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Originally published In Press as doi:10.1074/jbc.C000156200 on April 25, 2000

J. Biol. Chem., Vol. 275, Issue 25, 18619-18622, June 23, 2000
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ACCELERATED PUBLICATION
Comparison of Folding Rates of Homologous Prokaryotic and Eukaryotic Proteins*

Margit Widmann and Philipp ChristenDagger

From the Biochemisches Institut der Universität Zürich, CH-8057 Zürich, Switzerland

The rate of polypeptide chain elongation is up to one order of magnitude faster in prokaryotic cells than in eukaryotes. Here we report that the rates of in vitro refolding of orthologous prokaryotic and eukaryotic proteins correlate with their differential rates of biosynthesis. The mitochondrial and cytosolic aspartate aminotransferases of chicken and aspartate aminotransferase of Escherichia coli show pairwise sequence identities of 41-48% and nearly identical three-dimensional structures. Nevertheless, the prokaryotic enzyme refolded 6 times faster (at 25 °C) than the eukaryotic isoenzymes after denaturation in 6 M guanidine hydrochloride. Prokaryotic malate dehydrogenase and lactate dehydrogenase also renatured faster than their orthologous eukaryotic counterparts, suggesting that evolutionary pressure has adapted the rate of folding to the rate of elongation of polypeptide chains.

* This work was supported in part by Swiss National Science Foundation Grant 31-45940.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Biochemisches Institut, Universität Zürich, Winterthurerstr. 190, CH-8057 Zürich, Switzerland. Tel.: +41-1-635-5511; Fax: +41-1-635-5907; E-mail: christen@biocfebs.unizh.ch.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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