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. 1990 Dec;2(12):1131–1143. doi: 10.1105/tpc.2.12.1131

Tissue-specific and pathogen-induced regulation of a Nicotiana plumbaginifolia beta-1,3-glucanase gene.

C Castresana 1, F de Carvalho 1, G Gheysen 1, M Habets 1, D Inzé 1, M Van Montagu 1
PMCID: PMC159961  PMID: 2152158

Abstract

The Nicotiana plumbaginifolia gn1 gene encoding a beta-1,3-glucanase isoform has been characterized. The gn1 product represents an isoform distinct from the previously identified tobacco beta-1,3-glucanases. By expressing gn1 in Escherichia coli, we have determined directly that the encoded protein does, indeed, correspond to a beta-1,3-glucanase. In N. plumbaginifolia, gn1 was found to be expressed in roots and older leaves. Transgenic tobacco plants containing the 5'-noncoding region of gn1 fused to the beta-glucuronidase (GUS) reporter gene also showed maximum levels of GUS activity in roots and older leaves. No detectable activity was present in the upper part of the transgenic plants with the exception of stem cells at the bases of emerging shoots. The expression conferred by the gn1 promoter was differentially induced in response to specific plant stress treatments. Studies of three plant-bacteria interactions showed high levels of GUS activity when infection resulted in a hypersensitive reaction. Increased gene expression was confined to cells surrounding the necrotic lesions. The observed expression pattern suggests that the characterized beta-1,3-glucanase plays a role both in plant development and in the defense response against pathogen infection.

