Regulation of the specific DNA binding function of p53

T R Hupp, D W Meek, C A Midgley, D P Lane

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

The DNA binding activity of p53 is required for its tumor suppressor function; we show here that this activity is cryptic but can be activated by cellular factors acting on a C-terminal regulatory domain of p53. A gel mobility shift assay demonstrated that recombinant wild-type human p53 binds DNA sequence specifically only weakly, but a monoclonal antibody binding near the C terminus activated the cryptic DNA binding activity stoichiometrically. p53 DNA binding could be activated by a C-terminal deletion of p53, mild proteolysis of full-length p53, E. coli dnaK (which disrupts protein-protein complexes), or casein kinase II (and coincident phosphorylation of a C-terminal site on p53). Activation of p53 DNA binding may be critical in regulation of its ability to arrest cell growth and thus its tumor suppressor function.
Original languageEnglish
Pages (from-to)875-886
Number of pages12
JournalCell
Volume71
Issue number5
DOIs
Publication statusPublished - 27 Nov 1992

Keywords / Materials (for Non-textual outputs)

  • Animals
  • Antigen-Antibody Reactions
  • Base Sequence
  • Carrier Proteins
  • Casein Kinases
  • Cells, Cultured
  • Heat-Shock Proteins
  • Molecular Sequence Data
  • Oligodeoxyribonucleotides
  • Protein Kinases
  • Rats
  • Recombinant Proteins
  • Structure-Activity Relationship
  • Trypsin
  • Tumor Suppressor Protein p53

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