Skip to main content
SpringerLink
Log in

The ribosomal protein P0 of soybean (Glycine max L. Merr.) has antigenic cross-reactivity to soybean seed lectin

  • Published:
Plant Molecular Biology Aims and scope Submit manuscript

Abstract

Soybean (Glycine max L. Merr.) mutants lacking the ability to produce the lectin normally found in soybean seeds (SBL) are designated Le-. A protein of higher molecular weight that cross-reacts with antibodies raised to SBL was found at nearly equivalent levels in roots, hypocotyls, and leaves, and at lower levels in cotyledons and dry seeds of both Le+ and Le- soybean cultivars. Earlier work suggested that this protein was a novel lectin. Clones isolated from a Le- soybean root cDNA library produced a cross-reacting protein of the same size in Escherichia coli. Sequence analysis of these clones revealed a high degree of similarity to the ribosomal protein P0. The cross-reacting protein co-purified with ribosomes, and a monoclonal antibody raised to purified brine shrimp P0 cross-reacted to the same protein. The protein showed no lectin activity in a hemagglutination assay, nor did it bind to an N-acetyl-D-galactosamine affinity column. On the basis of this evidence, we conclude that the SBL-cross-reacting protein is not a lectin but a homologue of the ribosomal protein P0. Consequently, Le- soybeans must produce a lectin that is dissimilar to SBL at both the DNA and amino acid levels and we suggest that it is this lectin which is involved in nodulation.

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

Access this article

Log in via an institution

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

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. Altschul SF, Gish W, Miller W, Myers EW: Basic local alignment search tool. J Mol Biol 215: 403–410 (1990).

    Google Scholar 

  2. Arango R, Adar R, Rozenblatt S, Sharon N: Expression of Erythrina corallodendron lectin in Escherichia coli. Eur J Biochem 205: 575–581 (1992).

    Google Scholar 

  3. Bhuvaneswari TV, Turgeon BG, Bauer WD: Early events in the infection of soybean (Glycine max L. Merr) by Rhizobium japonicum. Plant Physiol 66: 1027–1031 (1980).

    Google Scholar 

  4. Bohlool BB, Schmidt EL: Lectins: a possible basis for specificity in the Rhizobium-legume root nodule symbiosis. Science 185: 269–271 (1974).

    Google Scholar 

  5. Bonner TI, Brenner DJ, Neufeld BR, Britten RJ: Reduction in the rate of DNA reassociation by sequence divergence. J Mol Biol 81: 123 (1973).

    Google Scholar 

  6. Dazzo FB, Hubbell DH: Cross-reactive antigens and lectins as determinants of symbiotic specificity in the Rhizobium-clover symbiosis. Appl Microb 30: 1017–1033 (1975).

    Google Scholar 

  7. Del Sal G, Manfioletti G, Schneider C: The CTAB-DNA precipitation method: a common mini-scale preparation of template DNA from phagemids, phages or plasmids suitable for sequencing. BioTechniques 7: 514–520 (1989).

    Google Scholar 

  8. Dellaporta SL, Wood J, Hicks JB: A plant DNA minipreparation: Version II. Plant Mol Biol Rep 1: 19–21 (1983).

    Google Scholar 

  9. Dénarié J, Debellé F and Promé J-C: Rhizobium lipochitooligosaccharide nodulation factors: signaling molecules mediating recognition andmorphogenesis. Annu Rev Biochem 65: 503–535 (1996).

    Google Scholar 

  10. Díaz CL, Melchers LS, Hooykaas PJJ, Lugtenberg BJJ, Kijne JW: Root lectin as a determinant of host-plant specificity in the Rhizobium-legume symbiosis. Nature 338: 579–581 (1989).

    Google Scholar 

  11. D'Sousa SE, Ginsberg MH, Plow EF: Arginyl-glycyl-aspartic acid (RGD): a cell adhesion motif. Trends Biochem Sci 16: 246–250 (1991).

    Google Scholar 

  12. Etzler ME and Murphy JB: Do legume vegetative tissue lectins play roles in plant-microbial interactions? In: Stacey G, Mullin B and Gresshoff PM (eds) Biology of Plant-Microbe Interactions, pp. 105–110. International Society of Molecular Plant-Microbe Interactions, St Paul, MN (1996).

