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Volume 271, Number 46, Issue of November 15, 1996 pp. 29060-29066
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Immobilization of the C-terminal Extension of Bovine alpha A-Crystallin Reduces Chaperone-like Activity

(Received for publication, June 13, 1996, and in revised form, September 4, 1996)

Ronald H. P. H. Smulders Dagger , John A. Carver § , Robyn A. Lindner § , Martinus A. M. van Boekel Dagger , Hans Bloemendal Dagger and Wilfried W. de Jong Dagger

From the Dagger  Department of Biochemistry, University of Nijmegen, 6500 HB Nijmegen, The Netherlands and the § Department of Chemistry, University of Wollongong, Northfields Avenue, Wollongong, New South Wales 2522, Australia

alpha -Crystallins occur as multimeric complexes, which are able to suppress precipitation of unfolding proteins. Although the mechanism of this chaperone-like activity is unknown, the affinity of alpha -crystallin for aggregation-prone proteins is probably based on hydrophobic interactions. alpha -Crystallins expose a considerable hydrophobic surface to solution, but nevertheless they are very stable and highly soluble. An explanation for this paradox may be that alpha -crystallin subunits have a polar and unstructured C-terminal extension that functions as a sort of solubilizer. In this paper we have described five alpha A-crystallins in which charged and hydrophobic residues were inserted in the C-terminal extension. Introduction of lysine, arginine, and aspartate does not substantially influence chaperone-like activity. In contrast, introduction of a hydrophobic tryptophan greatly diminishes functional activity. CD experiments indicate that this mutant has a normal secondary structure and fluorescence measurements show that the inserted tryptophan is located in a polar environment. However, NMR spectroscopy clearly demonstrates that the presence of the tryptophan residue dramatically reduces the flexibility of the C-terminal extension. Furthermore, the introduction of this tryptophan results in a considerably decreased thermostability of the protein. We conclude that changing the polarity of the C-terminal extension of alpha A-crystallin by insertion of a highly hydrophobic residue can seriously disturb structural and functional integrity.


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