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 pro tein matrix is subsequently replaced by a fully mineralized crystallit e material. The enamel extracellular matrix is comprised principally b y two gene products; the amelogenins and enamelins, The enamelins, inc luding the 389 amino-acid, 44kDa tuftelin, are a group of acidic prote ins 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 t hrough 345 contain structurally relevant determinants for self-assembl y.