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Papers In Press, published online ahead of print April 25, 2000
J. Biol. Chem, 10.1074/jbc.C000156200
Submitted on March 10, 2000
Accepted on April 20, 2000

Comparison of folding rates of homologous prokaryotic and eukaryotic proteins

Margit Widmann and Philipp Christen

Biochemisches Institut, Universität Zürich, Zürich, ZH 8057

Corresponding Author: christen{at}biocfebs.unizh.ch

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 3-D 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.


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