In vivo observation of polypeptide flux through the bacterial chaperonin system Journal Article
| Authors: | Ewalt, K. L.; Hendrick, J. P.; Houry, W. A.; Hartl, F. U. |
| Article Title: | In vivo observation of polypeptide flux through the bacterial chaperonin system |
| 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. |
| Keywords: | nonhuman; animal cell; protein protein interaction; protein binding; in vivo study; bacteria (microorganisms); animalia; bacterial proteins; amino acid sequence; kinetics; protein synthesis; escherichia coli; recombinant proteins; rna translation; protein biosynthesis; plasmids; protein folding; cell free system; peptide synthesis; beta-lactamases; chaperonins; priority journal; article; heat stress; chloramphenicol o-acetyltransferase; chaperonin; groel protein; models, structural; thiosulfate sulfurtransferase |
| Journal Title: | Cell |
| Volume: | 90 |
| Issue: | 3 |
| ISSN: | 0092-8674 |
| Publisher: | Cell Press |
| Date Published: | 1997-08-08 |
| Start Page: | 491 |
| End Page: | 500 |
| Language: | English |
| DOI: | 10.1016/s0092-8674(00)80509-7 |
| PUBMED: | 9267029 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Article -- Export Date: 17 March 2017 -- Source: Scopus |
