Cooperativity in the thermosome

Journal of Molecular Biology

Volumn 348, Issue 1, 2005, Pages 13-26

  Bigotti, Maria Giulia ^a   Clarke, Anthony R ^a  

^a UNIVERSITY OF BRISTOL   (United Kingdom)

Author keywords

Allostery; Chaperones; Chaperonins; Cooperativity; Thermosome

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; CELL EXTRACT; CHAPERONIN; CHAPERONIN I; CHAPERONIN II; INDOLE; NUCLEOTIDE; THERMOSOME; TRYPTOPHAN; UNCLASSIFIED DRUG;

ALPHA CHAIN; ARTICLE; BETA CHAIN; CELL COMMUNICATION; CELL ENCAPSULATION; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CYTOPLASM; ESCHERICHIA COLI; EUKARYOTIC CELL; EXAMINATION; FLOW MEASUREMENT; FLUORESCENCE; GENE EXPRESSION; GENE REARRANGEMENT; GENETIC CODE; NONHUMAN; OBSERVATION; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN INDUCTION; PROTEIN ISOLATION; PROTEIN PURIFICATION; QUANTUM YIELD; REPORTER GENE; STEADY STATE; TEMPERATURE; THERMOPLASMA ACIDOPHILUM;

EID: 16244380542     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.01.066     Document Type: Article

References (65)

