The Chaperonin ATPase Cycle: Mechanism of Allosteric Switching and Movements of Substrate-Binding Domains in GroEL

Aharoni, 1996, Inter-ring communication is disrupted in the GroEL mutant Arg13→Gly; Ala126→Val with known crystal structure, J. Mol. Biol., 258, 732, 10.1006/jmbi.1996.0282

Azem, 1995, The protein folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer, Proc. Natl. Acad. Sci. USA, 92, 12021, 10.1073/pnas.92.26.12021

Baker, 1996, A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy, J. Struct. Biol., 116, 120, 10.1006/jsbi.1996.0020

Bochkareva, 1994, ATP induces non-identity of two rings in chaperonin GroEL, J. Biol. Chem., 269, 23869, 10.1016/S0021-9258(19)51017-1

Bochkareva, 1992, Positive cooperativity in the functioning of molecular chaperone GroEL, J. Biol. Chem., 267, 6796, 10.1016/S0021-9258(19)50496-3

Boisvert, 1996, The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγS, Nature Struct. Biol., 3, 170, 10.1038/nsb0296-170

Braig, 1994, The crystal structure of the bacterial chaperonin GroEL at 2.8 Å, Nature, 371, 578, 10.1038/371578a0

Braig, 1995, Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution, Nature Struct. Biol., 2, 1083, 10.1038/nsb1295-1083

Burston, 1995, The origins and consequences of asymmetry in the chaperonin reaction cycle, J. Mol. Biol., 249, 138, 10.1006/jmbi.1995.0285

Chandrasekhar, 1986, Purification and properties of the groES morphogenetic protein of Escherichia coli, J. Biol. Chem., 261, 12414, 10.1016/S0021-9258(18)67256-4

Chen, 1994, Location of a folding protein and shape changes in GroEL–GroES complexes imaged by cryo-electron microscopy, Nature, 371, 261, 10.1038/371261a0

Fenton, 1994, Residues in chaperonin GroEL required for polypeptide binding and release, Nature, 371, 614, 10.1038/371614a0

Frank, 1996, SPIDER and WEB, J. Struct. Biol., 116, 190, 10.1006/jsbi.1996.0030

Goloubinoff, 1989, Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP, Nature, 342, 884, 10.1038/342884a0

Gorovits, 1995, The chaperonin GroEL is destabilized by binding of ADP, J. Biol. Chem., 270, 28551, 10.1074/jbc.270.48.28551

Gray, 1991, Cooperativity in ATP hydrolysis by GroEL is increased by GroES, FEBS Lett., 292, 254, 10.1016/0014-5793(91)80878-7

Hartl, 1996, Molecular chaperones in cellular protein folding, Nature, 381, 571, 10.1038/381571a0

Hunt, 1996, The crystal structure of the GroES co-chaperonin at 2.8 Å resolution, Nature, 379, 37, 10.1038/379037a0

Jackson, 1993, Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle, Biochemistry, 32, 2554, 10.1021/bi00061a013

Kovalenko, 1994, Residue lysine-34 in GroES modulates allosteric transitions in GroEL, Biochemistry, 33, 14974, 10.1021/bi00254a004

Landry, 1993, Characterization of a functionally important mobile domain of GroES, Nature, 364, 255, 10.1038/364255a0

Langer, 1992, Chaperonin-mediated protein folding, EMBO J., 11, 4757, 10.1002/j.1460-2075.1992.tb05581.x

Llorca, 1994, The formation of symmetrical GroEL–GroES complexes in the presence of ATP, FEBS Lett., 345, 181, 10.1016/0014-5793(94)00432-3

Martin, 1991, Chaperonin-mediated protein folding at the surface of groEL through a “molten globule”-like intermediate, Nature, 352, 36, 10.1038/352036a0

Martin, 1993, The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding, Nature, 366, 228, 10.1038/366228a0

Mayhew, 1996, Protein folding in the central cavity of the GroEL–GroES chaperonin complex, Nature, 379, 420, 10.1038/379420a0

Milligan, 1987, Structural relationships of actin, myosin and tropomyosin revealed by cryo-electron microscopy, J. Cell Biol., 105, 29, 10.1083/jcb.105.1.29

Nicholls, 1993, GRASP, Biophys. J., 64, A166

Penczek, 1994, The ribosome at improved resolution, Ultramicroscopy, 53, 251, 10.1016/0304-3991(94)90038-8

Radermacher, 1994, Three-dimensional reconstruction from random projections, Ultramicroscopy, 53, 121, 10.1016/0304-3991(94)90003-5

Saibil, 1993, ATP induces large quaternary rearrangements in a cage-like chaperonin structure, Curr. Biol., 3, 265, 10.1016/0960-9822(93)90176-O

Schatz, 1995, Structure of Lumbricus terrestris hemoglobin at 30 Å resolution determined using angular reconstitution, J. Struct. Biol., 114, 28, 10.1006/jsbi.1995.1003

Staniforth, 1994, Affinity of chaperonin 60 for a protein substrate and its modulation by nucleotides and chaperonin 10, Biochem. J., 300, 651, 10.1042/bj3000651

Todd, 1993, Hydrolysis of adenosine 5′ triphosphate by Escherichia coli GroEL, Biochemistry, 32, 8560, 10.1021/bi00084a024

Todd, 1994, Dynamics of the chaperonin ATPase cycle, Science, 265, 659, 10.1126/science.7913555

Weissman, 1994, GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms, Cell, 78, 693, 10.1016/0092-8674(94)90533-9

Weissman, 1995, Mechanism of GroEL action, Cell, 83, 577, 10.1016/0092-8674(95)90098-5

Weissman, 1996, Characterization of the active intermediate of a GroEL–GroES-mediated protein folding reaction, Cell, 84, 481, 10.1016/S0092-8674(00)81293-3

Yifrach, 1994, Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196→Ala, J. Mol. Biol., 243, 397, 10.1006/jmbi.1994.1667

Yifrach, 1995, Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL, Biochemistry, 34, 5303, 10.1021/bi00016a001

Yifrach, 1996, Allosteric control by ATP of non-folded protein binding to GroEL, J. Mol. Biol., 255, 356, 10.1006/jmbi.1996.0028