Crossref journal-article
Annual Reviews
Annual Review of Biochemistry (22)
Abstract

Recent structural and biochemical investigations have come together to allow a better understanding of the mechanism of chaperonin (GroEL, Hsp60)–mediated protein folding, the final step in the accurate expression of genetic information. Major, asymmetric conformational changes in the GroEL double toroid accompany binding of ATP and the cochaperonin GroES. When a nonnative polypeptide, bound to one of the GroEL rings, is encapsulated by GroES to form a cis ternary complex, these changes drive the polypeptide into the sequestered cavity and initiate its folding. ATP hydrolysis in the cis ring primes release of the products, and ATP binding in the trans ring then disrupts the cis complex. This process allows the polypeptide to achieve its final native state, if folding was completed, or to recycle to another chaperonin molecule, if the folding process did not result in a form committed to the native state.

Bibliography

Sigler, P. B., Xu, Z., Rye, H. S., Burston, S. G., Fenton, W. A., & Horwich, A. L. (1998). STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING. Annual Review of Biochemistry, 67(1), 581–608.

Authors 6
  1. Paul B. Sigler (first)
  2. Zhaohui Xu (additional)
  3. Hays S. Rye (additional)
  4. Steven G. Burston (additional)
  5. Wayne A. Fenton (additional)
  6. Arthur L. Horwich (additional)
References 84 Referenced 485
  1. 10.1038/nsb0197-10
  2. 10.1126/science.2756425
  3. 10.1126/science.272.5268.1606
  4. 10.1093/emboj/16.7.1501
  5. 10.1038/nsb0597-342
  6. 10.1093/emboj/16.2.221
  7. 10.1093/emboj/16.3.659
  8. 10.1074/jbc.272.12.8007
  9. 10.1126/science.7761850
  10. 10.1002/pro.5560060401
  11. {'key': 'b11', 'volume-title': 'The Chaperonins.', 'author': 'Ellis RJ', 'year': '1996'} / The Chaperonins. by Ellis RJ (1996)
  12. 10.1038/381571a0
  13. 10.1016/0022-2836(79)90502-3
  14. 10.1016/0022-2836(79)90501-1
  15. 10.1073/pnas.78.3.1629
  16. 10.1016/S0021-9258(18)67256-4 / J. Biol. Chem. by Chandrasekhar GN (1986)
  17. 10.1038/353025b0
  18. 10.1002/j.1460-2075.1992.tb05581.x
  19. 10.1016/0014-5793(92)80240-H
  20. 10.1126/science.7913553
  21. 10.1126/science.7913554
  22. 10.1126/science.7638600
  23. 10.1073/pnas.92.26.12021
  24. 10.1073/pnas.90.9.3978
  25. 10.1038/371261a0
  26. 10.1016/S0969-2126(96)00011-1
  27. 10.1002/j.1460-2075.1991.tb07695.x
  28. 10.1038/354490a0
  29. 10.1093/emboj/16.14.4311
  30. 10.1098/rstb.1993.0030
  31. 10.1016/S0960-9822(94)00024-2
  32. 10.1083/jcb.132.1.1
  33. 10.1038/371578a0
  34. 10.1038/379037a0
  35. 10.1126/science.271.5246.203
  36. 10.1038/364255a0
  37. 10.1038/342884a0
  38. 10.1016/0960-9822(93)90176-O
  39. 10.1016/S0092-8674(00)81293-3
  40. 10.1038/42047
  41. 10.1038/371614a0
  42. 10.1074/jbc.270.3.1011
  43. 10.1021/bi00044a037
  44. 10.1006/jmbi.1996.0666
  45. 10.1006/jmbi.1997.1081
  46. 10.1021/bi00244a001
  47. 10.1073/pnas.94.8.3571
  48. 10.1126/science.271.5249.642
  49. 10.1038/41892
  50. 10.1006/jmbi.1994.1567
  51. 10.1073/pnas.93.18.9425
  52. 10.1021/bi00104a021
  53. 10.1038/368261a0
  54. 10.1038/372646a0
  55. 10.1073/pnas.94.4.1080
  56. 10.1002/pro.5560051213
  57. 10.1006/jmbi.1995.0399
  58. 10.1002/j.1460-2075.1990.tb07403.x
  59. 10.1021/bi00476a003
  60. 10.1038/352036a0
  61. 10.1021/bi00220a020
  62. 10.1021/bi00102a010
  63. 10.1016/0014-5793(91)80878-7
  64. 10.1016/S0021-9258(19)50496-3 / J. Biol. Chem. by Bochkareva ES (1992)
  65. 10.1021/bi00061a013
  66. 10.1021/bi00084a024
  67. 10.1006/jmbi.1995.0285
  68. 10.1016/S0092-8674(00)81342-2
  69. 10.1021/bi00016a001
  70. 10.1038/nsb0296-170
  71. 10.1016/0968-0004(94)90058-2
  72. 10.1038/nsb1295-1083
  73. 10.1006/jmbi.1996.0282
  74. 10.1038/41944
  75. 10.1074/jbc.271.45.28229
  76. 10.1126/science.7913555
  77. 10.1016/S0092-8674(00)80408-0
  78. 10.1096/fasebj.10.1.8566535
  79. 10.1016/S0092-8674(00)80343-8
  80. 10.1038/383096a0
  81. 10.1016/0092-8674(94)90533-9
  82. 10.1074/jbc.270.37.21517
  83. 10.1016/0014-5793(95)00041-7
  84. 10.1038/379420a0
Dates
Type When
Created 23 years ago (July 27, 2002, 7:42 a.m.)
Deposited 3 years, 10 months ago (Oct. 5, 2021, 9:50 a.m.)
Indexed 1 month, 2 weeks ago (July 11, 2025, 6:51 a.m.)
Issued 27 years, 2 months ago (June 1, 1998)
Published 27 years, 2 months ago (June 1, 1998)
Published Print 27 years, 2 months ago (June 1, 1998)
Funders 0

None

@article{Sigler_1998, title={STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING}, volume={67}, ISSN={1545-4509}, url={http://dx.doi.org/10.1146/annurev.biochem.67.1.581}, DOI={10.1146/annurev.biochem.67.1.581}, number={1}, journal={Annual Review of Biochemistry}, publisher={Annual Reviews}, author={Sigler, Paul B. and Xu, Zhaohui and Rye, Hays S. and Burston, Steven G. and Fenton, Wayne A. and Horwich, Arthur L.}, year={1998}, month=jun, pages={581–608} }