Carboxyl-region of tuftelin mediates self-assembly

Enamel biomineralization relies on a complex series of protein-protein interactions resulting in the formation of an enamel matrix. This protein matrix is subsequently replaced by a fully mineralized crystallite material. The enamel extracellular matrix is comprised principally by two gene products; the amelogenins and enamelins. The enamelins, including the 389 amino-acid, 44kDa tuftelin, are a group of acidic proteins found in the enamel extracellular matrix. This study has employed the yeast two-hybrid system to investigate the ability of tuftelin to self-assemble and to define protein regions participating in tuftelin self-assembly. We show that for tuftelin the amino-acid residues 252 through 345 contain structurally relevant determinants for self-assembly.