Two distinct motifs within the p53 transactivation domain bind to the Taz2 domain of p300 and are differentially affected by phosphorylation

The affinity of phosphorylated forms of the tumor suppressor p53 N-terminal acidic transactivation domains (TAD) for the transcriptional adaptor zinc-binding (Taz2) domain of p300 is explored to understand the role of phosphorylation in the regulation of p53 interactions. The findings for the two binding sites on p53 for Taz2 provide evidence for the significant role of p53 posttranslational modifications in the regulation of its protein-protein interactions.