1. P.B. Sigler, Z.H. Xu, H.S. Rye, S.G. Burston, W.A. Fenton, and A.L. Horwich Structure and function in GroEL-mediated protein folding Annu. Rev. Biochem. 67 1998 581 608
2. J. Frydman Folding of newly translated proteins in vivo: the role of molecular chaperones Annu. Rev. Biochem. 70 2001 603 647
3. L. Figueiredo, D. Klunker, D. Ang, D.J. Naylor, M.J. Kerner, and C. Georgopoulos Functional characterization of an archaeal GroEL/GroES chaperonin system: significance of substrate encapsulation J. Biol. Chem. 279 2004 1090 1099
4. I. Gutsche, L.-O. Essen, and W. Baumeister Group IIchaperonins: new TriC(k)s and turns of a protein folding machine J. Mol. Biol. 293 1999 295 312
5. J.M. Valpuesta, J. Martin-Benito, P. Gomez-Puertas, J. Carrascosa, and K.R. Willinson Structure and function of a protein folding machine: the eukaryotic cytosolic chaperonin CCT FEBS Letters 529 2002 11 16
6. K. Braig, Z. Otwinowsky, R. Hedge, D.C. Boisvert, A. Joachimiak, A.L. Horwich, and P.B. Sigler The crystal structure of the bacterial chaperonin GroEL at 2.8 Å Nature 371 1994 578 586
7. L. Ditzel, J. Lowe, D. Stock, K.O. Stetter, H. Huber, R. Huber, and S. Steinbacher Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT Cell 93 1998 125 138
8. A.K. Liou, and K.R. Willinson Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT microcomplexes EMBO J. 16 1997 4311 4361
9. J.D. Trent, E. Nimmesgern, J.S. Wall, F.U. Hartl, and A.L. Horwich A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1 Nature 354 1991 490 493
10. J.L. Carrascosa, O. Lorca, and J.M. Valpuesta Structural comparison of prokaryotic and eukaryotic chaperonins Micron 32 2001 43 50
11. H. Grallert, and J. Buchner Review: a structural view of the GroE chaperone cycle J. Struct. Biol. 135 2001 95 103
12. J.S. Weissman The ins and outs of GroEL-mediated protein folding Mol. Cell 8 2001 730 732
13. S. Walter Structure and function of the GroE chaperone Cell. Mol. Life Sci. 59 2002 1589 1597
14. J.F. Hunt, A.J. Weaver, S.J. Landry, L. Gierasch, and J. Deisenhofer The crystal structure of the GroES co-chaperonin at 2.8 Å resolution Nature 379 1996 37 45
15. S.C. Mande, V. Mehra, B.R. Bloom, and W.G.J. Hol Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae Science 271 1996 203 207
16. A.M. Roseman, S. Chen, H. White, K. Braig, and H.R. Saibil The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL Cell 87 1996 241 251
17. 7 chaperonin complex Nature 388 1997 741 750
18. S.J. Landry, J. Zeilstra-Ryalls, O. Fayet, C. Georgopoulos, and L.M. Gierash Characterization of an important mobile domain of GroES Nature 364 1993 255 258
19. A.M. Buckle, R. Zahn, and A.R. Fersht A structural model for GroEL-polypeptide recognition Proc. Natl Acad. Sci. USA 94 1997 3571 3575
20. L. Chen, and P.B. Sigler The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate recognition Cell 99 1999 757 768
21. G.W. Farr, K. Furtak, M.B. Rowland, N.A. Ranson, H.R. Saibil, T. Kirchhausen, and A.L. Horwich Multivalent binding of nonnative substrate proteins by the chaperonin GroEL Cell 100 2000 561 573
22. J.S. Weissman, H.S. Rye, W.A. Fenton, J.M. Beechem, and A.L. Horwich Characterization of the active intermediate of a GroEL-GroES-mediated protein-folding reaction Cell 84 1996 481 490
23. S.G. Burston, J.S. Weissman, G.W. Farr, W.A. Fenton, and A.L. Horwich Release of both native and nonnative proteins from a cis-only GroEL ternary complex Nature 383 1996 96 99
24. H.S. Rye, S.G. Burston, W.A. Fenton, J.M. Beechem, Z.H. Xu, P.B. Sigler, and A.L. Horwich Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL Nature 388 1997 792 798
25. J.D. Wang, and J.S. Weissman Thinking outside the box: new insights into the mechanism of GroEL-mediated protein folding Nature Struct. Biol. 6 1999 597 600
26. 14 at 2.0 Å resolution J. Mol. Biol. 327 2003 843 855
27. G.S. Jackson, R.A. Staniforth, D.J. Halsall, T. Atkinson, J.J. Holbrook, A.R. Clarke, and S.G. Burston Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding Biochemistry 32 1993 2554 2563
28. R.A. Staniforth, S.G. Burston, T. Atkinson, and A.R. Clarke Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10 Biochem. J. 300 1994 651 658
29. M.J. Todd, P.V. Viitanen, and G.H. Lorimer Dynamics of the chaperonin ATPase cycle: implications for facilitated protein-folding Science 265 1994 659 666
30. J.M. Cliff, N.M. Kad, N. Haty, P.A. Lund, M.R. Webb, S.G. Burston, and A.R. Clarke A kinetic analysis of the nucleotide-induced allosteric transition of GroEL J. Mol. Biol. 293 1999 667 684
31. O. Yifrach, and A. Horovitz Coupling between protein folding and allostery in the GroE chaperonin system Proc. Natl Acad. Sci. USA 97 2000 1521 1524
32. H.R. Saibil, D. Zheng, A.R. Roseman, A.S. Hunter, G.M.F. Watson, and S. Chen ATP induces large quaternary rearrangements in a cage-like chaperonin structure Curr. Biol. 3 1993 265 273
33. R.J. Ellis Opening and closing the Anfinsen cage Curr. Biol. 4 1994 633 635
34. A. Crouy-Chanel, A. El Yaagoubi, M. Kohiyama, and G. Richarme Reversal by GroES of the GroEL preference from hydrophobic amino acids toward hydrophilic amino acids J. Biol. Chem. 270 1995 10571 10575
35. M.R. Leroux, and F.U. Hartl Protein folding: versatility of the cytosolic chaperonin TRIC/CCT Curr. Biol. 10 2000 R260 R264
