THE P53 NUCLEAR-LOCALIZATION SIGNAL IS STRUCTURALLY LINKED TO A P34CDC2 KINASE MOTIF

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  • 1 March 1990
    • journal article
    • research article
    • Vol. 5  (3) , 423-426
Abstract
We have identified a region of human p53 proteinwith striking homology to a sequence motif on Simian Virus 40 T antigen which includes the nuclear localisation signal. Mutation of basic amino acid residues in this region of p53 (residues 312 to 323; SSSPQPKKKP) compromises transport of p53 protein to the nucleus. The sequence functions efficiently as a nuclear localisation signal when fused to Escherichia coli .beta. galactosidase. Serine 315 within this p53 structural motif is phosphorylated in vitro by the cell cycle kinase p34cdc2. Thus in both T antigen and p53, nuclear localisation signal and p34cdc2 kinase acceptor residue map to a contiguous region of primary amino acid sequence.