    Google Scholar 

  13. Grade W, Jack MA, Dahl JB, Schmidt EL, Wold F: The isolation and characterization of a root lectin fromsoybean (Glycine max (L), cultivar Chippewa). J Biol Chem 256: 12905–12910 (1981).

    Google Scholar 

  14. Goldberg RB, Hoschek G, Vodkin LO: An insertion sequence blocks the expression of a soybean lectin gene. Cell 33: 465–475 (1983).

    Google Scholar 

  15. Halverson LJ, Stacey G: Host recognition in the Rhizobiumsoybean symbiosis: detection of a protein factor in soybean root exudate which is involved in the nodulation process. Plant Physiol 74: 84–89 (1984).

    Google Scholar 

  16. Halverson LJ, Stacey G: Host recognition in the Rhizobiumsoybean symbiosis: evidence for the involvement of lectin in nodulation. Plant Physiol 77: 621–625 (1985).

    Google Scholar 

  17. Halverson LJ, Stacey G: Effect of lectin on nodulation by wildtype Bradyrhizobium japonicum and a nodulation-defective mutant. Appl Envir Microbiol 51: 753–760 (1986).

    Google Scholar 

  18. Hamblin J, Kent SP: Possible role of phytohemagglutinin in Phaseolus vulgaris L. Nature New Biol 245: 28–29 (1973).

    Google Scholar 

  19. Hirsch AM: Developmental biology of legume nodulation. New Phytol 122: 211–237 (1992).

    Google Scholar 

  20. Jackson AO, Larkins BA: Influence of ionic strength, pH, and chelation of divalent metals on isolation of polyribosomes from tobacco leaves. Plant Physiol 57: 5–10 (1976).

    Google Scholar 

  21. Kijne J, Diaz C, de Pater S, Lugtenberg BJJ: Lectins in the symbiosis between Rhizobia and leguminous plants. In: Franz H (ed) Advances in Lectin Research, pp. 15–50. Ullstein Mosby, Berlin (1992).

    Google Scholar 

  22. Kjemtrup S, Borkhsenious O, Raikhel NV, Chrispeels M: Targeting and release of phytohemaglutinin from the roots of bean seedlings. Plant Physiol 109: 603–610 (1995).

    Google Scholar 

  23. Laemmli UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–685 (1970).

    Google Scholar 

  24. Lis H, Sela B-A, Sachs L, Sharon N: Specific inhibition by N-acetyl-D-galactosamine of the interaction between soybean agglutination and animal cell surfaces. Biochim Biophys Acta 211: 582–585 (1970).

    Google Scholar 

  25. Long SR: Rhizobium symbiosis: Nod factors in perspective. Plant Cell 8: 1885–1898 (1996).

    Google Scholar 

  26. Marston FAO: The purification of eukaryotic polypeptides expressed in Escherichia coli. In: Glover DM (ed) DNA Cloning: A Practical Approach, pp. 59. IRL Press, Oxford (1987).

    Google Scholar 

  27. Montesano L, Glitz DG: Wheat germ cytoplasmic ribosomes. J Biol Chem 263: 4932–4938 (1988).

    Google Scholar 

  28. Norris JH, Macol LA, Hirsch AM: Nodulin gene expression in effective nodules and in nodules arrested at three different stages of development. Plant Physiol 88: 321–328 (1988).

    Google Scholar 

  29. Okamuro JK, Jofuku KD, Goldberg RB: Soybean seed lectin gene and flanking nonseed protein genes are developmentally regulated in transformed tobacco plants. Proc Natl Acad Sci USA 83: 8240–8244 (1986).

    Google Scholar 

  30. Pull SP, Pueppke SG, Hymowitz T, Orf JH: Soybean lines lacking the 120 000-Dalton seed lectin. Science 200: 1177–1279 (1978).

    Google Scholar 

  31. Rutherford WM, Dick WE, Cavins JF, Dombrink-Kurtzman MA, Slodki ME: Isolation and characterization of a soybean lectin having 4-0-methylglucuronic acid specificity. Biochemistry 25: 952–958 (1986).

