Abstract
Mammalian ras oncogenes encode polypeptides of relative molecular mass (Mr) 21,000 (p21) which bind GTP and GDP1,2. Oncogenic ras-encoded proteins differ from their normal homologues by an amino acid substitution for Gly 12, Ala 59 or Gln 61 (refs 3–14). Recently, we and others have observed that normal p21, encoded by the Ha-ras gene, has a GTP hydrolytic activity that is reduced by the oncogenic substitutions Val 12 (refs 15–17) or Thr 59 (ref. 15). The yeast Saccharomyces cerevisiae contains two ras-related genes, RASsc1 and RASsc2 (refs 18, 19), the expression of either of which is sufficient for viability20,21. RASsc1 and RASsc2 encode proteins of 309 (SC1) and 322 (SC2) residues which are 62% homologous to mammalian p21 in their 172-amino acid N-terminal sequences19,22. We report here that the N-terminal domain of SC1 binds GTP and GDP and has a GTP hydrolytic activity that is reduced in the variants SC1 [Thr 66] and SC1[Leu 68] which are analogous to oncogenic Ha[Thr 59] and Ha[Leu 61], respectively. These results suggest that yeast and mammalian ras proteins have similar biochemical and possibly biological functions.
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References
Scolnick, E. M., Papageorge, A. G. & Shih, T. Y. Proc. natn. Acad. Sci. U.S.A. 76, 5355–5359 (1979).
Shih, T. Y., Papageorge, A. G., Stokes, P. E., Weeks, M. O. & Scolnick, E. M. Nature 287, 686–691 (1980).
Reddy, E. P., Reynolds, R. K., Santos, E. & Barbacid, M. Nature 300, 148–152 (1982).
Tabin, C. J. et al. Nature 300, 143–148 (1982).
Taparowsky, E. et al. Nature 300, 762–765 (1982).
Capon, D. J. et al. Nature 304, 501–507 (1982).
Yuasa, Y. et al. Nature 303, 775–779 (1982).
Taparowsky, E., Shimizu, K., Goldfarb, M. & Wigler, M. Cell 34, 581–586 (1983).
Sukumar, S., Notario, V., Martin-Zanca, D. & Barbacid, M. Nature 306, 658–661 (1983).
Santos, E., Reddy, E. P., Pulciani, S., Feldmann, R. J. & Barbacid, M. Proc. natn. Acad. Sci. U.S.A. 80, 4679–4683 (1983).
Yuasa, Y. et al. Proc. natn. Acad. Sci. U.S.A. 81, 3670–3674 (1984).
Sekiya, T. et al. Proc. natn. Acad. Sci. U.S.A. 81, 4771–4775 (1984).
Dahr, R. et al. Science 217, 934–937 (1982).
Tsuchida, N., Ryder, T. & Ohtsubo, E. Science 217, 937–938 (1982).
Gibbs, J. B., Sigal, I. S., Poe, M. & Scolnick, E. M. Proc. natn. Acad. Sci. U.S.A. 81, 5704–5708 (1984).
McGrath, J. P., Capon, D. J., Goeddel, D. V. & Levinson, A. D. Nature 310, 644–649 (1984).
Sweet, R. W. et al. Nature 311, 273–275 (1984).
DeFeo-Jones, D., Scolnick, E. M., Koller, R. & Dahr, R. Nature 306, 707–709 (1983).
Powers, S. et al. cell 36, 607–612 (1984).
Tatchell, K., Chaleff, D. T., DeFeo-Jones, D. & Scolnick, E. M. Nature 309, 523–527 (1984).
Kataoka, T. et al. Cell 37, 437–445 (1984).
Dahr, R., Nieto, A., Koller, R., DeFeo-Jones, D. & Scolnick, E. M. Nucleic Acids Res. 12, 3611–3618 (1984).
Stein, R. B., Robinson, P. S. & Scolnick, E. M. J. Virol. 50, 343–351 (1984).
Furth, M. E., Davis, L. J., Fleurdelys, B. & Scolnick, E. M. J. Virol. 43, 294–304 (1982).
Gibbs, J. B., Ellis, R. W. & Scolnick, E. M. Proc. natn. Acad. Sci U.S.A. 81, 2674–2678 (1984).
Temeles, G. L., DeFeo-Jones, D., Tatchell, K., Ellinger, M. S. & Scolnick, E. M. Molec. cell. Biol. 4, 2298–2305 (1984).
Poe, M., Scolnick, E. M. & Stein, R. B. J. biol. Chem. (in the press).
Pincus, M. R. et al. Proc. natn. Acad. Sci. U.S.A. 80, 5253–5257 (1983).
Laemmli, U. K. Nature 227, 680–684 (1970).
Bradford, M. Analyt. Biochem. 72, 248–252 (1976).
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Temeles, G., Gibbs, J., D'Alonzo, J. et al. Yeast and mammalian ras proteins have conserved biochemical properties. Nature 313, 700–703 (1985). https://doi.org/10.1038/313700a0
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DOI: https://doi.org/10.1038/313700a0
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