Abstract
We have studied the chaperone activity and conformation of Escherichia coli heat shock protein (Hsp)33, whose activity is known to be switched on by oxidative conditions. While oxidized Hsp33 completely prevents the heat-induced aggregation of ζ-crystallin at 42°C at a ratio of 1:1 (w/w), the reduced form exhibits only a marginal effect on the aggregation. Far UV–circular dichroism (CD) spectra show that reduced Hsp33 contains a significant α-helical component. Oxidation results in significant changes in the far UV–CD spectrum. Near UV–CD spectra show changes in tertiary structural packing upon oxidation. Polarity-sensitive fluorescent probes report enhanced hydrophobic surfaces in the oxidized Hsp33. Our studies show that the oxidative activation of the chaperone function of Hsp33 involves observable conformational changes accompanying increased exposure of hydrophobic pockets.
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