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okadaic acid/nicotiana

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Phosphoproteins involved in the signal transduction of cryptogein, an elicitor of defense reactions in tobacco.

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We previously reported that the signal transduction of cryptogein, an elicitor of defense reactions in Nicotiana tabacum cells, involves upstream protein phosphorylation. In the present study, induction of these early physiological events was further investigated with inhibitors of protein

Inhibitors of Protein Phosphatases 1 and 2A Block the Sugar-Inducible Gene Expression in Plants.

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Genes coding for two major proteins of the tuberous root of sweet potato (Ipomoea batatas), namely, sporamin and [beta]-amylase, are inducible in leaves and petioles when they are supplied with high concentrations of sucrose or other metabolizable sugars, such as glucose and fructose, and the

Serine/threonine protein phosphatase is required for tobacco mosaic virus-mediated programmed cell death.

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A major gap in our understanding of host response to virus infection is how the molecular signals are passed within infected cells. Tobacco mosaic virus-mediated programmed cell death in genotype NN tobaccos was used to evaluate the hypothesis that these molecular signals are transduced via
Oligogalacturonide-induced modifications of protein phosphorylation in cells of Nicotiana tabacum L. were investigated by in-vitro phosphorylation of plasma-membrane-enriched fractions and electrophoretic analysis on two-dimensional gels. About 100 polypeptides were resolved; among these 40

Cytokinins and auxins control the expression of a gene in Nicotiana plumbaginifolia cells by feedback regulation.

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Both cytokinin (N6-benzyladenine [BA]) and auxin (2,4-dichlorophenoxyacetic acid [2,4-D]) stimulate the accumulation of an mRNA, represented by the cDNA pLS216, in Nicotiana plumbaginifolia suspension culture cells. The kinetics of RNA accumulation were different for the two hormones; however, the
The recently synthesized isocyanonaphtalene derivatives ACAIN and CACAIN are fluorochromes excitable at wavelengths of around 366 nm and bind cysteine-rich proteins with hydrophobic motifs. We show that these compounds preferentially label tonoplasts in living Arabidopsis and tobacco (Nicotiana
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