groel-groesreview98

groel-groesreview98 - Annu Rev Biochem 1998 67:581–608...

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Unformatted text preview: Annu. Rev. Biochem. 1998. 67:581–608 Copyright c 1998 by Annual Reviews. All rights reserved STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING Paul B. Sigler, 1,2 Zhaohui Xu, 1,2 Hays S. Rye, 2,3 Steven G. Burston, 3 Wayne A. Fenton, 3 and Arthur L. Horwich 2,3 1 Department of Molecular Biophysics and Biochemistry, 2 Howard Hughes Medical Institute, and 3 Department of Genetics, School of Medicine, Yale University, New Haven, Connecticut 06510; e-mail: [email protected] KEY WORDS: ATP, chaperonin, GroES, Hsp60 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 accom- pany 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. CONTENTS PURPOSE . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 582 THE ROLE OF MOLECULAR CHAPERONES IN THE CELL . . . . . . . . . . . . . . . . . . . . . . . 582 Biological Catalysts . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 582 The Entropic Barrier to Expressing Genes Accurately . . . . . . . . . . . . . . . . . . . . . . . . . . . . 583 Categories of Molecular Chaperones . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 584 CHAPERONINS . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 585 Chaperonin Architecture . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 585 581 0066-4154/98/0701-0581$08.00 A n n u . R e v . B i o c h e m . 1 9 9 8 . 6 7 : 5 8 1- 6 8 . D o w n l o a d e d f r o m a r j o u r n a l s . a n n u a l r e v i e w s . o r g b y U n i v e r s i t y o f B r i t i s h C o l u m b i a L i b r a r y o n 1 1 / 3 / 9 . F o r p e r s o n a l u s e o n l y . 582 SIGLER ET AL GroEL and GroES Structures . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 586 The Chaperonin Reaction Cycle . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 587 Phase I: Polypeptide Binding . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .....
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This note was uploaded on 12/05/2010 for the course CHBE 251 taught by Professor Scotty during the Winter '09 term at UBC.

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groel-groesreview98 - Annu Rev Biochem 1998 67:581–608...

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