Abstract
Human Ha-ras1 cDNAs encoding normal and activated p21 polypeptides have been efficiently expressed in Escherichia coli and the biochemical activities associated with each polypeptide compared. In addition to the guanine nucleotide binding activity, normal p21 displays a GTPase activity which is selectively impaired by a mutation which activates its oncogenic potential
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
Shih, C., Shilo, B-Z., Goldfarb, M. P., Dannenberg, A. & Weinberg, R. A. Proc. natn. Acad. Sci. U.S.A. 76, 5714–5718 (1979).
Cooper, G. M., Okenquist, S. & Silverman, L. Nature 284, 418–421 (1980).
Shih, C., Padhy, L. C., Murray, M. & Weinberg, R. A. Nature 290, 261–264 (1981).
Krontiris, T. G. & Cooper, G. M. Proc. natn. Acad. Sci. U.S.A. 78, 1181–1184 (1981).
Perucho, M. et al. Cell 27, 467–476 (1981).
Land, M., Parada, L. F. & Weinberg, R. A. Science 222, 771–778 (1983).
Ellis, R. W. et al. Nature 292, 506–511 (1981).
Tabin, C. J. et al. Nature 300, 143–149 (1982).
Reddy, E. P., Reynolds, R. K., Santos, E. & Barbacid, M. Nature 300, 149–152 (1982).
Capon, D. J., Chen, E. Y., Levinson, A. D., Seeburg, P. H. & Goeddel, D. V. Nature 302, 33–37 (1983).
Capon, D. J. et al. Nature 304, 507–513 (1983).
Shimizu, K., Goldfarb, M., Perucho, M. & Wigler, M. Proc. natn. Acad. Sci. U.S.A. 80, 383–387 (1983).
McGrath, J. P. et al. Nature 304, 501–506 (1983).
Taparowsky, E., Shimizu, K., Goldfarb, M. & Wigler, M. Cell 34, 581–586 (1983).
Yuasa, Y. et al. Nature 303, 775–779 (1983).
Willingham, M. C., Pastan, I., Shih, T. Y. & Scolnick, E. M. Cell 19, 1005–1014 (1980).
Furth, M. E., Davis, L. J., Fleurdelys, B. & Scolnick, E. M. J. Virol. 43, 294–304 (1982).
Finkel, T., Der, C. J. & Cooper, G. M. Cell 37, 151–158 (1984).
Shih, T. Y., Papageorge, A. G., Stokes, P. E., Weeks, M. O. & Scolnick, E. M. Nature 287, 686–691 (1980).
Shih, T. Y. et al. J. Virol. 42, 253–261 (1982).
Papageorge, A., Lowy, D. & Scolnick, E. M. J. Virol. 44, 509–519 (1982).
Reddy, E. P. Science 220, 1061–1063 (1983).
Gluzman, Y. Cell 23, 175–182 (1981).
Goldfarb, M., Shimizu, K., Perucho, M. & Wigler, M. Nature 296, 404–409 (1982).
Fasano, O., Taparowsky, E., Fiddes, J., Wigler, M. & Goldfarb, M. J. molec. appl. Genet. 2, 173–180 (1983).
Goeddel, D. V. et al. Nature 287, 411–416 (1980).
Sefton, B. M., Trowbridge, I. S., Cooper, J. A. & Scolnick, E. M. Cell 31, 465–474 (1982).
Gibbs, J. B., Ellis, R. W. & Scolnick, E. M. Proc. natn. Acad. Sci. U.S.A. 81, 2674–2678 (1984).
Der, C. J. & Cooper, G. M. Cell 32, 201–208 (1983).
Gay, N. J. & Walker, J. E. Nature 301, 262–264 (1983).
Weirenga, R. K. & Hol, W. G. J. Nature 302, 842–844 (1983).
Shih, T. Y., Stokes, P. E., Smythers, G. W., Dhar, R. & Oroszlan, S. J. biol. Chem. 257, 11767–11773 (1982).
Morrison, J. F. & Heyde, E. A. Rev. Biochem. 41, 29–54 (1972).
Gilman, A. G. Cell 36, 577–579 (1984).
Leberman, R. & Egner, U. EMBO J. 3, 339–341 (1984).
Scolnick, E. M., Papageorge, A. G. & Shih, T. Y. Proc. natn. Acad. Sci. U.S.A. 76, 5355–5359 (1979).
Lautenberger, J. A., Ulsh, L., Shih, T. Y. & Papas, T. S. Science 221, 858–860 (1983).
Gershoni, J. M. & Palade, G. E. Analyt. Biochem. 131, 1–15 (1983).
Wang, J. & Koshland, D. E. J. biol. Chem. 253, 7605–7608 (1978).
Garnak, M. & Reeves, H. C. J. biol. Chem. 254, 7915–7920 (1979).
Sompayrac, L. M. & Danna, K. J. Proc. natn. Acad. Sci. U.S.A. 78, 7575–7578 (1981).
Aviv, M. & Leder, P. Proc. natn. Acad. Sci. U.S.A. 69, 1408–1412 (1972).
Wickens, M. P., Buell, G. N. & Schimke, R. T. J. Biol. Chem. 253, 2483–2495 (1978).
Goeddel, D. V. et al. Nature 281, 544–548 (1979).
Grunstein, M. & Hogness, D. Proc. natn. Acad. Sci. U.S.A. 72, 3961–3965 (1975).
Crea, R. & Horn, T. Nucleic Acids Res. 8, 2331–2348 (1980).
Wallace, R. B., Schold, M., Johnson, M. J., Dembek, P. & Itakura, K. Nucleic Acids Res. 9, 3647–3656 (1981).
Towbin, H., Staehelin, T. & Gordon, J. Proc. natn. Acad. Sci. U.S.A. 76, 4350–5354 (1979).
McGrath, J. P. & Levinson, A. D. Nature 295, 423–425 (1982).
Chang, E., Furth, M., Scolnick, E. & Lowy, D. Nature 297, 479–483 (1982).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
McGrath, J., Capon, D., Goeddel, D. et al. Comparative biochemical properties of normal and activated human ras p21 protein. Nature 310, 644–649 (1984). https://doi.org/10.1038/310644a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/310644a0
This article is cited by
-
Retroviral oncogenes: a historical primer
Nature Reviews Cancer (2012)
-
HRAS mutants identified in Costello syndrome patients can induce cellular senescence: possible implications for the pathogenesis of Costello syndrome
Journal of Human Genetics (2011)
-
Ras oncogenes: split personalities
Nature Reviews Molecular Cell Biology (2008)
-
Costello syndrome: clinical diagnosis in the first year of life
European Journal of Pediatrics (2008)
-
ARHI is a Ras-related small G-protein with a novel N-terminal extension that inhibits growth of ovarian and breast cancers
Oncogene (2003)
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.