Recombination of protein domains facilitated by co-translational folding in eukaryotes

@article{Netzer1997RecombinationOP,
  title={Recombination of protein domains facilitated by co-translational folding in eukaryotes},
  author={William Joseph Netzer and F. Ulrich Hartl},
  journal={Nature},
  year={1997},
  volume={388},
  pages={343-349}
}
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… CONTINUE READING

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