Skip to main content
PMC home page
The Plant Cell logoLink to The Plant Cell
. 1993 Dec;5(12):1697–1710. doi: 10.1105/tpc.5.12.1697

Induction Patterns of an Extensin Gene in Tobacco upon Nematode Infection.

A Niebel 1, J De Almeida Engler 1, C Tire 1, G Engler 1, M Van Montagu 1, G Gheysen 1
PMCID: PMC160397  PMID: 12271052

Abstract

When sedentary endoparasitic nematodes infect plants, they induce complex feeding sites within the root tissues of their host. To characterize cell wall changes induced within these structures at a molecular level, we studied the expression of an extensin gene (coding for a major structural cell wall protein) in nematode-infected tobacco roots. Extensin gene expression was observed to be induced very early upon infection. This induction was weak, transient, and probably due to wounding during penetration and migration of the tobacco cyst nematode Globodera tabacum ssp solanacea-rum. In contrast, high extensin gene expression was observed during the whole second larval stage (an ~2-week-long phase of establishment of the feeding site) of the root knot nematode Meloidogyne javanica. During later stages of this interaction, expression gradually decreased. Extensin gene expression was found in at least three different tissues of the gall. We propose that distinct mechanisms lead to induced expression in these different cell types. The significance of these results for the understanding of plant-nematode interactions as well as the function of structural cell wall proteins, such as extensin, is discussed.

