Skip to main content
Log in

Identification and localisation of a nucleoporin-like protein component of the plant nuclear matrix

  • Published:
Planta Aims and scope Submit manuscript

Abstract

Salt-detergent extraction of purified plant nuclei yields a fraction enriched in putative structural proteins known as the “nuclear matrix”. Compared with mammalian nuclear matrices, which contain three major proteins, plant nuclear matrices are complex, containing at least 100 polypeptides. In order to characterise more fully the plant nuclear matrix we have used antibodies raised against both yeast (Saccharomyces cerevisiae) and mammalian (rat) nuclear pore proteins. We have shown that the nuclear matrix of carrot (Daucus carota L.) contains at least one nucleoporin-like protein of about 100 kDa which is immunologically related to both the yeast nuclear pore protein NSP1 and mammalian nucleoporins (p62). Antibody labelling of a variety of plant cells at the light-microscope and electron-microscope levels confirms that this antigen is located at the nuclear pores. This, to our knowledge, is the first identification of a nuclear pore protein in plants.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

Abbreviations

IgG:

immunoglobulin G

kDa:

kilodaltons

DAPI:

4,6-diamidino-2-phenylindole

FITC:

fluorescein isothioganate

References

  • Akey, C.W., Goldfarb, D.S. (1989) Protein import through the nuclear pore complex is a multistep process. J. Cell Biol. 109, 971–982

    Google Scholar 

  • Aris, J.P., Blobel, G. (1989) Yeast nuclear envelope proteins cross react with an antibody against mammalian pore complex proteins. J. Cell Biol. 108, 2059–2067

    Google Scholar 

  • Baglia, F.A., Maul, G.G. (1983) Nuclear ribonucleoprotein release and nucleoside triphosphatase activity are inhibited by antibodies directed against one nuclear matrix glycoprotein. Proc. Natl. Acad. Sci. USA. 80, 2285–2289

    Google Scholar 

  • Benavente, R., Scheer, U., Chaly, N. (1989) Nucleocytoplasmic sorting of macromolecules following mitosis: fate of nuclear constituents after inhibition of pore complex function. Eur. J. Cell Biol. 50, 209–219

    Google Scholar 

  • Beven, A., Guan Y, Peart J., Cooper, C., Shaw, P. (1991) Monoclonal antibodies to plant nuclear matrix reveal intermediate filament-related components within the nucleus. J. Cell Sci. 98, 293–302

    Google Scholar 

  • Carmo-Fonseca, M., Kern, H., Hurt, E.C. (1991) Human nucleoporin p62 and the essential yeast nuclear pore protein NSP1 show sequence homology and a similar domain organization. Eur. J. Cell Biol. 55, 17–30

    Google Scholar 

  • Corben, E., Butcher, G., Hutchings, A., Wells, B., Roberts, K. (1989) A nucleolar matrix protein from carrot cells identified by a monoclonal antibody. Eur. J. Cell Biol. 50, 353–359

    Google Scholar 

  • Davis, L.I., Blobel, G. (1986) Identification and characterization of a nuclear pore complex protein. Cell 45, 699–709

    Google Scholar 

  • Davis, L.I., Fink, G.R. (1990) The NSP1 gene encodes an essential component of the yeast nuclear pore complex. Cell 61, 965–978

    Google Scholar 

  • Dingwall, C., Laskey, R.A. (1986) Protein import into the cell nucleus. Annu. Rev. Cell Biol. 2, 367–390

    Google Scholar 

  • Doonan, J.H., Clayton, L. (1986) Immunofluorescent studies on the plant cytoskeleton. In: Immunology in plant science (SEB Seminar Series) pp. 111–135, Wang, T., ed. Cambridge University Press, UK

    Google Scholar 

  • Dreyer, C., Stick, R., Hausen, P. (1986) Uptake of oocyte nuclear proteins by nuclei of xenopus embryos. In: Nucleoplasmic Transport, Workshop Heidelberg, FRG, pp. 143–158, Peters, R., Trendelenburg, M.F., eds. Springer-Verlag, New York

    Google Scholar 

  • Finlay, D.R., Forbes, D.J. (1990) Reconstitution of biochemically altered nuclear pores: Transport can be eliminated and restored. Cell 60, 17–29

    Google Scholar 

  • Finlay, D.R., Newmeyer, D.D., Price, T.M., Forbes, D.J. (1987) Inhibition of in vitro nuclear transport by a lectin that binds to nuclear pores. J. Cell Biol. 104, 189–200

    Google Scholar 

  • Fisher, P.A., Blobel, G. (1983) Preparation of a nuclear matrixpore complex-lamina fraction from embryos of Drosophila melanogaster. Methods Enzymol. 96, 589–596

