Abstract
Purpose: :
γS-crystallin is one of the lens γ-crystallins and differs in developmental expression pattern from other γ-crystallins. It is expressed in late stage as opposed to other γ-crystallins being early genes. Thus, γS-crystallin is distributed in the cortical region. We have investigated its interaction properties with other γ-crystallins as well as with the congenital cataract G18V mutant.
Methods: :
A two-hybrid system assay was used to detect protein-protein interactions. γS-crystallin and its congenital cataract mutant G18V were expressed and their biophysical properties, such as secondary and tertiary structure, thermal and conformational stability, and hydrophobicity, were compared.
Results: :
γS-crystallin shows some protein-protein interaction with other γ-crystallins (γC- and γD-) and some enhancement of interaction with G18V γS-crystallin mutant. The mutant shows no conformational change, but shows decreased thermal and conformational stability as well as increased hydrophobicity.
Keywords: crystallins • mutations • cataract