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Volumn 8, Issue 1, 1998, Pages 93-100

Structural aspects of GroEL function

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONIN; PROTEIN;

EID: 0032005913     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(98)80015-8     Document Type: Article
Times cited : (54)

References (76)
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    • 7 chaperonin complex determined by X-ray crystallography at 3.0 Å resolution. Elevation and twist of the apical domains enable bound GroES to stabilize a folding chamber that is doubled in volume and has a hydrophilic lining. In contrast, the trans ring, which is in an acceptor state for nonfolded proteins, has a hydrophobic lining. An inward tilt of the equatorial domains in the cis ring, causes an outward tilt of the subunits in the trans ring, which explains the observed negative cooperatively between rings in GroEL.
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    • Structural basis of allosteric changes in the GroEL mutant Arg197→Ala
    • of outstanding interest. The 3D structures of the Arg197Ala GroEL mutant [37] in the absence and presence of different concentrations of ATP were determined at 30 Å resolution by electron cryo-microscopy and single particle reconstruction. The differences between the structures of the three allosteric states are clearly visualized. The structure of the TR state, which is strongly asymmetric, shows ring opening and anticlockwise rotation of the apical domains in the ATP-bound (R) ring and ring closing and clockwise rotation of the apical domains in the T ring. In the RR state, both rings open and only anticlockwise rotation is observed. Also seen is the elongation of the structure during this transitions TT→TR→RR. A fit of the atomic coordinates of the apical domain [35] to the EM density maps shows that the lining of the cavity in the TT state is continuous and hydrophobic, thus forming a binding site for nonfolded proteins, whereas in the rings in the R state
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    • of outstanding interest. This paper describes the 1.7 Å resolution structure of the apical domain of GroEL with a 17-residue N-terminal tag. The N-terminal tag of one molecule is bound to a neighbouring molecule in the crystal at a site that corresponds to a region previously identified by site-directed mutagenesis [21] to be involved in polypeptide binding. This appears to mimic the binding of a peptide substrate to GroEL, thereby providing the first high-resolution information on GroEL - polypeptide interactions. The conformation of the tag is extended and the binding involves both hydrophobic interactions and hydrogen bonds between sidechains of GroEL and the mainchain of the substrate.
    • of outstanding interest Buckle AM, Zahn R, Fersht AR. A structural model for GroEL - polypeptide recognition. Proc Natl Acad Sci USA. 94:1997;3571-3575 This paper describes the 1.7 Å resolution structure of the apical domain of GroEL with a 17-residue N-terminal tag. The N-terminal tag of one molecule is bound to a neighbouring molecule in the crystal at a site that corresponds to a region previously identified by site-directed mutagenesis [21] to be involved in polypeptide binding. This appears to mimic the binding of a peptide substrate to GroEL, thereby providing the first high-resolution information on GroEL - polypeptide interactions. The conformation of the tag is extended and the binding involves both hydrophobic interactions and hydrogen bonds between sidechains of GroEL and the mainchain of the substrate.
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    • of special interest Walter S, Lorimer GH, Schmid FX. A thermodynamic coupling mechanisms for GroEL-mediated unfolding. Proc Natl Acad Sci USA. 93:1996;9425-9430 This study shows that GroEL induces the unfolding of a variant of RNase T1 by shifting the equilibrium toward the unfolded state and not by catalysing unfolding.
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    • of special interest. Cross-linking of the apical domains to the equatorial domains by formation of a disulphide bridge between residues at position 83 in the equatorial domain and position 327 in the apical domain blocks the hinge motion and inhibits ATP hydrolysis, GroES binding and substrate release, thereby indicating that the hinge movements in GroEL are critical for its function.
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    • of special interest. This paper shows that mixed-ring complexes provide an extremely powerful tool for analysing the role of the double-ring structure in GroEL's function. By preparing a mixed-ring GroEL complex in which only one ring is able to bind polypeptide and GroES it was shown that both native and non-native forms are released from cis ternary complexes.
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    • Protein folding: How the mechanism of GroEL action is defined by kinetics
    • of special interest. An interesting discussion of issues concerning the kinetic mechanism of GroEL action. Based on their work using various DHFRs as substrates, the authors suggest that folding in the cavity occurs by the same mechanism and at the same rate as in solution.
    • of special interest Frieden C, Clark AC. Protein folding: how the mechanism of GroEL action is defined by kinetics. Proc Natl Acad Sci USA. 94:1997;5535-5538 An interesting discussion of issues concerning the kinetic mechanism of GroEL action. Based on their work using various DHFRs as substrates, the authors suggest that folding in the cavity occurs by the same mechanism and at the same rate as in solution.
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    • GroEL provides a folding pathway with lower apparent activation energy compared to spontaneous refolding of human carbonic anhydrase II
    • Persson M, Carlsson U, Bergenhem N. GroEL provides a folding pathway with lower apparent activation energy compared to spontaneous refolding of human carbonic anhydrase II. FEBS Lett. 411:1997;43-47.
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    • GroE modulates kinetic partitioning of folding intermediates between alternative states to maximize the yield of biologically active protein
    • Fedorov AN, Baldwin TO. GroE modulates kinetic partitioning of folding intermediates between alternative states to maximize the yield of biologically active protein. J Mol Biol. 268:1997;712-723.
