Recombination of protein domains facilitated by co-translational folding in eukaryotes Journal Article
| Authors: | Netzer, W. J.; Hartl, F. U. |
| Article Title: | Recombination of protein domains facilitated by co-translational folding in eukaryotes |
| Abstract: | The evolution of complex genomes requires that new combinations of pre- existing protein domains successfully fold into modular polypeptides. During eukaryotic translation model two-domain polypeptides fold efficiently by sequential and co-translational folding of their domains. In contrast, folding of the same proteins in Escherichia coli is post-translational, and leads to intramolecular misfolding of concurrently folding domains. Sequential domain folding in eukaryotes may have been critical in the evolution of modular polypeptides, by increasing the probability that random gene-fusion events resulted in immediately foldable protein structures. |
| Keywords: | protein domain; animals; mice; transcription factors; evolution, molecular; cloning, molecular; bacterial proteins; protein processing; protein processing, post-translational; recombinant fusion proteins; eukaryota; recombination, genetic; escherichia coli; gene fusion; rna translation; protein biosynthesis; binding sites; ras proteins; protein folding; tetrahydrofolate dehydrogenase; cytosol; eukaryote; ribosomes; eukaryotic cells; humans; priority journal; article |
| Journal Title: | Nature |
| Volume: | 388 |
| Issue: | 6640 |
| ISSN: | 0028-0836 |
| Publisher: | Nature Publishing Group |
| Date Published: | 1997-07-24 |
| Start Page: | 343 |
| End Page: | 349 |
| Language: | English |
| DOI: | 10.1038/41024 |
| PUBMED: | 9237751 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Article -- Export Date: 17 March 2017 -- Source: Scopus |
