Abstract
The protein p53 is capable of participating in neoplastic transformation1–3 and can form specific complexes with the large-T antigen of simian virus 40 (SV40)4–6. This interaction probably results in the stabilization of p53 (refs 7, 8) and may contribute to SV40-mediated transformation9,10. Several non-SV40-trans-formed cells also exhibit a stabilized p53 which is present in elevated levels11–13. 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 antibodies13–15. 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 overproduces, p53 also forms a complex with the related highly inducible HSP68.
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Pinhasi-Kimhi, O., Michalovitz, D., Ben-Zeev, A. et al. Specific interaction between the p53 cellular tumour antigen and major heat shock proteins. Nature 320, 182–185 (1986). https://doi.org/10.1038/320182a0
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DOI: https://doi.org/10.1038/320182a0
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