Abstract
A group of membrane-associated guanine nucleotide binding proteins (G-proteins) are essential for transducing signals generated at cell-surface receptors into changes in cellular function and metabolism1. These proteins are a complex of three subunits designated α, β and γ. The α-subunit is responsible for binding guanine nucleotides and seems to be characteristic of each protein. Transducin, a member of this protein family, mediates visual transduction by coupling the signal of photolysed rhodopsin with activation of a cyclic GMP phosphodiesterase2. We have now cloned and sequenced the complementary DNA encoding the α-subunit of bovine retinal transducin and from this we have deduced the complete amino-acid sequence. The transducin α-subunit shares several homologous amino-acid sequences with ras gene products. The homologous segments correspond mostly to the regions thought to be involved in the guanine nucleotide binding and GTPase activity of ras proteins and to the ADP-ribosylation sites of the transducin α-subunit.
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
Gilman, A. G. Cell 36, 577–579 (1984).
Stryer, L. Cold Spring Harb. Symp. quant. Biol. 48, 841–852 (1983).
Vieira, J. & Messing, J. Gene 19, 259–268 (1982).
Helfman, D. M., Feramisco, J. R., Fiddes, J. C., Thomas, G. P. & Hughes, S. H. Proc. natn. Acad. Sci. U.S.A. 80, 31–35 (1983).
Maxam, A. M. & Gilbert, W. Meth. Enzym. 65, 499–560 (1980).
Okayama, H. & Berg, P. Molec. cell. Biol. 2, 161–170 (1982).
Hanahan, D. & Meselson, M. Gene 10, 63–67 (1980).
Baehr, W. Morita, E. A., Swanson, R. J. & Applebury, M. L. J. biol. Chem. 257, 6452–6460 (1982).
Thomas, P. S. Proc. natn. Acad. Sci. U.S.A. 77, 5201–5205 (1980).
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).
Willingham, M. C., Pastan, I., Shih, T. Y. & Scolnick, E. M. Cell 19, 1005–1014 (1980).
McGrath, J. P., Capon, D. J., Goeddel, D. V. & Levinson, A. D. Nature 310, 644–649 (1984).
Gay, N. J. & Walker, J. E. Nature 301, 262–264 (1983).
Wierenga, 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).
Leberman, R. & Egner, U. EMBO J. 3, 339–341 (1984).
Arai, K. et al. Proc. natn. Acad. Sci. U.S.A. 77, 1326–1330 (1980).
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).
Taparowsky, E. et al. Nature 300, 762–765 (1982).
Yuasa, Y. et al. Nature 303, 775–779 (1983).
Santos, E., Reddy, E. P., Pulciani, S., Feldmann, R. J. & Barbacid, M. Proc. natn. Acad. Sci. U.S.A. 80, 4679–4683 (1983).
Shimizu, K. et al. Nature 304, 497–500 (1983).
McGrath, J. P. et al. Nature 304, 501–506 (1983).
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).
Fasano, O. et al. Proc. natn. Acad. Sci. U.S.A. 81, 4008–4012 (1984).
Van Dop, C., Tsubokawa, M., Bourne, H. R. & Ramachandran, J. J. biol. Chem. 259, 696–698 (1984).
Manning, D. R., Fraser, B. A., Kahn, R. A. & Gilman, A. G. J. biol. Chem. 259, 749–756 (1984).
Willumsen, B. M., Norris, K., Papageorge, A. G., Hubbert, N. L. & Lowy, D. R. EMBO J. 3, 2581–2585 (1984).
Chou, P. Y. & Fasman, G. D. A. Rev. Biochem. 47, 251–276 (1978).
Kyte, J. & Doolittle, R. F. J. molec. Biol. 157, 105–132 (1982).
Hurley, J. B., Simon, M. I., Teplow, D. B., Robishaw, J. D. & Gilman, A. G. Science 226, 860–862 (1984).
Reddy, V. B. et al. Science 200, 494–502 (1978).
Proudfoot, N. J. & Brownlee, G. G. Nature 263, 211–214 (1976).
Chirgwin, J. M., Przybyla, A. E., MacDonald, R. J. & Rutter, W. J. Biochemistry 18, 5294–5299 (1979).
Aviv, H. & Leder, P. Proc. natn. Acad. Sci. U.S.A. 69, 1408–1412 (1972).
Noda, M. et al. Nature 312, 121–127 (1984).
Köhler, G. & Milstein, C. Nature 256, 495–497 (1975).
Weinstock, R., Sweet, R., Weiss, M., Cedar, H. & Axel, R. Proc. natn. Acad. Sci. U.S.A. 75, 1299–1303 (1978).
Hewick, R. M., Hunkapiller, M. W., Hood, L. E. & Dreyer, W. J. J. biol. Chem. 256, 7990–7997 (1981).
Laemmli, U. K. Nature 227, 680–685 (1970).
Hunkapiller, M. W., Lujan, E., Ostrander, F. & Hood, L. E. Meth. Enzym. 91, 227–236 (1983).
McMaster, G. K. & Carmichael, G. G. Proc. natn. Acad. Sci. U.S.A. 74, 4835–4838 (1977).
Capon, D. J., Chen, E. Y., Levinson, A. D., Seeburg, P. H. & Goeddel, D. V. Nature 302, 33–37 (1983).
Dhar, R. et al. Science 217, 934–937 (1982).
Tsuchida, N., Ryder, T. & Ohtsubo, E. Science 217, 937–939 (1982).
Rasheed, S., Norman, G. L. & Heidecker, G. Science 221, 155–157 (1983).
Neuman-Silberberg, F. S., Schejter, E., Hoffmann, F. M. & Shilo, B-Z. Cell 37, 1027–1033 (1984).
DeFeo-Jones, D., Scolnick, E. M., Koller, R. & Dhar, R. Nature 306, 707–709 (1983).
Powers, S. et al. Cell 36, 607–612 (1984).
Gallwitz, D., Donath, C. & Sander, C. Nature 306, 704–707 (1983).
Dayhoff, M. O., Schwartz, R. M. & Orcutt, B. C. in Atlas of Protein Sequence and Structure Vol. 5, Suppl. 3 (ed. Dayhoff, M. O.) 345–352 (National Biomedical Research Foundation, Silver Spring, Maryland, 1978).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Tanabe, T., Nukada, T., Nishikawa, Y. et al. Primary structure of the α-subunit of transducin and its relationship to ras proteins. Nature 315, 242–245 (1985). https://doi.org/10.1038/315242a0
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1038/315242a0
This article is cited by
-
The intercalated cells of the mouse kidney OMCDis are the target of the vasopressin V1a receptor axis for urinary acidification
Clinical and Experimental Nephrology (2013)
-
Novel conserved synteny between human Chromosome 22 and cattle Chromosome 22 established by linkage mapping of transducin alpha-1 subunit (GNAZ)
Mammalian Genome (1997)
-
Coupling of bitter receptor to phosphodiesterase through transducin in taste receptor cells
Nature (1995)
-
Lipid modification at the N terminus of photoreceptor G-protein α-subunit
Nature (1992)
-
Gustducin is a taste-cell-specific G protein closely related to the transducins
Nature (1992)
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.