Abstract
THE function of transformation proteins coded for by RNA-and DNA-containing tumour viruses is a major question in oncology. A large number of diverse alterations are produced in cells following viral transformation, and such changes are thought to be the result of the action of one or a very few viral gene products. Until recently, very little was known concerning the mechanism of action of such transforming proteins. However, studies carried out by Collett and Erikson with the RNA tumour virus Rous sarcoma virus (RSV) suggested that the RSV transforming protein, src, either possesses or is associated with protein kinase activity1. Using antiserum directed against virus-coded proteins, it was found that phosphorylation of the heavy chain of the antibody occurred when immunoprecipitates containing src protein were incubated with [γ-32P]ATP. No such protein kinase activity was observed in immunoprecipitates using uninfected cell extracts, extracts from cells infected with transformation-defective virus, or control nonimmune serum. These data suggest that alterations in protein phosphorylation may regulate RSV transformation. This concept is quite appealing, as protein phosphorylation is already known to have an important regulatory role in several cellular processes2–4. We show here that antiserum directed against tumour antigens of a DNA virus, human adenovirus type 5 (Ad 5), will also immunoprecipitate protein kinase activity. Further, immunoprecipitates from cells infected with transformation-defective host range mutants of Ad 5 contain reduced levels of protein kinase activity.
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
Collett, M. S. & Erikson, R. L. Proc. natn. Acad. Sci. U.S.A. 75, 2021–2024 (1978).
Krebs, E. G. Curr. Topics cell. Regulation 5, 99–133 (1972).
Langan, T. A. Adv. Cyclic Nucleotide Res. 3, 99–153 (1973).
Rubin, C. S. & Rosen, O. M. A. Rev. Biochem. 44, 831–887 (1975).
Sambrook, J. et al. Cold Spring Harb. Symp. quant. Biol. 39, 615–632 (1974).
Flint, S. J., Sambrook, J., Williams, J. F. & Sharp, P. A. Virology 72, 456–470 (1976).
Graham, F. L. et al. Cold Spring Harb. Symp. quant. Biol. 39, 615–632 (1974).
Gallimore, P. H., Sharp, P. A. & Sambrook, J. J. molec. Biol. 89, 49–72 (1974).
Schaffhausen, B. S., Silver, J. E. & Benjamin, T. L. Proc. natn. Acad. Sci. U.S.A. 75, 79–84 (1978).
Harrison, T., Graham, F. L. & Williams, J. Virology 77, 319–329 (1977).
Graham, F. L., Harrison, T. & Williams, J. Virology 86, 10–21 (1978).
Branton, P. E. & Landry-Magnan, J. Biochim. biophys. Acta 508, 246–259 (1978).
Ross, S. R., Linzer, D. I. H., Flint, S. J. & Levine, A. J. in ICNU-UCLA Symp. Persistent Viruses (eds Stevens, J. & Todaro, G.) (in the press).
Lassam, N. J., Bayley, S. T. & Graham, F. L. (in preparation).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
LASSAM, N., BAYLEY, S., GRAHAM, F. et al. Immunoprecipitation of protein kinase activity from adenovirus 5-infected cells using antiserum directed against tumour antigens. Nature 277, 241–243 (1979). https://doi.org/10.1038/277241a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/277241a0
This article is cited by
-
Protein kinase in immunoprecipitate of DMBA-transformed epithelial cells with serum from tumour-bearing rabbits
Nature (1980)
-
Guanine nucleotide-binding and autophosphorylating activities associated with the p21src protein of Harvey murine sarcoma virus
Nature (1980)
-
Malignant transformation and protein phosphorylation
Nature (1980)
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.