwise homologous E. coli enzyme, appear to be responsible for the much higher GroEL affinity of the eukaryotic protein in its unfolded state. How the presence or absence of these loops affects the conformation of folding intermediates that are recognized by GroEL remains to be determined.
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Biochemistry
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Clark, A.C.1
Hugo, E.2
Frieden, C.3
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Ellis RJ, Hartl FU. Protein folding in the cell: competing models of chaperonin function. FASEB J. 10:1996;20-26.
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Ellis, R.J.1
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Todd MJ, Viitanen PV, Lorimer GH. Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding. Science. 265:1994;659-666.
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Science
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Todd, M.J.1
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GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms
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Weissman JS, Kashi Y, Fenton WA, Horwich AL. GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms. Cell. 78:1994;693-702.
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Todd MJ, Lorimer G, Thirumalai D. Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism. Proc Natl Acad Sci USA. 93:1996;4030-4035.
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Todd, M.J.1
Lorimer, G.2
Thirumalai, D.3
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65
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The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding
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Martin J, Mayhew M, Langer T, Hartl FU. The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding. Nature. 366:1993;228-233.
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Nature
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Martin, J.1
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Hartl, F.U.4
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66
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Ellis RJ: Molecular chaperones: opening and closing the anfinsen cage. Curr Biol, 4:633-635.
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67
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Toward a mechanism for GroEL-GroES chaperone activity: An ATPase-gated and -pulsed folding and annealing cage
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of special interest. The rates of folding of the small model substrate barnase and several mutant forms are measured in the presence of GroEL, GroES and nucleotides. The data suggest that barnase leaves the chaperonin complex in its native conformation.
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Corrales FJ, Fersht AR. Toward a mechanism for GroEL-GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage. of special interest Proc Natl Acad Sci USA. 93:1996;4509-4512 The rates of folding of the small model substrate barnase and several mutant forms are measured in the presence of GroEL, GroES and nucleotides. The data suggest that barnase leaves the chaperonin complex in its native conformation.
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Proc Natl Acad Sci USA
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Corrales, F.J.1
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68
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0028785583
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Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under GroES
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of outstanding interest. This paper shows that productive GroEL-mediated protein folding occurs only from the cis complex in which substrate is capped by GroES, and not from the trans complex in which GroES and substrate protein are bound to opposite GroEL rings. While this would be consistent with folding occurring in the GroEL cavity, the authors conclude from fluorescence anisotropy measurements (in the presence of ADP) that folding does not occur when protein is enclosed in th GroEL cavity by GroES, but rather after its release into bulk solution.
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Weissman JS, Hohl CM, Kovalenko O, Kashi Y, Chen S, Braig K, Saibil HR, Fenton WA, Horwich AL. Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES. of outstanding interest Cell. 83:1995;577-587 This paper shows that productive GroEL-mediated protein folding occurs only from the cis complex in which substrate is capped by GroES, and not from the trans complex in which GroES and substrate protein are bound to opposite GroEL rings. While this would be consistent with folding occurring in the GroEL cavity, the authors conclude from fluorescence anisotropy measurements (in the presence of ADP) that folding does not occur when protein is enclosed in th GroEL cavity by GroES, but rather after its release into bulk solution.
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Cell
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Weissman, J.S.1
Hohl, C.M.2
Kovalenko, O.3
Kashi, Y.4
Chen, S.5
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Fenton, W.A.8
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69
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A thermodynamic coupling mechanism for GroEL-mediated unfolding
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Walter S, Lorimer GH, Schmid FX. A thermodynamic coupling mechanism for GroEL-mediated unfolding. Proc Natl Acad Sci USA. 93:1996;9425-9430.
