The function of vacuolar β-1,3-glucanase investigated by antisense transformation. Susceptibility of transgenic Nicotiana sylvestris plants to Cercospora nicotianae infection View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1992-08

AUTHORS

Jean-Marc Neuhaus, Susan Flores, Dennis Keefe, Patricia Ahl-Goy, Frederick Meins

ABSTRACT

Vacuolar class I β-1,3-glucanases (EC 3.2.1.39) are believed to be important in the induced defense reaction of plants to fungal infection. We used antisense transformation to test this hypothesis and to identify other possible physiological functions of this enzyme. Nicotiana sylvestris plants were transformed with antisense constructions containing the region from position 27 to 608 of the coding sequence of the basic, vacuolar β-1,3-glucanase gene GLA of tobacco regulated by cauliflower mosaic virus 35S RNA expression signals. Plants homozygous for this transgene showed a marked, ca. 20-fold reduction in the constitutive expression of class I β-1,3-glucanase antigen in their leaves. RNA blot analysis indicated that the antisense plants expressed low levels of the sense transcript of the host β-1,3-glucanase gene and the antisense transcript of the transgene. Immune blot analysis of plant extracts indicated that only expression of the N. sylvestris homologue of class I tobacco β-1,3-glucanase and not the acidic, class II isoforms of the enzyme was blocked in the antisense plants. Class I isoforms of β-1,3-glucanase and chitinase were coordinately induced in leaves of untransformed and empty-vector-transformed N. sylvestris plants treated with ethylene or infected with the fungal leaf pathogen Cercospora nicotianae. In antisense plants, chitinase but not β-1,3-glucanase was induced under these conditions indicating that antisense transformation effectively blocks constitutive as well as induced expression of class I β-1,3-glucanase. Under greenhouse conditions, antisense plants developed normally and were fertile. The plants did not exhibit increased susceptibility to C. nicotianae infection. These results suggest that expression of the β-1,3-glucanase isoform blocked by antisense transformation is not necessary for ‘house-keeping’ functions of N. sylvestris nor defense against the fungal pathogen tested. More... »

PAGES

803-813

References to SciGraph publications

  • 1990-12. Evidence for a third structural class of β-1,3-glucanase in tobacco in PLANT MOLECULAR BIOLOGY
  • 1981-02. (1→3)-β-D-Glucan (callose) is a probable intermediate in biosynthesis of cellulose of cotton fibres in NATURE
  • 1987-11. Ethylene regulation of β-1,3-glucanase in tobacco in PLANTA
  • 1983-08. Evidence for an abundant 33,000-dalton polypeptide regulated by cytokinins in cultured tobacco tissues in PLANTA
  • 1986-02. Developmental and hormonal regulation of β-1,3-glucanase in tobacco in PLANTA
  • 1991-01. High-level expression of a tobacco chitinase gene in Nicotiana sylvestris. Susceptibility of transgenic plants to Cercospora nicotianae infection in PLANT MOLECULAR BIOLOGY
  • 1969-12. Cell-wall-hydrolysing enzymes in wall formation as measured by pollen-tube extension in PLANTA
  • 1969-10. Timing of callase activity and cytoplasmic male sterility in Petunia in BIOCHEMICAL GENETICS
  • 1971-01. Mechanism of male sterility in Petunia: The relationship between pH, callase activity in the anthers, and the breakdown of the microsporogenesis in THEORETICAL AND APPLIED GENETICS
  • 1983-05. A binary plant vector strategy based on separation of vir- and T-region of the Agrobacterium tumefaciens Ti-plasmid in NATURE
  • 1981. Fungal Cell Walls: A Survey in PLANT CARBOHYDRATES II
  • 1970-08. Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 in NATURE
  • 1985-06. Purification, immunoassay and characterization of an abundant, cytokinin-regulated polypeptide in cultured tobacco tissues in PLANTA
  • 1990-08. The effect of ethylene on the cell-type-specific and intracellular localization of β-1,3-glucanase and chitinase in tobacco leaves in PLANTA
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    URI

    http://scigraph.springernature.com/pub.10.1007/bf00027076

    DOI

    http://dx.doi.org/10.1007/bf00027076

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1023349659

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/1643283


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    86 levels
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    90 physiological functions
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    93 position 27
    94 possible physiological function
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    97 region
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