    Google Scholar 

  32. Sambrook J, Fritsch EF, Maniatis T: Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Press, Cold Spring Harbor, NY (1989).

    Google Scholar 

  33. Sanchez-Madrid F, Reyes R, Conde P, Ballesta JPG: Acidic ribosomal proteins from eukaryotic cells: effect on ribosomal functions. Eur J Biochem 98: 409–416 (1979).

    Google Scholar 

  34. Sanger F, Nicklen S, Coulsen AR: DNAsequencingwith chainterminating inhibitors. Proc Natl Acad Sci USA 74: 5463–5467 (1977).

    Google Scholar 

  35. Sengupta-Gopalan C, Pitas JW, Hall TC: Re-examination of the role of lectin in Rhizobium-Glycine symbiosis. In: Veeger C, Newton WE (eds) Advances in Nitrogen Fixation Research, p. 427. Nijhoff, The Hague (1984).

    Google Scholar 

  36. Spilatro SR, Anderson JM: Characterization of a soybean leaf protein that is related to the seed lectin and is increased with pod removal. Plant Physiol. 90: 1387–1393 (1989).

    Google Scholar 

  37. Spilatro SR, Cochran GR, Walker RE, Cablish KL, Bittner CC: Characterization of a new lectin of soybean vegetative tissues. Plant Physiol 110: 825–834 (1996).

    Google Scholar 

  38. Uchiumi T, Traut RR, Kominami R: Monoclonal antibodies against acidic phosphoproteins P0, P1, and P2 of eukaryotic ribosomes as functional probes. J Biol Chem 265: 89–95 (1990).

    Google Scholar 

  39. Uchiumi T, Wahba AJ, Trout RR: Topography and stoichiometry of acidic proteins in large ribosomal subunits from Artemia salina as determined by crosslinking. Proc Natl Acad Sci USA 84: 5580–5584 (1987).

    Google Scholar 

  40. van Eijsden RR, Díaz CL, Hoedemaeker PJ, de Pater BS, Kijne JW: Sugar binding activity of Pisum sativum lectin is essential for heterologous infection of transgenic white clover roots by Rhizobium leguminosarum bv. viciae. Plant Mol Biol 29: 431–439 (1995).

    Google Scholar 

  41. Vodkin LO: Isolation and characterization of messenger RNAs for seed lectin and Kunitz trypsin inhibitor in soybeans. Plant Physiol 68: 766–771 (1981).

    Google Scholar 

  42. Vodkin LO, Raikhel NV: Soybean lectin and related proteins in seeds and roots of Le+ and Le_soybean varieties. Plant Physiol 81: 558–565 (1986).

    Google Scholar 

  43. Yang F, Demma M, Warren V, Dharmawardhane S, Condeelis J: Identification of an actin-binding protein from Dictyostelium as elongation factor 1α. Nature 347: 494–496 (1990).

    Google Scholar 

  44. Zhu J-K, Damsz B, Kononowicz AK, Bressan RA, Hasegawa PM: A higher plant extracellular vitronectin-like adhesion protein is related to the translational elongation factor-1α. Plant Cell 6: 393–404 (1994).

    Google Scholar 

Download references

Author information

Author notes

  1. Keith L. Wycoff

    Present address: Planet Biotechnology, Inc., 2462 Wyandotte St., Mountain View, CA, 94043, USA

Authors and Affiliations

  1. Department of Molecular, Cell and Developmental Biology, USA

    Keith L. Wycoff, Pieternel van Rhijn & Ann M. Hirsch

  2. Molecular Biology Institute, University of California, Los Angeles, 405 Hilgard Ave., Los Angeles, CA, 90095-1606, USA

    Ann M. Hirsch

Authors
  1. Keith L. Wycoff
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Pieternel van Rhijn
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Ann M. Hirsch
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Wycoff, K.L., van Rhijn, P. & Hirsch, A.M. The ribosomal protein P0 of soybean (Glycine max L. Merr.) has antigenic cross-reactivity to soybean seed lectin. Plant Mol Biol 34, 295–306 (1997). https://doi.org/10.1023/A:1005817114562

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1005817114562

Search

Navigation