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

Author

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  • William J. Netzer

    (*Cellular Biochemistry & Biophysics Program and Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center)

  • F. Ulrich Hartl

    (*Cellular Biochemistry & Biophysics Program and Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center
    †Max-Planck-Institut für Biochemie)

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.

Suggested Citation

  • William J. Netzer & F. Ulrich Hartl, 1997. "Recombination of protein domains facilitated by co-translational folding in eukaryotes," Nature, Nature, vol. 388(6640), pages 343-349, July.
    • Handle: RePEc:nat:nature:v:388:y:1997:i:6640:d:10.1038_41024
    DOI: 10.1038/41024
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    Cited by:

    1. Minkoo Ahn & Tomasz Włodarski & Alkistis Mitropoulou & Sammy H. S. Chan & Haneesh Sidhu & Elena Plessa & Thomas A. Becker & Nediljko Budisa & Christopher A. Waudby & Roland Beckmann & Anaïs M. E. Cass, 2022. "Modulating co-translational protein folding by rational design and ribosome engineering," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    2. Thapakorn Jaroentomeechai & Yong Hyun Kwon & Yiwen Liu & Olivia Young & Ruchika Bhawal & Joshua D. Wilson & Mingji Li & Digantkumar G. Chapla & Kelley W. Moremen & Michael C. Jewett & Dario Mizrachi &, 2022. "A universal glycoenzyme biosynthesis pipeline that enables efficient cell-free remodeling of glycans," Nature Communications, Nature, vol. 13(1), pages 1-17, December.

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