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Selected References

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  1. Boller T., Vögeli U. Vacuolar localization of ethylene-induced chitinase in bean leaves. Plant Physiol. 1984 Feb;74(2):442–444. doi: 10.1104/pp.74.2.442. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  3. Broglie K. E., Gaynor J. J., Broglie R. M. Ethylene-regulated gene expression: molecular cloning of the genes encoding an endochitinase from Phaseolus vulgaris. Proc Natl Acad Sci U S A. 1986 Sep;83(18):6820–6824. doi: 10.1073/pnas.83.18.6820. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bulcke M. V., Bauw G., Castresana C., Van Montagu M., Vandekerckhove J. Characterization of vacuolar and extracellular beta(1,3)-glucanases of tobacco: Evidence for a strictly compartmentalized plant defense system. Proc Natl Acad Sci U S A. 1989 Apr;86(8):2673–2677. doi: 10.1073/pnas.86.8.2673. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. De Loose M., Alliotte T., Gheysen G., Genetello C., Gielen J., Soetaert P., Van Montagu M., Inzé D. Primary structure of a hormonally regulated beta-glucanase of Nicotiana plumbaginifolia. Gene. 1988 Oct 15;70(1):13–23. doi: 10.1016/0378-1119(88)90100-x. [DOI] [PubMed] [Google Scholar]
  6. Deblaere R., Bytebier B., De Greve H., Deboeck F., Schell J., Van Montagu M., Leemans J. Efficient octopine Ti plasmid-derived vectors for Agrobacterium-mediated gene transfer to plants. Nucleic Acids Res. 1985 Jul 11;13(13):4777–4788. doi: 10.1093/nar/13.13.4777. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. 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]
  8. 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]
  9. Joosten M. H., De Wit P. J. Identification of Several Pathogenesis-Related Proteins in Tomato Leaves Inoculated with Cladosporium fulvum (syn. Fulvia fulva) as 1,3-beta-Glucanases and Chitinases. Plant Physiol. 1989 Mar;89(3):945–951. doi: 10.1104/pp.89.3.945. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Keen N. T., Yoshikawa M. beta-1,3-Endoglucanase from Soybean Releases Elicitor-Active Carbohydrates from Fungus Cell Walls. Plant Physiol. 1983 Mar;71(3):460–465. doi: 10.1104/pp.71.3.460. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Keil M., Sánchez-Serrano J. J., Willmitzer L. Both wound-inducible and tuber-specific expression are mediated by the promoter of a single member of the potato proteinase inhibitor II gene family. EMBO J. 1989 May;8(5):1323–1330. doi: 10.1002/j.1460-2075.1989.tb03512.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Keller B., Schmid J., Lamb C. J. Vascular expression of a bean cell wall glycine-rich protein-beta-glucuronidase gene fusion in transgenic tobacco. EMBO J. 1989 May;8(5):1309–1314. doi: 10.1002/j.1460-2075.1989.tb03510.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Kombrink E., Schröder M., Hahlbrock K. Several "pathogenesis-related" proteins in potato are 1,3-beta-glucanases and chitinases. Proc Natl Acad Sci U S A. 1988 Feb;85(3):782–786. doi: 10.1073/pnas.85.3.782. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Langridge W. H., Fitzgerald K. J., Koncz C., Schell J., Szalay A. A. Dual promoter of Agrobacterium tumefaciens mannopine synthase genes is regulated by plant growth hormones. Proc Natl Acad Sci U S A. 1989 May;86(9):3219–3223. doi: 10.1073/pnas.86.9.3219. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Lotan T., Ori N., Fluhr R. Pathogenesis-related proteins are developmentally regulated in tobacco flowers. Plant Cell. 1989 Sep;1(9):881–887. doi: 10.1105/tpc.1.9.881. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Mauch F., Hadwiger L. A., Boller T. Antifungal Hydrolases in Pea Tissue : I. Purification and Characterization of Two Chitinases and Two beta-1,3-Glucanases Differentially Regulated during Development and in Response to Fungal Infection. Plant Physiol. 1988 Jun;87(2):325–333. doi: 10.1104/pp.87.2.325. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Mauch F., Staehelin L. A. Functional Implications of the Subcellular Localization of Ethylene-Induced Chitinase and [beta]-1,3-Glucanase in Bean Leaves. Plant Cell. 1989 Apr;1(4):447–457. doi: 10.1105/tpc.1.4.447. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Memelink J., Hoge J. H., Schilperoort R. A. Cytokinin stress changes the developmental regulation of several defence-related genes in tobacco. EMBO J. 1987 Dec 1;6(12):3579–3583. doi: 10.1002/j.1460-2075.1987.tb02688.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Memelink J., Linthorst H. J., Schilperoort R. A., Hoge J. H. Tobacco genes encoding acidic and basic isoforms of pathogenesis-related proteins display different expression patterns. Plant Mol Biol. 1990 Feb;14(2):119–126. doi: 10.1007/BF00018553. [DOI] [PubMed] [Google Scholar]
  20. Mohnen D., Shinshi H., Felix G., Meins F. Hormonal regulation of beta1,3-glucanase messenger RNA levels in cultured tobacco tissues. EMBO J. 1985 Jul;4(7):1631–1635. doi: 10.1002/j.1460-2075.1985.tb03830.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Ohshima M., Itoh H., Matsuoka M., Murakami T., Ohashi Y. Analysis of stress-induced or salicylic acid-induced expression of the pathogenesis-related 1a protein gene in transgenic tobacco. Plant Cell. 1990 Feb;2(2):95–106. doi: 10.1105/tpc.2.2.95. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Peleman J., Boerjan W., Engler G., Seurinck J., Botterman J., Alliotte T., Van Montagu M., Inzé D. Strong cellular preference in the expression of a housekeeping gene of Arabidopsis thaliana encoding S-adenosylmethionine synthetase. Plant Cell. 1989 Jan;1(1):81–93. doi: 10.1105/tpc.1.1.81. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Rigden J., Coutts R. Pathogenesis-related proteins in plants. Trends Genet. 1988 Apr;4(4):87–89. doi: 10.1016/0168-9525(88)90091-1. [DOI] [PubMed] [Google Scholar]
  24. Shinshi H., Mohnen D., Meins F. Regulation of a plant pathogenesis-related enzyme: Inhibition of chitinase and chitinase mRNA accumulation in cultured tobacco tissues by auxin and cytokinin. Proc Natl Acad Sci U S A. 1987 Jan;84(1):89–93. doi: 10.1073/pnas.84.1.89. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Van de Rhee M. D., Van Kan J. A., González-Jaén M. T., Bol J. F. Analysis of regulatory elements involved in the induction of two tobacco genes by salicylate treatment and virus infection. Plant Cell. 1990 Apr;2(4):357–366. doi: 10.1105/tpc.2.4.357. [DOI] [PMC free article] [PubMed] [Google Scholar]

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