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Science 16 October 1992:
Vol. 258. no. 5081, pp. 466 - 468
DOI: 10.1126/science.1357751
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Articles

Science, Vol 258, Issue 5081, 466-468
Copyright © 1992 by American Association for the Advancement of Science

articles

Isomerase and chaperone activity of prolyl isomerase in the folding of carbonic anhydrase

PO Freskgard, N Bergenhem, BH Jonsson, M Svensson, and U Carlsson

Institutionen for Fysik och Matteknik/Department of Chemistry, Linkoping University, Sweden.

Several proteins have been discovered that either catalyze slow protein-folding reactions or assist folding in the cell. Prolyl isomerase, which has been shown to accelerate rate-limiting cis-trans peptidyl-proline isomerization steps in the folding pathway, can also participate in the protein-folding process as a chaperone. This function is exerted on an early folding intermediate of carbonic anhydrase, which is thereby prevented from aggregating, whereas the isomerase activity is performed later in the folding process.


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