PMID:9267029
| Citation |
Ewalt, KL, Hendrick, JP, Houry, WA and Hartl, FU (1997) In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell 90:491-500 |
|---|---|
| Abstract |
The quantitative contribution of chaperonin GroEL to protein folding in E. coli was analyzed. A diverse set of newly synthesized polypeptides, predominantly between 10-55 kDa, interacts with GroEL, accounting for 10%-15% of all cytoplasmic protein under normal growth conditions, and for 30% or more upon exposure to heat stress. Most proteins leave GroEL rapidly within 10-30 s. We distinguish three classes of substrate proteins: (I) proteins with a chaperonin-independent folding pathway; (II) proteins, more than 50% of total, with an intermediate chaperonin dependence for which normally only a small fraction transits GroEL; and (III) a set of highly chaperonin-dependent proteins, many of which dissociate slowly from GroEL and probably require sequestration of aggregation-sensitive intermediates within the GroEL cavity for successful folding. |
| Links | |
| Keywords |
Bacterial Proteins/biosynthesis; Bacterial Proteins/chemistry; Chaperonin 60/metabolism; Chaperonins/metabolism; Chloramphenicol O-Acetyltransferase/biosynthesis; Chloramphenicol O-Acetyltransferase/chemistry; Escherichia coli/metabolism; Kinetics; Models, Structural; Plasmids; Protein Biosynthesis; Protein Folding; Recombinant Proteins/biosynthesis; Recombinant Proteins/chemistry; Thiosulfate Sulfurtransferase/biosynthesis; Thiosulfate Sulfurtransferase/chemistry; beta-Lactamases/biosynthesis; beta-Lactamases/chemistry |
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