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70
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Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis
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of special interest. GroEL-bound rhodanese is shown to induce the cycling of GroES on and off GroEL in the presence of ADP, promoting its efficient folding. At physiological salt concentrations, a single-ring variant of GroEL is also fully functional in supporting this reaction. It is concluded that neither the energy of ATP hydrolysis nor the allosteric coupling of the two GroEL rings is directly required for GroEL - GroES-mediated protein folding (see [51]). The minimal mechanism of the reaction is the binding and release to a polypeptide-containing ring of GroEL, thereby opening and closing the GroEL folding cage. The role of ATP hydrolysis is mainly to induce conformational changes in GroEL that result in GroES cycling at a physiologically relevant rate. Rhodanese folding in the presence of ADP and GroES was first demonstrated by M Fisher and coworkers (M Fisher, personal communication).
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Hayer-Hartl MKH, Weber F, Hartl FU. Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis. of special interest EMBO J. 15:1996;6111-6121 GroEL-bound rhodanese is shown to induce the cycling of GroES on and off GroEL in the presence of ADP, promoting its efficient folding. At physiological salt concentrations, a single-ring variant of GroEL is also fully functional in supporting this reaction. It is concluded that neither the energy of ATP hydrolysis nor the allosteric coupling of the two GroEL rings is directly required for GroEL - GroES-mediated protein folding (see [51]). The minimal mechanism of the reaction is the binding and release to a polypeptide-containing ring of GroEL, thereby opening and closing the GroEL folding cage. The role of ATP hydrolysis is mainly to induce conformational changes in GroEL that result in GroES cycling at a physiologically relevant rate. Rhodanese folding in the presence of ADP and GroES was first demonstrated by M Fisher and coworkers (M Fisher, personal communication).
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EMBO J
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Release of both native and non-native proteins from a cis-only GroEL ternary complex
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2 complexes is precluded. In addition, experiments with cytosolic extracts and microinjection of chaperonin complexes into Xenopus oocytes attempt to evaluate the extent of non-native protein release from GroEL under more physiological conditions.
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2 complexes is precluded. In addition, experiments with cytosolic extracts and microinjection of chaperonin complexes into Xenopus oocytes attempt to evaluate the extent of non-native protein release from GroEL under more physiological conditions.
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Nature
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Schmidt, M.1
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Functional significance of symmetrical versus asymmetrical GroEL - GroES chaperonin complexes
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Engel A, Hayer-Hartl MK, Goldie KN, Pfeifer G, Hegerl R, Müller S, Da Silva ACR, Baumeister W, Hartl FU. Functional significance of symmetrical versus asymmetrical GroEL - GroES chaperonin complexes. Science. 269:1995;832-841.
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Engel, A.1
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78
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Whole-genome random sequencing and assembly of Haemophilus influenzae Rd
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Fleischmann RD, Adams MD, White O, Clayton RA, Kirkness EF, Kerlavage AR, Bult CJ, Tomb J-F, Dougherty BA, Merrick JM, et al. Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. Science. 269:1995;496-512.
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of special interest Tian G, Huang Y, Rommelaere H, Vandekerckhove J, Ampe C, Cowan NJ. Pathway leading to correctly folded-tubulin. of outstanding interest Cell. 86:1996;267-296 Two papers [94,95] describe a number of cofactors that are necessary for the folding of β-tubulin and their sequential interaction with tubulin is established. Although the exact function of the factors is unknown, they appear to act at a postchaperonin step, after tubulin has been released from the cytosolic chaperonin TRiC. Factor A, previously thought to interact directly with TRiC, is now shown to exert its effect indirectly by binding to tubulin-folding intermediate.
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The human cytosolic molecular chaperones Hsp90, Hsp70 (Hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding
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of special interest. The ability of Hsp90 to maintain denatured β-galactosidase in a soluble, refolding competent state is demonstrated in vitro. In contrast to the Hsp70 - Hsp40 system, Hsp90 is not capable of mediating the actual refolding reaction. The molecular mechanism underlying this difference in performance between the two chaperone systems is still unknown.
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of outstanding interest. A cytosplasmically inherited genetic element in yeast, [PSI+], is shown to be a prion-like aggregate of the cellular protein Sup35. Interestingly, aggregation of Sup35 depends on the functional state of the chaperone protein Hsp104 in the same manner as does [PSI+] inheritance. This is the first study that makes a direct connection between a prion phenomenon and the function of a molecular chaperone.
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