Using Yeast to Study Exchange of Macromolecules between the Cytoplasm and the Nucleus

  • P. Silver
Conference paper
Part of the NATO ASI Series book series (volume 71)

Abstract

Research over the past ten years has yielded information about the mechanism and some of the factors required for the specific uptake of certain proteins by the nucleus (see, for example, Garcia-Bustos et al., 1991; Silver, 1991; Stochaj and Silver, 1992 for recent review). Proteins move from their site of synthesis in the cytoplasm to the nuclear envelope. Specific targeting to the nucleus is accomplished in some cases by the presence of a short stretch of amino acids on the nuclear-destined proteins, termed an NLS for nuclear localization sequence. The NLS may mediate the interaction of the transported protein with cytoplasmic carriers or “receptors.” We know that proteins enter the nucleus via an aqueous channel formed by a complex of proteins in the nuclear envelope (termed the NPC for nuclear pore complex [Feldherr et al., 1984]). NLS-containing proteins may pass through the pore in association with the receptor or released from the receptor at the pore entry. The import process has been shown to require ATP in animal cells, Xenopus oocytes and yeast (Newmeyer and Forbes, 1988; Richardson et al., 1988; Breeuwer and Goldfarb, 1990; Garcia-Bustos et al., 1991).

Keywords

Zinc Migration Glycerol Lysine Polypeptide 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Bossie, M., DeHoratius, C., Barcelo, G., and Silver, P. (1992). A mutant nuclear protein with similarity to RNA binding proteins interferes with nuclear import in yeast. Molecular Biology of the Cell, In press.Google Scholar
  2. Breeuwer, M. and Goldfarb, D. (1990). Facilitated nuclear transport of histone H1 and other small nucleophilic proteins. Cell 60: 999–1008.PubMedCrossRefGoogle Scholar
  3. Davis, L. and Fink, G. R. (1990). The NUP1 gene encodes an essential component of the yeast nuclear pore complex. Cell 61: 965–978.PubMedCrossRefGoogle Scholar
  4. Dingwall, C., Sharnick, S.V., and Laskey, R.A. (1982). A polypeptide domain that specifies migration of nucleoplasmin into the nucleus. Cell 30: 449–458.PubMedCrossRefGoogle Scholar
  5. Dingwall, C. and Laskey, R.A. (1991). Nuclear targeting sequences-a consensus? Trends in Biochem. sci. 16: 478–481.CrossRefGoogle Scholar
  6. Feldherr, C., Kallenbach, E., and Schultz, N. (1984). Movement of a karyophillic protein through the nuclear pores of oocytes. J. Cell Biol. 99: 2216–2222.PubMedCrossRefGoogle Scholar
  7. Garcia-Bustos, J., Heitman, J., and Hall, M. (1991). Nuclear protein localization. Biochim. Biophys. Acta. 1071: 83–101.PubMedGoogle Scholar
  8. Goldfarb, D.S., Gariepy, J., Schoolnik, G. and Kornberg, R. (1986). Synthetic peptides as nuclear localization signals. Nature 322: 641–644.PubMedCrossRefGoogle Scholar
  9. Kalderon, D., Roberts, B.L., Richardson, W.D., and Smith, A.E. (1984). A short amino acid sequence able to specify nuclear location. Cell 39: 499–509.PubMedCrossRefGoogle Scholar
  10. Lanford, R.E. and Butel, J.S. (1984). Construction and characterization of an SV40 mutant defective in nuclear transport of T antigen. Cell 37: 801–813.PubMedCrossRefGoogle Scholar
  11. Lee, W.-C, Xue, Z., and Melese, T. (1991). The NSR1 gene encodes a protein that specifically binds nuclear localization sequences and has two RNA recognition motifs. J. Cell Biol. 113: 1–12.PubMedCrossRefGoogle Scholar
  12. Meier, U.T. and Blobel, G. (1990). A nuclear localization signal binding protein in the nucleolus. J. Cell Biol. 111: 2235–2245.PubMedCrossRefGoogle Scholar
  13. Nelson, M. and Silver, P. (1989). Context affects nuclear protein localization in Saccharomyces cerevisiae. Mol. Cell. Biol. 9: 384–389.PubMedGoogle Scholar
  14. Newmeyer, D.D. and Forbes, D. (1988). Nuclear import can be separated into distinct steps in vitro: nuclear pore binding and translocation. Cell 52: 641–653.PubMedCrossRefGoogle Scholar
  15. Richardson, W.D., Mills, A.D., Dilworth, S.M., Laskey, R.A. and Dingwall, C. (1988). Nuclear protein migration involves two steps: rapid binding at the nuclear envelope followed by slower translocation through nuclear pores. Cell 52: 655–664.PubMedCrossRefGoogle Scholar
  16. Rothblatt, J.A., Deshaies, R., Sanders, S., Dawn, G. and Schekman, R. (1989). Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeast. J. Cell Biol. 109: 2641–2652.PubMedCrossRefGoogle Scholar
  17. Sadler, I., Chiang, A., Kurihara, T., Rothblatt, J., Way, J. and Silver, P. (1989). A yeast gene important for assembly into the endoplasmic reticulum and the nucleus has homology to DnaJ, an E. coli heat shock protein. J. Cell Biol. 109: 2665–2675.Google Scholar
  18. Silver, P., Keegan, L., and Ptashne, M. (1984). Amino terminus of the yeast GAL4 gene product is sufficient for nuclear localization. Proc. Natl. Acad. sci. 81: 5951–5955.PubMedCrossRefGoogle Scholar
  19. Silver, P., Chiang, A. and Sadler, I. (1988). Mutations that alter both localization and production of a yeast nuclear protein. Genes Dev. 2: 707–717.PubMedCrossRefGoogle Scholar
  20. Silver, P., Sadler, I. and Osborne, M. (1989). Yeast proteins that recognize nuclear localization sequences. J. Cell Biol. 109: 983–989.PubMedCrossRefGoogle Scholar
  21. Silver, P. (1991). How proteins enter the nucleus. Cell 64: 489–497.PubMedCrossRefGoogle Scholar
  22. Stochaj, U. and Silver, P. (1992). Nucleocytoplasmic traffic of proteins. Eur. J. of Cell Biol., In press.Google Scholar
  23. Stochaj, U., Osborne, M., Kurihara, T., and Silver, P. (1991). A yeast protein that binds nuclear localization signals: Purification, localization, and antibody inhibition of activity. J. Cell Biol. 113: 1243–1254.PubMedCrossRefGoogle Scholar
  24. Stochaj, U. and Silver, P. (1992). A conserved phosphoprotein that specifically binds nuclear localization sequences is involved in nuclear import. J. Cell Biol. 117: 473–482.PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1993

Authors and Affiliations

  • P. Silver
    • 1
  1. 1.Department of Molecular BiologyPrinceton UniversityPrincetonUSA

Personalised recommendations