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    • Structural adaptations in the specialized bacteriophage T4 co-chaperonin Gp31 expand the size of the Anfinsen cage
    • of special interest. This paper describes the 2.3 Å resolution structure of the co-chaperonin Gp31 which is required for the folding/assembly of the T4 major capsid protein and is able to functionally substitute for GroES in GroE-mediated folding. The paper highlights structural differences between GroES and Gp31 that may lead to expansion of the Anfinsen cage when Gp31 is in complex with GroEL.
    • of special interest Hunt JF, Van der Vies SM, Henry L, Deisenhofer J. Structural adaptations in the specialized bacteriophage T4 co-chaperonin Gp31 expand the size of the Anfinsen cage. Cell. 90:1997;361-371 This paper describes the 2.3 Å resolution structure of the co-chaperonin Gp31 which is required for the folding/assembly of the T4 major capsid protein and is able to functionally substitute for GroES in GroE-mediated folding. The paper highlights structural differences between GroES and Gp31 that may lead to expansion of the Anfinsen cage when Gp31 is in complex with GroEL.
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    • GroES promotes the T to R transition of the GroEL ring distal to GroES in the GroEL - GroES complex
    • of special interest. It is shown that GroES can facilitate the release of protein substrates from both trans and cis ternary complexes with GroEL - GroES by promoting the T to R transition of the GroEL ring distal to GroES in the complex.
    • of special interest Inbar E, Horovitz A. GroES promotes the T to R transition of the GroEL ring distal to GroES in the GroEL - GroES complex. Biochemistry. 36:1997;12276-12281 It is shown that GroES can facilitate the release of protein substrates from both trans and cis ternary complexes with GroEL - GroES by promoting the T to R transition of the GroEL ring distal to GroES in the complex.
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    • ATP hydrolysis is critical for induction of conformational changes in GroEL that expose hydrophobic surfaces
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    • Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL
    • 2+ ion associated with ATP [18]. The mutation Asp398Ala inhibits ATP hydrolysis but does not affect ATP binding. By analysing the functional properties of wild type and Asp398Ala mutant single and double rings, and also mixed double rings, it is shown that ATP hydrolysin in the cis ring, and ATP binding (but not hydrolysis) in the trans ring, are necessary for the ejections of GroES from the cis side, thus allowing proteins in the cavity to be released.
    • 2+ ion associated with ATP [18]. The mutation Asp398Ala inhibits ATP hydrolysis but does not affect ATP binding. By analysing the functional properties of wild type and Asp398Ala mutant single and double rings, and also mixed double rings, it is shown that ATP hydrolysin in the cis ring, and ATP binding (but not hydrolysis) in the trans ring, are necessary for the ejections of GroES from the cis side, thus allowing proteins in the cavity to be released.
    • (1997) Nature , vol.388 , pp. 792-798
    • Rye, H.S.1    Burston, S.G.2    Fenton, W.A.3    Beechem, J.M.4    Xu, Z.5    Sigler, P.B.6    Horwich, A.L.7
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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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    • A quantitative assessment of the role of chaperonin proteins in protein folding in vivo
    • of special interest. A theoretical analysis is presented indicating that the amount of GroEL and GroES is sufficient to facilitate the folding of no more than 5% of all the proteins in an E. coli cell.
    • of special interest Lorimer GH. A quantitative assessment of the role of chaperonin proteins in protein folding in vivo. FASEB J. 10:1996;5-9 A theoretical analysis is presented indicating that the amount of GroEL and GroES is sufficient to facilitate the folding of no more than 5% of all the proteins in an E. coli cell.
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    • Lorimer, G.H.1
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    • In vivo observation of polypeptide flux through the bacterial chaperonin system
    • of special interest. The contribution of the GroE system to folding in E. coli and in a cell-free translation system is analysed. It is estimated that only 10-15% of all cytoplasmic E. coli proteins interact with GroEL under normal growth conditions, whereas during heat shock a larger fraction of proteins (about 30%) interacts with GroEL.
    • of special interest 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 contribution of the GroE system to folding in E. coli and in a cell-free translation system is analysed. It is estimated that only 10-15% of all cytoplasmic E. coli proteins interact with GroEL under normal growth conditions, whereas during heat shock a larger fraction of proteins (about 30%) interacts with GroEL.
    • (1997) Cell , vol.90 , pp. 491-500
    • Ewalt, K.L.1    Hendrick, J.P.2    Houry, W.A.3    Hartl, F.U.4
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    • Recombination of protein domains facilitated by co-translational folding in eukaryotes
    • Netzer WJ, Hartl FU. Recombination of protein domains facilitated by co-translational folding in eukaryotes. Nature. 388:1997;343-349.
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    • Netzer, W.J.1    Hartl, F.U.2
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    • The effect of macromolecular crowding on chaperonin-mediated protein folding
    • Martin J, Hartl FU. The effect of macromolecular crowding on chaperonin-mediated protein folding. Proc Natl Acad Sci USA. 94:1997;1107-1112.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 1107-1112
    • Martin, J.1    Hartl, F.U.2
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    • Evidence for a lipochaperonin: Association of active protein-folding GroESL oligomers with lipids can stabilize membranes under heat shock conditions
    • Török Z, Horváth I, Goloubinoff P, Kovács E, Glatz A, Balogh G, Vigh L. Evidence for a lipochaperonin: association of active protein-folding GroESL oligomers with lipids can stabilize membranes under heat shock conditions. Proc Natl Acad Sci USA. 94:1997;2192-2197.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2192-2197
    • Török, Z.1    Horváth, I.2    Goloubinoff, P.3    Kovács, E.4    Glatz, A.5    Balogh, G.6    Vigh, L.7


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