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

William J. Netzer and F. Ulrich Hartl ()
Additional contact information
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

Nature, 1997, vol. 388, issue 6640, 343-349

Abstract: 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.

Date: 1997
References: Add references at CitEc
Citations: View citations in EconPapers (2)

Downloads: (external link)
https://www.nature.com/articles/41024 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:388:y:1997:i:6640:d:10.1038_41024

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/41024

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().