36. S. Andra, G. Frey, M. Nitsch, W. Baumeister, and K.O. Stetter Purification and structural characterization of the thermosome from the hyperthermophilic archaeum Methanopyrus kandleri FEBS Letters 379 1996 127 131
37. B.M. Phipps, A. Hoffmann, K.O. Stetter, and W. Baumeister A novel ATPase complex selectively accumulated upon heat shock is a major cellular component of thermophilic archaebacteria EMBO J. 10 1991 1711 172246
38. Y.P. Kuo, D.K. Thompson, A. St Jean, R.L. Charlebois, and C.J. Daniels Characterization of two heat shock genes from Haloferax volcanii: a model system for transcription regulation in the Archaea J. Bacteriol. 179 1997 6318 6324
39. M. Klumpp, W. Baumeister, and L.O. Essen Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin Cell 91 1997 263 270
40. G. Pappenberger, J.A. Wilsher, S.M. Roe, D.J. Counsell, K.R. Willison, and L.H. Pearl Crystal structure of the CCT gamma apical domain: implications for substrate binding to the eukaryotic cytosolic chaperonin J. Mol. Biol. 318 2002 1367 1379
41. A.L. Horwich, and H.R. Saibil The thermosome: chaperonin with a built-in lid Nature Struct. Biol. 5 1998 333 336
42. G. Schoehn, M. Hayes, M. Cliff, A.R. Clarke, and H.R. Saibil Domain rotation between open, closed and bullet-shaped forms of the thermosome, an archaeal chaperonin J. Mol. Biol. 301 2000 323 332
43. O. Llorca, J. Martin-Benito, J. Grantham, M. Ritco-Vonsovici, K.R. Willinson, J.L. Carrascosa, and J.M. Valpuesta The 'sequential allosteric ring' mechanism in the eukaryotic chaperonin-assisted folding of actin and tubulin EMBO J. 20 2001 4065 4075
44. S. Marco, J.L. Carrascosa, and J.M. Valpuesta Reversibile interaction of b-actin along the channel of the TCP-1 cytoplasmic chaperonin Biophys. J. 67 1994 634 638
45. G.W. Farr, E.C. Scharl, R.J. Schumacher, S. Sondek, and A.L. Horwich Chaperonin mediated folding in the eukaryotic cytosol proceeds through rounds of release of native and nonnative forms Cell 89 1997 927 937
46. S. Steinbacher, and L. Ditzel Review: nucleotide binding to the Thermoplasma thermosome: implications for the functional cycle of group II chaperonins J. Struct. Biol. 135 2001 147 156
47. M. Nitsch, J. Walz, D. Typke, M. Klumpp, L.O. Essen, and W. Baumeister Group II chaperonin in an open conformation examined by electron tomography Nature Struct. Biol. 5 1998 855 857
48. I. Gutsche, O. Mihalache, R. Hegerl, D. Typke, and W. Baumeister ATPase cycle controls the conformation of an archaeal chaperonin as visualized by cryo-electron microscopy FEBS Letters 477 2000 278 282
49. I. Gutsche, J. Holzinger, N. Rauh, W. Baumeister, and R.P. May ATP-induced structural change of the thermosome is temperature-dependent J. Struct. Biol. 135 2001 139 146
50. O. Llorca, M.G. Smyth, J.L. Carrascosa, K.R. Willison, M. Radermacher, S. Steinbacher, and J.M. Valpuesta 3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin Nature Struct. Biol. 6 1999 639 642
51. A.S. Meyer, J.R. Gillespie, D. Walther, I.S. Millet, S. Doniach, and J. Frydman Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis Cell 113 2003 369 381
52. O. Yifrach, and A. Horovitz Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL Biochemistry 34 1995 5303 5308
53. S.G. Burston, N.A. Ranson, and A.R. Clarke The origins and consequences of asymmetry in the chaperonin reaction cycle J. Mol. Biol. 249 1995 138 152
54. O. Yifrach, and A. Horovitz Transient kinetic analysis of adenosine 5′-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL Biochemistry 37 1998 7083 7088
55. G. Kafri, K.R. Willison, and A. Horovitz Nested allosteric interactions in the cytoplasmic chaperonin containing TCP-1 Protein Sci. 10 2001 445 449
56. G. Kafri, and A. Horovitz Transient kinetic analysis of ATP-induced allosteric transitions in the eukaryotic chaperonin containing TCP-1 J. Mol. Biol. 326 2003 981 987
57. T. Waldmann, M. Nitsch, M. Klumpp, and W. Baumeister Expression of an archaeal chaperonin in E. coli: formation of homo- (α,β) and hetero-oligomeric (α+β) thermosome complexes FEBS Letters 376 1995 67 73
58. I. Gutsche, O. Mihalache, and W. Baumeister ATPase cycle of an archaeal chaperonin J. Mol. Biol. 300 2000 187 196
59. I. Gutsche, J. Holzinger, M. Rossle, H. Heumann, W. Baumeister, and R.P. May Conformational rearrangements of an archaeal chaperonin upon ATPase cycling Curr. Biol. 10 2000 405 408
60. S.K. Kim, S.R. Kim, Y.H. Kim, P. Kwack, D. Son, and G.-W. Cheong Structural analysis of the thermosome from hyperthermophilic archaeon Thermococcus Mol. Cells 14 2002 85 92
61. A.R. Kusmierczyk, and J. Martin Nested cooperativity and salt dependence of the ATPase activity of the archaeal chaperonin Mm-cpn FEBS Letters 547 2003 201 204
62. K.N. Kreuzer, and C.V. Jongeneel Escherichia coli phage T4 topoisomerase Methods Enzymol. 100 1983 144 160
63. H. Grallert, K. Rutkat, and J. Buchner Limits of protein folding inside GroE complexes J. Biol. Chem. 27 2000 20424 20430
64. D. Walker, W.N. Chia, and H. Muirhead Key residues in the allosteric transition of Bacillus stearothermophilus pyruvate kinase identified by site-directed mutagenesis J. Mol. Biol. 228 1992 265 276
65. D.A. Barstow, A.R. Clarke, W.N. Chia, D. Wigley, A.F. Sharman, and J.J. Holbrook Cloning, expression and complete nucleotide sequence of the Bacillus stearothermophilus l-lactate dehydrogenase gene Gene 46 1986 47 55