Skip to main content
Log in

The detection of fucose residues in plant nuclear envelopes

  • Published:
Planta Aims and scope Submit manuscript

Abstract

Protoplasts from suspension-culturedDaucus carota L. cells, when fixed and incubated with fluorescein conjugates of the fucosyl-specific lectinUlex europaeus agglutinin I, exhibited the following pattern of labeling: plasma membranes were not marked, but striking halos of fluorescence appeared around the periphery of all nucleic. Identical observations were made with protoplasts fromVicia faba L. leaves,Pisum sativum L. epicotyls,Zea mays L. roots andGlycine max L. cell suspensions, as well as with nucleic in cell-free preparations from the same sources. These results indicate that in a broad spectrum of angiosperm cells, fucose residues are associated with the nuclear envelope. The relationship of this finding in plant cells to recent discoveries regarding nuclear glycoconjugates in animal cells remains to be explored.

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

Con A:

Concanavalin A

PNA:

peanut agglutinin

UEA I:

Ulex europaeus agglutinin I

References

  • Banks, M.S., Evans, P.K. (1976) A comparison of the isolation and culture of mesophyll protoplasts from severalNicotiana species and their hybrids. Plant Sci. Lett.7, 409–416

    Google Scholar 

  • Chrispeels, M.J. (1984) Biosynthesis, processing and transport of storage proteins and lectins in cotyledons of developing legume seeds. Phil. Trans. R. Soc. London Ser. B304, 309–322

    Google Scholar 

  • Datta, N., Chen, Y.-R., Roux, S.J. (1985) Phytochrome and calcium stimulation of protein phosphorylation in isolated pea nucleic. Biochem. Biophys. Res. Commun.128, 1403–1408

    Google Scholar 

  • Davis, L.I., Blobel, G. (1986) Identification and characterization of a nuclear pore complex protein. Cell45, 699–709

    Google Scholar 

  • Davis, L.I., Blobel, G. (1987) Nuclear pore complex contains a family of glycoproteins that includes p62: glycosylation through a previously unidentified cellular pathway. Proc. Natl. Acad. Sci. USA84, 7552–7556

    Google Scholar 

  • Eriksson, T. (1965) Studies on the growth requirements and growth measurements of cell cultures ofHaplopappus gracilis. Physiol. Plant.18, 976–993

    Google Scholar 

  • Frederick, S.E., Nies, B., Gruber, P.J. (1981) An ultrastructural search for lectin-binding sites on surfaces of spinach leaf organelles. Planta152, 145–152

    Google Scholar 

  • Gamborg, O.L., Miller, R.A., Ojima, K. (1968) Nutrient requirements of suspension cultures of soybean root cells. Exp. Cell Res.50, 151–158

    Google Scholar 

  • Gregoire, M., Hernandez-Verdun, D., Bouteille, M. (1984) Visualization of chromatin distribution in living PTO cells by Hoechst 33342 fluorescent staining. Exp. Cell Res.152, 38–46

    Google Scholar 

  • Gronwald, J.W., Leonard, R.T. (1982) Isolation and transport properties of protoplasts from cortical cells of corn roots. Plant Physiol.70, 1391–1395

    Google Scholar 

  • Gruber, P.J. (1987) Lectins. In: Handbook of plant cytochemistry, vol. II, pp. 45–63, Vaughn, K.C., ed. CRC Press, Boca Raton, Fla., USA

    Google Scholar 

  • Gruber, P.J., Glimelius, K., Eriksson, T., Frederick, S.E. (1984) Interactions of galactose-binding lectins with plant protoplasts. Protoplasma121, 34–41

    Google Scholar 

  • Gruber, P.J., Sweeney, K.A., Frederick, S.E. (1985) Lectin binding by the nuclear envelope inDaucus carota protoplasts. (Abstr.) Plant Physiol.77, Suppl., 73

    Google Scholar 

  • Herman, E.M., Shannon, L.M., Chrispeels, M.J. (1986) The Golgi apparatus mediates the transport and post-translational modification of protein body proteins. In: Molecular biology of seed storage proteins and lectins, pp. 163–173, Shannon, L.M., Chrispeels, M.J., eds. American Society of Plant Physiologists, Rockville, Md., USA

    Google Scholar 

  • Holt, G.D., Snow, C.M., Senior, A., Haltiwanger, R.S., Gerace, L., Hart, G.W. (1987) Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine. J. Cell Biol.104, 1157–1164

    Google Scholar 

  • Hori, H., Elbein, A.D. (1983) Processing of N-linked oligosaccharides in soybean cultured cells. Arch. Biochem. Biophys.220, 415–425

    Google Scholar 

  • Kan, F.W.K., Pinto da Silva, P. (1986) Preferential association of glycoproteins to the euchromatin regions of cross-fractured nuclei is revealed by fracture-label. J. Cell Biol.102, 576–586

    Google Scholar 

  • Kornfeld, R., Kornfeld, S. (1985) Assembly of asparagine linked oligosaccharides. Annu. Rev. Biochem.54, 631–664

    Google Scholar 

  • Saxena, P.K., Fowke, L.C., King, J. (1985) An efficient procedure for isolation of nuclei from plant protoplasts. Protoplasma128, 184–189

    Google Scholar 

  • Snow, C.M., Senior, A., Gerace, L. (1987) Monoclonal antibodies identify a group of nuclear pore complex glycoproteins. J. Cell Biol.104, 1143–1156

    Google Scholar 

  • Sturm, A., Johnson, K.D., Szumilo, T., Elbein, A.D., Chrispeels, M.J. (1987) Subcellular localization of glycosidases and glycosyltransferases involved in the processing of N-linked oligosaccharides. Plant Physiol.85, 741–745

    Google Scholar 

  • Tallman, G., Reeck, G.R. (1980) Isolation of nucleic from plant protoplasts without the use of a detergent. Plant Sci. Lett.18, 271–275

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Gruber, P.J., Sweeney, K.A. & Frederick, S.E. The detection of fucose residues in plant nuclear envelopes. Planta 174, 298–304 (1988). https://doi.org/10.1007/BF00959513

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00959513

Key words

Navigation