Expression of the gene for a small GTP binding protein in transgenic tobacco elevates endogenous cytokinin levels, abnormally induces salicylic acid in response to wounding, and increases resistance to tobacco mosaic virus infection
- PMID: 11607497
- PMCID: PMC45060
- DOI: 10.1073/pnas.91.22.10556
Expression of the gene for a small GTP binding protein in transgenic tobacco elevates endogenous cytokinin levels, abnormally induces salicylic acid in response to wounding, and increases resistance to tobacco mosaic virus infection
Abstract
Tobacco plants transformed with rgp1, a gene encoding a Ras-related small GTP binding protein, were previously shown to exhibit a distinct reduction in apical dominance with increased tillering. These abnormal pheno-types were later found to be associated with elevated levels of endogenous cytokinins (zeatin and zeatin riboside). Analysis of the expression of several genes known to be affected by cytokinins identified a clear increase in the mRNA levels of genes encoding acidic pathogenesis-related proteins in both transgenic plants and their progenies. This increase was directly attributable to elevated levels of the acidic pathogenesis-related protein inducers, salicylic acid (SA) and salicylic acid beta-glucoside, due to an abnormal and sensitive response of the transgenic plants to wounding. In contrast, mRNA levels of the gene for proteinase inhibitor II, which is normally induced by wounding, were generally suppressed in the same wounded plants, probably due to SA overproduction. The changes in SA and pathogenesis-related protein levels in the transgenic plants resulted in a distinct increase in their resistance to tobacco mosaic virus infection. In normal plants, the wound and pathogen-induced signal transduction pathways are considered to function independently. However, the wound induction of SA in the transgenic plants suggests that overexpression of this small GTP binding protein somehow interferes with the normal signal pathways, possibly by affecting cytokinin biosynthesis, and results in cross-signaling between these two transduction systems.
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