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| SUCCESSIVE ACTION OF DNAK, DNAJ AND GROEL ALONG THE PATHWAY OF CHAPERONE-MEDIATED PROTEIN FOLDING |
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| Author(s): LANGER T, LU C, ECHOLS H, FLANAGAN J, HAYER MK, HARTL FU |
| Source: NATURE Volume: 356 Issue: 6371 Pages: 683-689 Published: APR 23 1992 |
| Times Cited: 704 References: 68 |
| Abstract: The main stress proteins of Escherichia coli function in an ordered protein-folding reaction. DnaK (heat-shock protein 70) recognizes the folding polypeptide as an extended chain and cooperates with DnaJ in stabilizing an intermediate conformational state lacking ordered tertiary structure. Dependent on GrpE and ATP hydrolysis, the protein is then transferred to GroEL (heat-shock protein 60) which acts catalytically in the production of the native state. This sequential mechanism of chaperone action may represent an important pathway for the folding of newly synthesized polypeptides. |
| Document Type: Article |
| Language: English |
Addresses:
1. SLOAN KETTERING MEM CANC CTR, ROCKEFELLER RES LABS, PROGRAM CELLULAR BIOCHEM & BIOPHYS, NEW YORK, NY 10021 USA
2. UNIV CALIF BERKELEY, DEPT MOLEC & CELL BIOL, BERKELEY, CA 94720 USA
3. YALE UNIV, DEPT MOLEC BIOPHYS & BIOCHEM, NEW HAVEN, CT 06511 USA |
| Publisher: MACMILLAN MAGAZINES LTD, PORTERS SOUTH, 4 CRINAN ST, LONDON, ENGLAND N1 9XW |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: HQ146 |
| ISSN: 0028-0836 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |