Identification and characterization of the DNA binding domain of CpG-binding protein.

摘要: CpG-binding protein is a transcriptional activator that exhibits unique DNA binding specificity for unmethylated CpG motifs. contains cysteine-rich CXXC domain conserved in methyltransferase 1, methyl and human trithorax. In vitro assays reveal single comprised of the short carboxyl extension. Specific mutation to alanine individual cysteine residues within abolishes activity. Denaturation/renaturation experiments presence various metal cations demonstrate requires zinc efficient Ligand selection high affinity sites from pool degenerate oligonucleotides reveals interacts with variety sequences dinucleotide consensus site (A/C)CpG(A/C). Mutation motif(s) present ligand-selected ablates interaction protein, thymine nucleotides flanking motifs reduces protein. Hence, motif necessary sufficient comprise although immediate sequence affects affinity.