Full Text

The Full Text of this article is available as a PDF (4.7 MB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Angerer L. M., Angerer R. C. Detection of poly A+ RNA in sea urchin eggs and embryos by quantitative in situ hybridization. Nucleic Acids Res. 1981 Jun 25;9(12):2819–2840. doi: 10.1093/nar/9.12.2819. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Barker S. J., Harada J. J., Goldberg R. B. Cellular localization of soybean storage protein mRNA in transformed tobacco seeds. Proc Natl Acad Sci U S A. 1988 Jan;85(2):458–462. doi: 10.1073/pnas.85.2.458. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Block M. D., Botterman J., Vandewiele M., Dockx J., Thoen C., Gosselé V., Movva N. R., Thompson C., Montagu M. V., Leemans J. Engineering herbicide resistance in plants by expression of a detoxifying enzyme. EMBO J. 1987 Sep;6(9):2513–2518. doi: 10.1002/j.1460-2075.1987.tb02537.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Corbin D. R., Sauer N., Lamb C. J. Differential regulation of a hydroxyproline-rich glycoprotein gene family in wounded and infected plants. Mol Cell Biol. 1987 Dec;7(12):4337–4344. doi: 10.1128/mcb.7.12.4337. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Cox K. H., DeLeon D. V., Angerer L. M., Angerer R. C. Detection of mrnas in sea urchin embryos by in situ hybridization using asymmetric RNA probes. Dev Biol. 1984 Feb;101(2):485–502. doi: 10.1016/0012-1606(84)90162-3. [DOI] [PubMed] [Google Scholar]
  6. De Clercq A., Vandewiele M., De Rycke R., Van Damme J., Van Montagu M., Krebbers E., Vandekerckhove J. Expression and Processing of an Arabidopsis 2S Albumin in Transgenic Tobacco. Plant Physiol. 1990 Apr;92(4):899–907. doi: 10.1104/pp.92.4.899. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. De Loose M., Gheysen G., Tiré C., Gielen J., Villarroel R., Genetello C., Van Montagu M., Depicker A., Inzé D. The extensin signal peptide allows secretion of a heterologous protein from protoplasts. Gene. 1991 Mar 1;99(1):95–100. doi: 10.1016/0378-1119(91)90038-d. [DOI] [PubMed] [Google Scholar]
  8. Esquerré-Tugayé M. T., Lafitte C., Mazau D., Toppan A., Touzé A. Cell Surfaces in Plant-Microorganism Interactions: II. Evidence for the Accumulation of Hydroxyproline-rich Glycoproteins in the Cell Wall of Diseased Plants as a Defense Mechanism. Plant Physiol. 1979 Aug;64(2):320–326. doi: 10.1104/pp.64.2.320. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Evans I. M., Gatehouse L. N., Gatehouse J. A., Yarwood J. N., Boulter D., Croy R. R. The extensin gene family in oilseed rape (Brassica napus L.): characterisation of sequences of representative members of the family. Mol Gen Genet. 1990 Sep;223(2):273–287. doi: 10.1007/BF00265064. [DOI] [PubMed] [Google Scholar]
  10. Jefferson R. A., Kavanagh T. A., Bevan M. W. GUS fusions: beta-glucuronidase as a sensitive and versatile gene fusion marker in higher plants. EMBO J. 1987 Dec 20;6(13):3901–3907. doi: 10.1002/j.1460-2075.1987.tb02730.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Jones J. D., Dunsmuir P., Bedbrook J. High level expression of introduced chimaeric genes in regenerated transformed plants. EMBO J. 1985 Oct;4(10):2411–2418. doi: 10.1002/j.1460-2075.1985.tb03949.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Keller B., Lamb C. J. Specific expression of a novel cell wall hydroxyproline-rich glycoprotein gene in lateral root initiation. Genes Dev. 1989 Oct;3(10):1639–1646. doi: 10.1101/gad.3.10.1639. [DOI] [PubMed] [Google Scholar]
  13. Krebbers E., Herdies L., De Clercq A., Seurinck J., Leemans J., Van Damme J., Segura M., Gheysen G., Van Montagu M., Vandekerckhove J. Determination of the Processing Sites of an Arabidopsis 2S Albumin and Characterization of the Complete Gene Family. Plant Physiol. 1988 Aug;87(4):859–866. doi: 10.1104/pp.87.4.859. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Martineau B., Taylor W. C. Cell-specific photosynthetic gene expression in maize determined using cell separation techniques and hybridization in situ. Plant Physiol. 1986 Oct;82(2):613–618. doi: 10.1104/pp.82.2.613. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Mellon J. E., Helgeson J. P. Interaction of a hydroxyproline-rich glycoprotein from tobacco callus with potential pathogens. Plant Physiol. 1982 Aug;70(2):401–405. doi: 10.1104/pp.70.2.401. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Rumeau D., Maher E. A., Kelman A., Showalter A. M. Extensin and Phenylalanine Ammonia-Lyase Gene Expression Altered in Potato Tubers in Response to Wounding, Hypoxia, and Erwinia carotovora Infection. Plant Physiol. 1990 Jul;93(3):1134–1139. doi: 10.1104/pp.93.3.1134. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Showalter A. M., Bell J. N., Cramer C. L., Bailey J. A., Varner J. E., Lamb C. J. Accumulation of hydroxyproline-rich glycoprotein mRNAs in response to fungal elicitor and infection. Proc Natl Acad Sci U S A. 1985 Oct;82(19):6551–6555. doi: 10.1073/pnas.82.19.6551. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Showalter A. M. Structure and function of plant cell wall proteins. Plant Cell. 1993 Jan;5(1):9–23. doi: 10.1105/tpc.5.1.9. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Showalter A. M., Zhou J., Rumeau D., Worst S. G., Varner J. E. Tomato extensin and extensin-like cDNAs: structure and expression in response to wounding. Plant Mol Biol. 1991 Apr;16(4):547–565. doi: 10.1007/BF00023421. [DOI] [PubMed] [Google Scholar]
  20. Weiser R. L., Wallner S. J., Waddell J. W. Cell Wall and Extensin mRNA Changes during Cold Acclimation of Pea Seedlings. Plant Physiol. 1990 Jul;93(3):1021–1026. doi: 10.1104/pp.93.3.1021. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Ye Z. H., Varner J. E. Tissue-Specific Expression of Cell Wall Proteins in Developing Soybean Tissues. Plant Cell. 1991 Jan;3(1):23–37. doi: 10.1105/tpc.3.1.23. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from The Plant Cell are provided here courtesy of Oxford University Press

RESOURCES