Resistance of α-Crystallin Quaternary Structure to UV Irradiation

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A. V. Krivandin^*, K. O. Muranov, F. Yu. Yakovlev, N. B. Poliansky, L. A. Wasserman, and M. A. Ostrovsky

Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, Russia; E-mail: a.krivandin@sky.chph.ras.ru

^* To whom correspondence should be addressed.

Received November 17, 2008; Revision received December 31, 2008

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The damaging effect of UV radiation (λ > 260 nm) on bovine α-crystallin in solution was studied by small-angle X-ray scattering, gel permeation chromatography, electrophoresis, absorption and fluorescence spectroscopy, and differential scanning calorimetry. The results obtained show that damage to even a large number of subunits within an α-crystallin oligomer does not cause significant rearrangement of its quaternary structure, aggregation of oligomers, or the loss of their solubility. Due to the high resistance of its quaternary structure, α-crystallin is able to prevent aggregation of destabilized proteins (especially of γ- and β-crystallins) and so to maintain lens transparency throughout the life of an animal (the chaperone-like function of α-crystallin).

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KEY WORDS: α-crystallin, quaternary structure, UV radiation, small-angle X-ray scattering

DOI: 10.1134/S0006297909060078

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