Principles of chaperone-assisted protein folding: Differences between in vitro and in vivo mechanisms Journal Article
| Authors: | Frydman, J.; Hartl, F. U. |
| Article Title: | Principles of chaperone-assisted protein folding: Differences between in vitro and in vivo mechanisms |
| Abstract: | Molecular chaperones in the eukaryotic cytosol were shown to interact differently with chemically denatured proteins and their newly translated counterparts. During refolding from denaturant, actin partitioned freely between 70-kilodalton heat shock protein, the bulk cytosol, and the chaperonin TCP1-ring complex. In contrast, during cell-free translation, the chaperones were recruited to the elongating polypeptide and protected it from exposure to the bulk cytosol during folding. Posttranslational cycling between chaperone-bound and free states was observed with subunits of oligomeric proteins and with aberrant polypeptides; this cycling allowed the subunits to assemble and the aberrant polypeptides to be degraded. Thus, folding, oligomerization, and degradation are linked hierarchically to ensure the correct fate of newly synthesized polypeptides. |
| Keywords: | protein conformation; peptides; protein biosynthesis; adenosine triphosphate; protein subunit; protein folding; eukaryotic cell; actins; luciferases; cytosol; cell extracts; hsp70 heat-shock proteins; ribosomes; chaperone; molecular chaperones; heat shock protein; protein denaturation; oligomer; chaperonins; reticulocytes; priority journal; article; groel protein |
| Journal Title: | Science |
| Volume: | 272 |
| Issue: | 5267 |
| ISSN: | 0036-8075 |
| Publisher: | American Association for the Advancement of Science |
| Date Published: | 1996-06-07 |
| Start Page: | 1497 |
| End Page: | 1502 |
| Language: | English |
| PUBMED: | 8633246 |
| PROVIDER: | scopus |
| DOI: | 10.1126/science.272.5267.1497 |
| DOI/URL: | |
| Notes: | Article -- Export Date: 22 November 2017 -- Source: Scopus |
