COMPARISON OF THE HOMOLOGOUS CARBOXY-TERMINAL DOMAIN AND TAIL OF ALPHA-CRYSTALLIN AND SMALL HEAT-SHOCK PROTEIN

The C-terminal domain and tail, which is the most conserved region of the alpha-crystallin/small heat shock protein (HSP) family, was obtained from rat alphaA-crystallin, bovine alphaB-crystallin and mouse HSP25. All three domains have primarily beta-sheet conformation and less than 10% of alpha-helix, like the proteins from which they are derived. Whereas the C-terminal part of alphaA-crystallin forms dimer or tetramers, the corresponding regions for the alpha-crystallin/small HSP family, is not retained in the C-terminal domain and tail. In the course of this study some differences with the previously published sequence of HSP25 were observed, and a revision is proposed.