Signaling Events Leading to Red-Light-Induced Suppression of Photomorphogenesis in Wheat (Triticum aestivum)

  • Gupta, Varsha
  • Roy, Ansuman
  • Tripathy, Baishnab C.
Plant and Cell Physiology 51(10):p 1788-1799, October 2010. | DOI: 10.1093/pcp/pcq139

Perception of red light (400 μmol photon m2/s) by the shoot bottom turned off the greening process in wheat. To understand the signaling cascade leading to this photomorphogenic response, certain signaling components were probed in seedlings grown in different light regimes. Upon analysis the gene expression of heterotrimeric and were severely down-regulated in seedlings grown without vermiculite and having their shoot bottom exposed to red light (R/V−) and was similar to that of dark-grown seedlings. Supplementing the red-light-grown V− seedlings with blue light resulted in up-regulation of both and expression, suggesting that blue light is able to modulate G protein expression. Treatment of cytokinin analog benzyladenine to cytokinin-deficient red-light-grown R/V− seedlings resulted in up-regulation of gene expression of both and . To probe further, modulators of signal transduction pathway—AlF3 (G protein activator), LaCl3 (Ca2+ channel blocker), NaF (nonspecific phosphatase inhibitor), or calmodulin (CaM) antagonists trifluoperazine (TFP) and N-(6-aminohexyl)-5-chloro-1-nafthalene-sulfonamide (W-7)—were added along with Hoagland solution to the roots of 4-day-old etiolated seedlings, grown on germination paper and transferred to red light. AlF3, LaCl3, NaF failed to elicit any photomorphogenic response. However, CaM antagonists TFP and W-7 significantly reversed the red-light-induced suppression of photomorphogenesis. Phosphorylation of proteins assayed in the absence or presence of CaM antagonist TFP revealed respective up-regulation or down-regulation of phosphorylation of several plastidic proteins in R/V− seedlings. These suggest that signal transduction of red light perceived by the shoot bottom to suppress photomorphogenesis is mediated by CaM-dependent protein kinases.

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