    Google Scholar 

  • Gerace, L., Ottaviano, V., Kondor-Koch, C. (1982) Identification of a major polypeptide of the nulcear pore complex. J. Cell Biol. 95, 826–837

    Google Scholar 

  • Guiltinan, M.J., Schelling, M.E., Ehtesham, N.Z., Thomas, J.C., Christensen, M.E. (1988) The nucleolar RNA-binding protein B-36 is highly conserved among plants. Eur. J. Cell Biol. 46, 547–553

    Google Scholar 

  • Holt, G.D., Hart, G.W. (1986) The subcellular distribution of terminal N-acetylglucosamine moieties. J. Biol. Chem. 261, 8049–8057

    Google Scholar 

  • Hurt, E.C. (1988) A novel nucleoskeletal-like protein located at the nuclear periphery is required for the life cycle of Saccharomyces cerevisiae. EMBO J. 7, 4323–4334

    Google Scholar 

  • Hurt, C.H., McDowall, A., Schimmang, T. (1988) Nucleolar and nuclear envelope proteins of the yeast Saccharomyces cerevisiae. Eur. J. Cell Biol. 6, 554–563

    Google Scholar 

  • Jackson, D.A. (1991) Structure-function relationships in eukaryotic nuclei. BioEssays 13, 1–10

    Google Scholar 

  • La Cour, L.F., Wells, B. (1972) The nuclear pores of early meiotic prophase nuclei of plants. Z. Zellforsch, 123, 178–194

    Google Scholar 

  • La Cour, L.F., Wells, B. (1974) Nuclear pores at prophase of meiosis in plants. Philos. Trans. R. Soc. London, Ser. B. 268, 95–100

    Google Scholar 

  • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680–684

    PubMed  Google Scholar 

  • Nehrbass, U., Kern, H., Mutvei, A., Horstmann, H., Marshallsay, B., Hurt, E.C. (1990) NSP1: A yeast nuclear envelope protein localized at the nuclear pores exerts its essential function by its carboxy-terminal domain. Cell 61, 979–989

    Google Scholar 

  • Newport, J.W., Forbes, D.J. (1987) The nucleus: structure, function, and dynamics. Annu. Rev. Biochem. 56, 535–65

    Google Scholar 

  • Roberts, K., Northcote, D.H. (1971) Ultrastructure of the nuclear envelope; structural aspects of the interphase nucleus of sycamore suspension culture cells. Microsc. Acta 71, 102–120

    Google Scholar 

  • Silver, P.A. (1991) How proteins enter the nucleus. Cell 64, 489–497

    Google Scholar 

  • Starr, C.M., Hanover, J.A. (1990) Structure and function of the nuclear pore complex; new perspectives. BioEssays 12, 323–330

    Google Scholar 

  • Towbin, J., Staehelin, T., Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350–4354

    Google Scholar 

  • Vaughan, M.A. (1987) An autoimmune antibody from schleroderma patients recognizes a component of the plant cell nucleolus. Histochemistry 86, 533–535

    Google Scholar 

  • Wells, B. (1985) Low temperature box and tissue handling device for embedding biological tissue for immunostaining in electron microscopy. Micron. Microsc. Acta. 16, 49–53

    Google Scholar 

  • White, E.M., Allis, C.D., Goldfarb, D.S., Srivastva, A., Weir, J.W., Gorovsky, M.A. (1989) Nucleus-specific and temporally restricted localization of proteins in Tetrahymena macronuclei and micronuclei. J. Cell Biol. 109, 1983–1992

    Google Scholar 

  • Woffendin, C., Chambers, T.C., Schaller, K.L., Leichtling, B.H., Rickenberg, H.V. (1986) Translocation of cAMP-dependant protein kinase to the nucleus during development of Dictyostelium discoideum Dev. Biol. 115, 1–8

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Additional information

The authors would like to thank Dr. E. Hurt (European Molecular Biology Laboratory, Heidelberg, FRG) for antibodies against yeast nucleoporins, and Dr. L. Davis (Whitehead Institute for Biomedical Research, Cambridge, Mass., USA) for the monoclonal antibodies MAb 414 & 350. We thank Brian Wells for useful advice on electron microscopy. We also thank Peter Scott, Andrew Davis, and Nigel Hannant for photography, and Sue Bunnewell for development and printing of electronmicrographs.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Scofield, G.N., Beven, A.F., Shaw, P.J. et al. Identification and localisation of a nucleoporin-like protein component of the plant nuclear matrix. Planta 187, 414–420 (1992). https://doi.org/10.1007/BF00195666

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00195666

Key words

Navigation