Functional validation of hydrophobic adaptation to physiological temperature in the small heat shock protein αA-crystallin.

ABSTRACT: Small heat shock proteins (sHsps) maintain cellular homeostasis by preventing stress and disease-induced protein aggregation. While it is known that hydrophobicity impacts the ability of sHsps to bind aggregation-prone denaturing proteins, the complex quaternary structure of globular sHsps has made understanding the significance of specific changes in hydrophobicity difficult. Here we used recombinant protein of the lenticular sHsp α A-crystallin from six teleost fishes environmentally adapted to temperatures ranging from -2°C to 40°C to identify correlations between physiological temperature, protein stability and chaperone-like activity. Using sequence and structural modeling analysis we identified specific amino acid differences between the warm adapted zebrafish and cold adapted Antarc

SUBMITTER: Posner M 

PROVIDER: S-EPMC3315530 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature