Genes Coding for G Proteins in Mammalian and Yeast Cells

  • Y. Kaziro
Conference paper
Part of the 40. Colloquium der Gesellschaft für Biologische Chemie 6.– 8. April 1989 in Mosbach/Baden book series (MOSBACH, volume 40)

Abstract

GTP-binding proteins are classified largely into two groups, i.e., heterotrimeric GTP-binding proteins which are referred to as G proteins, and low-molecular-weight monomeric GTP-binding proteins (LMG) including ras, rap, rho, and rab proteins. The basic mechanism of the reaction catalyzed by these proteins appears to be analogous to that proposed for translational elongation factors (Kaziro 1978). The GTP-bound form is an active conformation which activates the transmission of signals, and the hydrolysis of bound GTP to GDP is required to shift the conformation to an inactive form, i.e., to shut off the signal transduction.

Keywords

Hydrolysis Carboxyl Retina Serine Polypeptide 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Barbacid, M. (1987) ras Genes. Annu. Rev. Biochem. 56: 779–827CrossRefGoogle Scholar
  2. Bray, P., Carter, A., Simons, C., Guo, V., Puckett, C., Kamholz, J., Spiegel, A., & Nirenberg, M. (1986) Human cDNA clones for four species of Gas signal transduction protein. Proc. Natl. Acad. Sci. USA 83: 8893–8897Google Scholar
  3. Broek, D., Samiy, N., Fasano, O., Fujiyama, A., Tamanoi, F., Northup, J., & Wigler, M. (1985) Differential activation of yeast adenylate cyclase by wild-type and mutant RAS proteins. Cell 41: 763–769PubMedCrossRefGoogle Scholar
  4. DeFeo-Jones, D., Scolnick, E.M., Koller, R., 33333 Dhar, R. (1983) ras-Related gene sequences identified and isolated from S. cerevisiae. Nature (London) 306:707–709 Google Scholar
  5. DeVos, A.M., Tong, L., Milburn. M.V., Matias, P.M., Jankark, J., Noguchi. S.. Nishimura, S., Miura, K., Ohtsuka, E., Kim. S.-H. (1988) Three-dimensional structure of an oncogene protein: catalytic domain of human c-H-ras p21. Science 239: 888–893CrossRefGoogle Scholar
  6. Dietzel, D. & Kurjan, J. (1987) The yeast SCG1 gene: a Ga-like protein implicated in the a-and a-factor response pathway. Cell 50: 1001–1010PubMedCrossRefGoogle Scholar
  7. Fong, H.K.W., Yoshimoto, K.K., Eversole-Cire, P., & Simon, M.I. (1988) Identification of a GTP-binding protein a subunit that lacks an apparent ADP-ribosylation site for pertussis toxin. Proc. Nati. Acad. Sci. USA 85: 3066–3070Google Scholar
  8. Fukui, Y. & Kaziro, Y. (1985) Molecular cloning and sequence analysis of a ras gene from Schizossacharomvices pombe. EM BO J. 4: 687–691Google Scholar
  9. Gilman, A.G. (1987) G proteins: transducers of receptor-generated signals. Annu. Rev. Biochem. 56: 615–649Google Scholar
  10. Hurley, J.B., Simon, M.I., Teplow, D.B., Robishaw, J.D., & Gilman, A.G. (1984) Homologies between signal transducing G proteins and ras gene products. Science 226: 860–862PubMedCrossRefGoogle Scholar
  11. Itoh, H., Kozasa, T., Nagata, S., Nakamura, S., Katada, T., Ui, M., Iwai, S., Ohtsuka, E., Kawasaki, H., Suzuki, K., & Kaziro, Y. (1986) Molecular cloning and sequence determination of cDNAs for a subunit of the guanine nucleotide-binding proteins Gs, Gi, and Go from rat brain. Proc. Natl. Acad. Sci. USA 83: 3776–3780Google Scholar
  12. Itoh, H., Toyama, R., Kozasa, T., Tsukamoto, T., Matsuoka, M., & Kaziro, Y. (1988) Presence of three distinct molecular species of Gi protein a subunit. J. Biol. Chem. 263: 6656–6664Google Scholar
  13. Jones, D.T. & Reed, R.R. (1987) Molecular cloning of five GTP-binding protein cDNA species from rat olfactory neuroepithelium. J. Biol. Chem. 262: 14241–14249Google Scholar
  14. Jurnak, F. (1985) Structure of the GDP domain of EF-Tu and location of the amino acids homologous to ras oncogene proteins. Science 230: 32–36PubMedCrossRefGoogle Scholar
  15. Kahn, R.A. & Gilman, A.G. (1984) ADP-ribosylation of Gs promoters and the dissociation of its a and ß subunits. J. Biol. Chem 259: 6235–6240Google Scholar
  16. Kaziro, Y. (1978) The role ofguanosine 5’-triphosphate in polypeptide chain elongation. Biochim. Biophys. Acta 505: 95–127Google Scholar
  17. Kaziro, Y., Itoh, H., Kozasa, T., Tsukamoto, T., Matsuoka, M., Nakafuku, M., Obara, T., Takagi, T., & Hernandez, R. (1988) Structure of the genes coding for G protein a subunits from mammalian and yeast cells. Cold Spring Harbor Symp. Quant. Biol. 53: 209–220Google Scholar
  18. Kozasa, T., Itoh, H., Tsukamoto, T., & Kaziro, Y. (1988) Isolation and characterization of human Gsa gene. Proc. Natl. Acad. Sci. USA 85: 2081–2085Google Scholar
  19. Lerea, C.L., Somers, D.E., Hurley, J.B., Klock, LB., & Bunt-Milam, A.H. (1986) Identification of specific transducin a subunits in retinal rod and cone photoreceptors. Science 324: 77–80CrossRefGoogle Scholar
  20. Masters, S.B., Stroud, R.M., & Bourne, H.R. (1986) Family of G protein a chains: amphipathic analysis and predicted structure of functional domains. Protein Eng. 1: 47–54.PubMedCrossRefGoogle Scholar
  21. Masters, S.B., Sullivan, K.A., Miller, R.T., Beiderman, B., Lopez, N.G., Ramachandran, J., & Bourne, H.R. (1988) Carboxyl terminal domain of Gsa specifies coupling of receptors to stimulation of adenylyl cyclase. Science 241: 448–451PubMedCrossRefGoogle Scholar
  22. Matsuoka, M., Itoh, H., Kozasa, T., & Kaziro, Y. (1988) Sequence analysis of cDNA and genomic DNA for a putative pertussis toxin-insensitive guanine nucleotide-binding regulatory protein a subunit. Proc. Natl. Acad. Sci. USA 85: 5384–5388Google Scholar
  23. Mattera, R., Codina, J., Crozat, A., Kidd, V., Woo. S.L.C., & Birnbaumer, L. (1986) Identification by molecular cloning of two forms of the a-subunit of the human liver stimulatory ( Gs) regulatory component of adenylate cyclase. FEBS Lett. 206: 36–41Google Scholar
  24. Miyajima, I., Nakafuku, M., Nakayama, N., Brenner, C., Miyajima, A., Kaibuchi, K., Arai, K., Kaziro. Y., & Matsumoto, K. (1987) Cell 50: 1011–1019Google Scholar
  25. Nakafuku, M., Itoh, H., Nakamura, S., & Kaziro, Y. (1987) Occurrence in Saccharomyces cerevisiae of a gene homologous to the cDNA coding for the a subunit of mammalian G proteins. Proc. Nati. Acad. Sci. USA 84: 2140–2144Google Scholar
  26. Nakafuku, M., Obara, T., Kaibuchi, K., Miyajima, I., Miyajima, A., Itoh, H., Nakamura, S., Arai, K., Matsumoto, K., & Kaziro, Y. (1988) Isolation of a second yeast Saccharomyces cerevisiae gene (GPA2) coding for guanine nucleotide-binding regulatory protein: studies on its structure and possible functions. Proc. Natl. Acad. Sci. USA 85: 1374–1378Google Scholar
  27. Northup, J.K., Sternweise, P.C., Smigel, M.D., Shleifer, L.S., Ross, E.M., and Gilman, A.G. (1980) Purification of the regulatory component of adenylate cyclase. Proc. Natl. Acad. Sci. USA 77: 6516–6520Google Scholar
  28. Powers, S., Kataoka, T., Fasano, O., Goldfarb, M., Strathern, J., Broach, J., & Wigler, M. (1984) Genes in S. cerevisiae encoding proteins with domains homologous to the mammalian ras proteins. Cell 36: 607–612PubMedCrossRefGoogle Scholar
  29. Robishaw, J.D., Russell, D.W., Harris, B.A., Smigel, M.D., & Gilman. A.G. (1986a) Deduced primary structure of the a subunit of the GTP-binding stimulatory protein of adenylate cyclase. Proc. Natl. Acad. Sci. USA 83: 1251–1255Google Scholar
  30. Robishaw, J.D., Smigel, M.D., & Gilman, A.G. (1986b) Molecular basis for two forms of the G protein that stimulates adenylate cyclase. J. Biol. Chem. 261: 9587–9590Google Scholar
  31. Sewell, J.L. & Kahn, R.A. (1988) Sequences of the bovine and yeast-ADP-ribosylation factor and comparison to other GTP-binding proteins. Proc. Natl. Acad. Sci. USA 85: 4620–4624Google Scholar
  32. Stryer, L. & Bourne, H.R. (1986) G proteins: a family of signal transducers. Annu. Rev. Cell Biol. 2:391 Sullivan, K.A., Miller, R.T., Masters, S.B., Beiderman, B.. Heideman, W., & Bourne, H.R. (1987) Identification of receptor contact site involved in receptor — G protein coupling. Nature (London) 330: 758–760Google Scholar
  33. Toda, T., Uno, I., Ishikawa, T., Powers, S., Kataoka, T., Broek, D., Cameron, S., Broach, J., Matsumoto, K.,& Wigler, M. (1985) In yeast, RA S proteins are controlling elements of adenylate cyclase. Celi 40: 27–36CrossRefGoogle Scholar
  34. Van Dop, C., Tsubokawa, M., Bourne, H.R., & Ramachandran, J. (1984) Amino acid sequences of retinal transducin at the site ADP-ribosylated by cholera toxin. J. Biol. Chem. 259: 696–698Google Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1989

Authors and Affiliations

  • Y. Kaziro
    • 1
  1. 1.Institute of Medical ScienceUniversity of TokyoMinato-ku, Tokyo 108Japan

Personalised recommendations