Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones Journal Article
| Authors: | Frydman, J.; Nimmesgern, E.; Ohtsuka, K.; Hartl, F. U. |
| Article Title: | Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones |
| Abstract: | The folding of polypeptides emerging from ribosomes was analysed in a mammalian translation system using firefly luciferase as a model protein. The growing polypeptide interacts with a specific set of molecular chaperones, including Hsp70, the DnaJ homologue Hsp40 and the chaperonin TRiC. The ordered assembly of these components on the nascent chain forms a high molecular mass complex that allows the cotranslational formation of protein domains and the completion of folding once the chain is released from the ribosome. © 1994 Nature Publishing Group. |
| Keywords: | animal; mammalia; carboxy terminal sequence; protein assembly; luciferase; protein binding; nuclear proteins; amino terminal sequence; adenosine triphosphate; protein folding; molecular weight; hydrolysis; cytosol; in vitro; ribosomes; rabbits; ribosome; heat-shock proteins; heat shock protein; translation regulation; reticulocytes; priority journal; article; support, u.s. gov't, p.h.s.; translation, genetic; peptide chain elongation |
| Journal Title: | Nature |
| Volume: | 370 |
| Issue: | 6485 |
| ISSN: | 0028-0836 |
| Publisher: | Nature Publishing Group |
| Date Published: | 1994-07-14 |
| Start Page: | 111 |
| End Page: | 117 |
| Language: | English |
| DOI: | 10.1038/370111a0 |
| PROVIDER: | scopus |
| PUBMED: | 8022479 |
| DOI/URL: | |
| Notes: | Export Date: 14 January 2019 -- Article -- Source: Scopus |
