αA-Crystallin-derived mini-chaperone modulates stability and function of cataract causing αAG98R-crystallin.

ABSTRACT:

Background

A substitution mutation in human αA-crystallin (αAG98R) is associated with autosomal dominant cataract. The recombinant mutant αAG98R protein exhibits altered structure, substrate-dependent chaperone activity, impaired oligomer stability and aggregation on prolonged incubation at 37 °C. Our previous studies have shown that αA-crystallin-derived mini-chaperone (DFVIFLDVKHFSPEDLTVK) functions like a molecular chaperone by suppressing the aggregation of denaturing proteins. The present study was undertaken to determine the effect of αA-crystallin-derived mini-chaperone on the stability and chaperone activity of αAG98R-crystallin.

Methodology/principal findings

Recombinant αAG98R was incubated in presence and absence of mini-chaperone and analyzed by chromatographic a

SUBMITTER: Raju M 

PROVIDER: S-EPMC3435407 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature