Regulated inactivation of homologous gene expression in transgenic Nicotiana sylvestris plants containing a defense-related tobacco chitinase gene View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1992-11

AUTHORS

Craig M. Hart, Bernt Fischer, Jean-Marc Neuhaus, Frederick Meins

ABSTRACT

The class I chitinases are vacuolar proteins implicated in the defense of plants against pathogens. Leaves of transgenic Nicotiana sylvestris plants homozygous for a chimeric tobacco (Nicotiana tabacum) chitinase gene with Cauliflower Mosaic Virus (CaMV) 35S RNA expression signals usually accumulate high levels of chitinase relative to comparable leaves of non-transformed plants. Unexpectedly, some transgenic plants accumulated lower levels of chitinase than nontransformed plants. We call this phenomenon silencing. The incidence of silencing depends on the early rearing conditions of the plants. When grown to maturity in a greenhouse, ≈25% of plants raised as seedlings in closed culture vessels were of the silent type; none of the plants raised from seed in a greenhouse showed this phenotype. Silencing is also developmentally regulated. Plants showed three patterns of chitinase expression: uniformly high levels of expression in different leaves, uniformly low levels of expression in different leaves, and position-dependent silencing in which expression was uniform within individual leaves but varied in different leaves on the same plant. Heritability of the silent phenotype was examined in plants homozygous for the transgene. Some direct descendants exhibited a high-silent-high sequence of activity phenotypes in successive sexual generations, which cannot be explained by simple Mendelian inheritance. Taken together, the results indicate that silencing results from stable but potentially reversible states of gene expression that are not meiotically transmitted. Gene-specific measurements of chitinase and chitinase mRNA showed that silencing results from co-suppression, i.e. the inactivation of both host and transgene expression in trans. The silent state was not correlated with cytosine methylation of the transgene at the five restriction sites investigated. More... »

PAGES

179-188

References to SciGraph publications

  • 1990-03. Structure of a tobacco endochitinase gene: evidence that different chitinase genes can arise by transposition of sequences encoding a cysteine-rich domain in PLANT MOLECULAR BIOLOGY
  • 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
  • 1990-07. Epigenetic changes in the expression of the maize A1 gene inPetunia hybrida: Role of numbers of integrated gene copies and state of methylation in MOLECULAR GENETICS AND GENOMICS
  • 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
  • 1986-11-01. Plant chitinases are potent inhibitors of fungal growth in NATURE
  • 1991-08. Reversible inactivation of a transgene in Arabidopsis thaliana in MOLECULAR GENETICS AND GENOMICS
  • 1991-01. Gene structure and expression of a tobacco endochitinase gene in suspension-cultured tobacco cells in PLANT MOLECULAR BIOLOGY
  • 1990-12. Expression of a truncated tomato polygalacturonase gene inhibits expression of the endogenous gene in transgenic plants in MOLECULAR GENETICS AND GENOMICS
  • 1992-02. Endogenous and environmental factors influence 35S promoter methylation of a maize A1 gene construct in transgenic petunia and its colour phenotype in MOLECULAR GENETICS AND GENOMICS
  • 1985-06. Purification, immunoassay and characterization of an abundant, cytokinin-regulated polypeptide in cultured tobacco tissues in PLANTA
  • 1988-03. DNA methylation and tissue-specific transcription of the storage protein genes of maize in PLANT MOLECULAR BIOLOGY
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/bf00279359

    DOI

    http://dx.doi.org/10.1007/bf00279359

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1052403304

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/1281514


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