Specific interaction between the p53 cellular tumour antigen and major heat shock proteins

Nature. 1986 Mar 13-19;320(6058):182-4. doi: 10.1038/320182a0.


The protein p53 is capable of participating in neoplastic transformation and can form specific complexes with the large-T antigen of simian virus 40 (SV40). This interaction probably results in the stabilization of p53 (refs 7,8) and may contribute to SV40-mediated transformation. Several non-SV40-transformed cells also exhibit a stabilized p53 which is present in elevated levels. Recently, this stabilization was shown to coincide with the ability to precipitate a polypeptide (p68) of relative molecular mass (Mr) 68,000-70,000 by anti-p53 monoclonal antibodies. We now report that this co-precipitation indeed represents a specific complex between the two proteins; the complex sediments on a sucrose gradient as a relatively broad peak of 10-14S and can be dissociated in vitro. Furthermore, p68 is the HSP70 heat shock protein cognate, found in elevated levels in a p53-overproducing cell line. On heat-shock treatment of such overproducers, p53 also forms a complex with the related highly inducible HSP68.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Cell Cycle
  • Cells, Cultured
  • Heat-Shock Proteins / metabolism*
  • Isoelectric Point
  • Molecular Weight
  • Neoplasm Proteins / metabolism*
  • Phosphoproteins / metabolism*
  • Protein Binding
  • Rats
  • Tumor Suppressor Protein p53


  • Heat-Shock Proteins
  • Neoplasm Proteins
  • Phosphoproteins
  • Tumor Suppressor Protein p53