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Biophys J, April 2001, p. 1986-1995, Vol. 80, No. 4

Study of the Chaperoning Mechanism of Bovine Lens alpha -Crystallin, a Member of the alpha -Small Heat Shock Superfamily

Saïd Abgar, Jos Vanhoudt, Tony Aerts, and Julius Clauwaert

Biophysics Research Group, Department of Biochemistry, University of Antwerp, B-2610 Antwerp, Belgium

We have studied the interaction between lysozyme, destabilized by reducing its -S-S- bonds, and bovine eye lens alpha -crystallin, a member of the alpha -small heat shock protein superfamily. We have used gel filtration, photon correlation spectroscopy, and analytical ultracentrifugation to study the binding of lysozyme by alpha -crystallin at 25°C and 37°C. We can conclude that alpha -crystallin chaperones the destabilized protein in a two-step process. First the destabilized proteins are bound by the alpha -crystallin so that nonspecific aggregation of the destabilized protein is prevented. This complex is unstable, and a reorganization and inter-particle exchange of the peptides result in stable and soluble large particles. alpha -Crystallin does not require activation by temperature for the first step of its chaperone activity as it prevents the formation of nonspecific aggregates at 25°C as well as at 37°C. The reorganization of the peptides, however, gives rise to smaller particles at 37°C than at 25°C. Indirect evidence shows that the association of several alpha -crystallin/substrate protein complexes leads to the formation of very large particles. These are responsible for the increase of the light scattering.

Biophys J, April 2001, p. 1986-1995, Vol. 80, No. 4
© 2001 by the Biophysical Society   0006-3495/01/04/1986/10  $2.00


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