Publication

Abstract : BZIP are a class of dimeric sequence specifi c DNA-binding proteins, is bipartite in structure containing regionof enriched basic amino acids which is adjacent to leucine zippers. It is characterized by several leucine residuesregularly spaced at seven amino acid intervals, basic region directly contacts with DNA. The leucine zipper mediatesheterodimerization and homodimerization of protein monomers through parallel interactions which is unique toeukaryotes. The plant Arabidopsis thaliana genome shows 67 BZIP proteins. We have predicted dimeric propertiesof alpha helical leucine zipper and coiled coil structure of BZIP proteins in plants. In this analysis the length of leucinezippers, placement of asparagines in the hydrophobic interface and presence of interhelical electrostatic interactionswere focused. Phylogenetic tree was also constructed by studying evolutionary relationship of BZIB existing among theplants.