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Originally published In Press as doi:10.1074/jbc.M101759200 on April 13, 2001

J. Biol. Chem., Vol. 276, Issue 27, 25372-25377, July 6, 2001
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Alleviation of a Defect in Protein Folding by Increasing the Rate of Subunit Assembly*

Lili A. Aramli and Carolyn M. TeschkeDagger

From the University of Connecticut, Department of Molecular and Cell Biology, Storrs, Connecticut 06269-3125

Understanding the nature of protein grammar is critical because amino acid substitutions in some proteins cause misfolding and aggregation of the mutant protein resulting in a disease state. Amino acid substitutions in phage P22 coat protein, known as tsf (temperature-sensitive folding) mutations, cause folding defects that result in aggregation at high temperatures. We have isolated global su (suppressor) amino acid substitutions that alleviate the tsf phenotype in coat protein (Aramli, L. A., and Teschke, C. M. (1999) J. Biol. Chem. 274, 22217-22224). Unexpectedly, we found that a global su amino acid substitution in tsf coat proteins made aggregation worse and that the tsf phenotype was suppressed by increasing the rate of subunit assembly, thereby decreasing the concentration of aggregation-prone folding intermediates.

* This work was supported by National Institutes of Health Grant GM53567.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: Dept. of Molecular and Cell Biology, U-3125, University of Connecticut, 75 N. Eagleville Rd., Storrs, CT 06269-3125. Tel.: 860-486-4282; Fax: 860-486-4331; E-mail: teschke@uconn.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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S. M. Doyle, E. Anderson, K. N. Parent, and C. M. Teschke
A Concerted Mechanism for the Suppression of a Folding Defect through Interactions with Chaperones
J. Biol. Chem., April 23, 2004; 279(17): 17473 - 17482.
[Abstract] [Full Text] [PDF]


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