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.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Eliyahu, D., Raz, A., Gruss, P., Givol, D. & Oren, M. Nature 312, 646–649 (1984).
Parada, L. F., Land, H., Weinberg, R. A., Wolf, D. & Rotter, V. Nature 312, 649–651 (1984).
Jenkins, J. R., Rudge, K. & Currie, G. A. Nature 312, 651–654 (1984).
Crawford, L. V. et al. Cold Spring Harb. Symp. quant. Biol. 44, 179–187 (1980).
McCormick, F. & Harlow, E. J. Virol. 34, 213–224 (1980).
Lane, D. P., Gannon, J. & Winchester, G. Adv. viral Oncol. 2, 23–39 (1982).
Oren, M., Maltzman, W. & Levine, A. J. Molec. cell. Biol. 1, 101–110 (1981).
Mora, P. T., Chandrasekaran, K., Hoffman, J. C. & McFarland, V. W. Molec. cell. Biol. 2, 763–771 (1982).
May, E., Lasne, C., Prives, C., Borde, J. & May, P. J. Virol. 45, 901–913 (1983).
Montenarh, M., Kohler, M., Aggeler, G. & Henning, R. EMBO J. (in the press).
Oren, M., Reich, N. C. & Levine, A. J. Molec. cell. Biol. 2, 443–449 (1982).
Reich, N. C., Oren, M. & Levine, A. J. Molec. cell. Biol. 3, 2143–2150 (1983).
Gronostajski, R. M., Goldberg, A. L. & Pardee, A. B. Molec. cell. Biol. 4, 442–448 (1984).
Ruscetti, S. K. & Scolnick, E. M. J. Virol. 46, 1022–1026 (1983).
Pinhasi, O. & Oren, M. Molec. cell. Biol. 4, 2180–2186 (1984).
Harlow, E., Crawford, L. V., Pim, D. C. & Williamson, N. M. J. Virol. 39, 861–869 (1981).
Rotter, V., Witte, O. N., Coffman, R. & Baltimore, D. J. Virol. 36, 547–555 (1980).
Crawford, L. V. Adv. viral Oncol. 2, 3–21 (1982).
Rotter, V., Friedman, H., Katz, A., Zerivitz, K. & Wolf, D. J. Immun. 131, 329–333 (1983).
Cleveland, D., Fisher, S., Kirshner, M. & Laemmli, U. K. J. biol. Chem. 252, 1102–1106 (1977).
Bensaude, O. & Morange, M. EMBO J. 2, 173–177 (1983).
Morange, M., Diu, A., Bensaude, O. & Babinet, C. Molec. cell. Biol. 4, 730–735 (1984).
Lowe, D. G. & Moran, L. A. Proc. natn. Acad. Sci. U.S.A. 81, 2317–2321 (1984).
Welch, W. J. & Feramisco, J. R. Molec. cell. Biol. 5, 1929–1937 (1985).
Steinberg, B., Pollack, R., Topp, W. & Botchan, M. Cell 13, 19–32 (1978).
Eliyahu, D., Michalovitz, D. & Oren, M. Nature 316, 158–160 (1985).
Opperman, H., Levinson, W. & Bishop, J. M. Proc. natn. Acad. Sci. U.S.A. 78, 1067–1071 (1981).
Welch, W. J. & Feramisco, J. R. J. biol. Chem. 259, 4501–4513 (1984).
Velasquez, J. M. & Lindquist, S. Cell 36, 655–662 (1984).
Rotter, V., Abutbul, H. & Ben-Zeev, A. EMBO J. 2, 1041–1047 (1983).
Tooze, J. (ed.) DNA Tumor Viruses Pt 2 (Cold Spring Harbor Laboratory, New York, 1982).
Bardwell, J. C. A. & Craig, E. Proc. natn. Acad. Sci. U.S.A. 81, 848–852 (1984).
Zylicz, M. & Georgopoulos, C. P. J. biol. Chem. 259, 8820–8825 (1984).
Kao, H. T., Capassa, D., Heintz, N. & Nevins, J. R. Molec. cell. Biol. 5, 628–633 (1985).
Curran, T., Van Beveren, C., Ling, N. & Verma, I. M. Molec. cell. Biol. 5, 167–172 (1985).
O'Farrell, P. Z., Goodman, H. M. & O'Farrell, P. H. Cell 12, 1133–1142 (1977).
Oren, M. & Levine, A. J. Proc. natn. Acad. Sci. U.S.A. 80, 56–59 (1983).
Bienz, B., Zakut-Houri, R., Givol, D. & Oren, M. EMBO J. 3, 2179–2184 (1984).
Mattzman, W., Oren, M. & Levine, A. J. Virology 112, 145–156 (1981).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
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
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/320182a0
This article is cited by
-
Transition of amyloid/mutant p53 from tumor suppressor to an oncogene and therapeutic approaches to ameliorate metastasis and cancer stemness
Cancer Cell International (2022)
-
A novel Hsp70 inhibitor prevents cell intoxication with the actin ADP-ribosylating Clostridium perfringens iota toxin
Scientific Reports (2016)
-
Hsp70 molecular chaperones are required to support p53 tumor suppressor activity under stress conditions
Oncogene (2009)
-
Simian virus 40 and cancer
Oncology Reviews (2007)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.