Human p53 protein is composed of 393 amino acid residues with several distinct regions. The N-terminal activation domain allows p53 protein to recruit the basal transcription machinery and activate the expression of target genes, whereas the core domain binds to target DNA in a sequence-specific manner and the majority of mutations found in human tumors occur in the region of the gene encoding this domain. The C-terminal domain is composed of predominantly basic residues and modification of the C-terminal basic domain, including acetylation, glycosylation and phosphorylation, is an essential mechanism for regulating p53 function.
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Science (New York, N.Y.), 253(5015), 49-53 (1991-07-05)
Mutations in the evolutionarily conserved codons of the p53 tumor suppressor gene are common in diverse types of human cancer. The p53 mutational spectrum differs among cancers of the colon, lung, esophagus, breast, liver, brain, reticuloendothelial tissues, and hemopoietic tissues.
It is well established that induction of the p53 tumor suppressor protein in cells can lead to either cell cycle arrest or apoptosis. To further understand features of p53 that contribute to these cell responses several p53-null Saos2 and H1299
Recent experiments have suggested that p53 action may be mediated through its interaction with DNA. We have now identified 18 human genomic clones that bind to p53 in vitro. Precise mapping of the binding sequences within these clones revealed a
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