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Protein folding

The difference with prokaryotes

Nature volume 388, pages 329–331 (1997)Cite this article

When proteins are made, they start off as chains of polypeptides. The study of how they come to fold into their correct three-dimensional structure is a wonderfully complicated business that has been tackled in numerous ways. In their paper on page 343of this issue1, Netzer and Hartl explore a somewhat neglected approach — that of looking at differences in the folding pattern of nascent polypeptides in the cytoplasm of prokaryotic and eukaryotic cells. In doing so, they tell us a great deal about some basic issues to do with protein folding, but we need to step back a little to understand why.

Anfinsen's classic in vitro experiments on the refolding of ribonuclease2,3 demonstrated that all of the information required to determine the final conformation of a protein can reside in the polypeptide chain itself: given the appropriate conditions, a denatured enzyme can refold into its native conformation in the absence of any other protein. Anfinsen's work was of seminal importance in establishing the central principle of self-assembly of proteins, but it probably delayed by a decade or two the initiation of investigations of protein folding in vivo — the trouble was we believed that the polypeptide sequence was all that there was to it. Nevertheless, over time we came to recognize that efficient folding in vitro is frequently limited to small, single-domain proteins and usually occurs under conditions of protein concentration, temperature, ionic strength and pH far removed from those occurring within cells.

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Authors and Affiliations

  1. Department of Biochemistry and Molecular Biology, University of Melbourne, Parkville, 3052, Victoria, Australia

    Mary-Jane Gething

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  1. Mary-Jane Gething
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Gething, MJ. The difference with prokaryotes. Nature 388, 329–331 (1997). https://doi.org/10.1038/40979

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