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J. Biol. Chem., Vol. 269, Issue 44, 27264-27268, Nov, 1994
B Raman and CM Rao
alpha-Crystallin has been shown to function as a molecular chaperone in
preventing thermal aggregation of crystallins and other proteins. The
molecular mechanism of this protection is not yet clear. gamma- Crystallin
aggregates upon exposure to UV light. We have investigated the effect of
the presence of alpha-crystallin in the photoaggregation process and find
that alpha-crystallin does not prevent photoaggregation at low
temperatures. The protection starts around 30 degrees C and steeply
increases with temperature. The plot of protection ability versus
temperature is sigmoidal, indicating a structural transition. Perturbation
of the quaternary structure of alpha by non-thermal mode, such as 3 M urea,
also results in enhanced protection. Pyrene, a hydrophobic fluorophore, is
sparingly soluble in water. alpha-Crystallin enhances the solubility of
pyrene by severalfold. Temperature dependence of this solubilization shows
a transition around 30 degrees C (another at about 50 degrees C).
Fluorescence intensity ratio of third and first peaks of pyrene emission
(I3/I1,), indicative of hydrophobicity of the reporting area, also shows
similar transitions suggesting enhanced hydrophobicity. Gel filtration
experiments of irradiated samples indicate the complex formation between
gamma- and alpha-crystallins. alpha-Crystallin does not prevent cold
precipitation of gamma-crystallin. On the basis of these results, we
hypothesize that alpha-crystallin prevents aggregation of non-native
structures by providing appropriately placed hydrophobic surfaces. A
structural transition above 30 degrees C enhances the protective ability,
perhaps by increasing or reorganizing the hydrophobic surfaces. A similar
temperature dependence has been reported for GroEL. Whether a structural
switch, either activated by temperature, solvent conditions, or small
molecule binding, forms a part of the general mechanism of chaperone
activity needs to be investigated.
Chaperone-like activity and quaternary structure of alpha-crystallin
Center for Cellular and Molecular Biology, Hyderabad, India.
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