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Volumn 7, Issue 1, 1997, Pages 41-52

Chaperone-assisted protein folding

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; CHAPERONIN; HEAT SHOCK PROTEIN 70; PROTEIN;

EID: 0343488499     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(97)80006-1     Document Type: Article
Times cited : (167)

References (99)
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    • Mutational analysis of the Hsp70-interacting protein Hip
    • 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.
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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
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    • 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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    • 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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    • Mande, S.C.1    Mehra, V.2    Bloom, B.R.3    Hol, W.G.J.4
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    • 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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    • Characterization of the active intermediate of a GroEL - GroES-mediated protein folding reaction
    • 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].)
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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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    • 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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    • Inter-ring communication is disrupted in the GroEL mutant Arg13→Gly; Ala126→Val with known crystal structure
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    • Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB
    • 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.
    • 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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    • Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling
    • 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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    • Determination of regions in the dihydrofolate reductase structure that interact with the molecular chaperonin GroEL
    • 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.
    • 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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    • Protein folding in the cell: Competing models of chaperonin function
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    • Chaperonin-facilitated protein folding: Optimization of rate and yield by an iterative annealing mechanism
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    • Molecular chaperones: Opening and closing the anfinsen cage
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    • Toward a mechanism for GroEL-GroES chaperone activity: An ATPase-gated and -pulsed folding and annealing cage
    • 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.
    • 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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    • Corrales, F.J.1    Fersht, A.R.2
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    • Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under GroES
    • 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.
    • 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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    • A thermodynamic coupling mechanism for GroEL-mediated unfolding
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    • Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis
    • 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).
    • 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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    • Release of both native and non-native proteins from a cis-only GroEL ternary complex
    • 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.
    • 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.
    • (1996) Nature , vol.383 , pp. 96-99
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    • 2 heterooligomers involved in protein release during the chaperonin cycle. J Biol Chem. 271:1996;16180-16186.
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    • Hsp60-independent protein folding in the matrix of yeast mitochondria
    • of special interest. This study addresses the general importance of the mitochondrial chaperonin Hsp60 for the folding of proteins that have been imported into mitochondria. It is shown that not all imported proteins require Hsp60 for folding. Rhodanese is one of the proteins that have to be transferred from the Hsp70 system to Hsp60 for folding.
    • Rospert S, Looser R, Dubaquie Y, Matouschek A, Glick BS, Schatz G. Hsp60-independent protein folding in the matrix of yeast mitochondria. of special interest EMBO J. 15:1996;764-774 This study addresses the general importance of the mitochondrial chaperonin Hsp60 for the folding of proteins that have been imported into mitochondria. It is shown that not all imported proteins require Hsp60 for folding. Rhodanese is one of the proteins that have to be transferred from the Hsp70 system to Hsp60 for folding.
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    • A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo
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    • Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding
    • Buchberger A, Schrüder H, Hesterkamp T, Schünfeld J-J, Bukau B. Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding. J Mol Biol. 261:1996;328-333.
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    • Principles of chaperone-assisted protein folding: Differences between in vitro and in vivo mechanisms
    • of outstanding interest. Chaperone interactions with newly synthesized polypeptides and with proteins diluted from denaturant into cell lysates are examined and compared. Whereas during de novo folding the chaperones Hsp70-Hsp40 and TRiC interact sequentially with a nascent polypeptide chain and restrict its exposure to bulk cytosolic protein, chemically denatured proteins such as actin and firefly luciferase partition themselves between the solution and different chaperone complexes. This study indicates that chaperones can act according to different organizational principles in de novo protein folding and in protein refolding.
    • Frydman J, Hartl FU. Principles of chaperone-assisted protein folding: differences between in vitro and in vivo mechanisms. of outstanding interest Science. 272:1996;1497-1502 Chaperone interactions with newly synthesized polypeptides and with proteins diluted from denaturant into cell lysates are examined and compared. Whereas during de novo folding the chaperones Hsp70-Hsp40 and TRiC interact sequentially with a nascent polypeptide chain and restrict its exposure to bulk cytosolic protein, chemically denatured proteins such as actin and firefly luciferase partition themselves between the solution and different chaperone complexes. This study indicates that chaperones can act according to different organizational principles in de novo protein folding and in protein refolding.
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    • Pathway leading to correctly folded-tubulin
    • of special interest. of outstanding interest. 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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    • 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.
    • Patino MM, Liu J-J, Glover JR, Lindquist S. Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. of outstanding interest Science. 273:1996;622-626 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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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.