Advertisement

Considerations on the Mechanism of Nuclear Protein Localization in Yeast

  • M. N. Hall
Conference paper

Abstract

The past ten years have witnessed tremendous advances in an understanding of how proteins are selectively localized to organelles or the cell exterior (1–5). However, the mechanism by which specific proteins accumulate in the nucleus is relatively poorly understood (6). Until recently, the commonly accepted model for nuclear protein localization has been that all proteins freely diffuse into the nucleus with subsequent retention of nuclear proteins by binding to a non-diffusible substrate (e.g., DNA) (7). The general acceptance of this model is perhaps responsible for the tardiness of recent observations which indicate that nuclear localization may involve more than simple diffusion. A second model, for which evidence is now emerging, is that proteins are selectively translocated across the nuclear envelope. This second model is based on observations that nuclear proteins contain a determinant which identifies them as proteins destined to be taken into the nucleus (8–12). Here I briefly review one such observation.

Keywords

Nuclear Envelope Hybrid Protein Selective Retention Localization Determinant Nuclear Protein Localization 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Sabatini, DD, Kreibich, G, Morimoto, T, and Adesnik, M (1982) Mechanisms for the incorporation of proteins in membranes and organelles. J Cell Biol 92: 1–22.PubMedCrossRefGoogle Scholar
  2. 2.
    Schekman, R, and Novick, P (1982). The secretory process and yeast cell-surface assembly. In Strathern, JN, Jones, EW, and Broach, JR (eds): “The Molecular Biology of the Yeast Saccharomyces: Metabolism and Gene Expression” Cold Spring Harbor, New York: Cold Spring Harbor Laboratory, p 361–393.Google Scholar
  3. 3.
    Walter, P, Gilmore, R, and Blobel, G (1984). Translocation across the endoplamsic reticulum. Cell 38: 5–8.PubMedCrossRefGoogle Scholar
  4. 4.
    Benson, SA, Hall, MN, Silhavy, TJ (1985). Genetic analysis of protein export in Escherichia coli K12. Ann Rev Biochem 54: 101–134.PubMedCrossRefGoogle Scholar
  5. 5.
    Dunphy, WG, and Rothman JE (1985). Compartmental organization of the golgi stack. Cell 42: 13–21.PubMedCrossRefGoogle Scholar
  6. 6.
    De Robertis, EM (1983). Nucleocytoplasmic segregation of proteins and RNAs. Cell 32: 1021–1025.PubMedCrossRefGoogle Scholar
  7. 7.
    Bonner, WM (1978). Protein migration and accumulation in nuclei. In Busch, H (ed): “The Cell Nucleus” Vol 6 New York Academic Press, p 97–148.Google Scholar
  8. 8.
    Dingwall, C, Sharnick, SV, and Laskey, RA (1982). A polypeptide domain that specifies migration of nucleoplasmin into the nucleus. Cell 30: 449–458.PubMedCrossRefGoogle Scholar
  9. 9.
    Hall, MN, Hereford, L, and Herskowitz, I (1984). Targeting of E. coli B-galactosidase to the nucleus in yeast. Cell 36: 1057–1065.Google Scholar
  10. 10.
    Lanford, RE, and Butel, JS (1984). Construction and characterization of an SV4 0 mutant defective in nuclear transport of T antigen. Cell 37: 801–813.PubMedCrossRefGoogle Scholar
  11. 11.
    Kalderon, D, Richardson, WD, Markham, AF, and Smith, AE (1984). Sequence requirements for nuclear location of simian virus 40 large-T antigen. Nature 311: 33–38.PubMedCrossRefGoogle Scholar
  12. 12.
    Kalderon, D Roberts, BL, Richardson, WD, and Smith, AE (1984). A short amino acid sequence is able to specify nuclear location. Cell 39: 499–509.CrossRefGoogle Scholar
  13. 13.
    Johnson, AD, and Herskowitz, I (1985). A repressor (MATa2 product) and its operator control expression of a set of cell type specific genes in yeast. Cell 42: 237–247.PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag, Berlin Heidelberg 1986

Authors and Affiliations

  • M. N. Hall
    • 1
  1. 1.Department of Biochemistry and BiophysicsUniversity of CaliforniaSan FranciscoUSA

Personalised recommendations