Molecular mechanism of the chaperone function of mini-α-crystallin, a 19-residue peptide of human α-crystallin.

ABSTRACT: α-Crystallin is the archetypical chaperone of the small heat-shock protein family, all members of which contain the so-called "α-crystallin domain" (ACD). This domain and the N- and C-terminal extensions are considered the main functional units in its chaperone function. Previous studies have shown that a 19-residue fragment of the ACD of human αA-crystallin called mini-αA-crystallin (MAC) shows chaperone properties similar to those of the parent protein. Subsequent studies have confirmed the function of this peptide, but no studies have addressed the mechanistic basis for the chaperone function of MAC. Using human γD-crystallin (HGD), a key substrate protein for parent α-crystallin in the ocular lens, we show here that MAC not only protects HGD from aggregation during thermal and chemical

SUBMITTER: Banerjee PR 

PROVIDER: S-EPMC4303307 | biostudies-literature | 2015 Jan

REPOSITORIES: biostudies-literature