Abstract
Current evidence suggests that ethylene signal transduction is mediated through protein phosphorylation . While ethylene has been shown to promote protein phosphorylation, incubation with cytokinin antagonises this effect in Triton X-100 solubilised membrane fractions from rosette leaves of Arabidopsis. In etr, protein phosphorylation is lower than wild type and is promoted by cytokinin. Protein phosphorylation in the mutant ctr is not only much higher than in wild type but is different in pattern. Ethylene treatment results in increased GTP binding to a monomeric G-protein in wild type membrane extracts. Constitutive GTP binding in etr is lower than in wild type. MAP kinase activity in cytosolic fractions is increased by ethylene and cytokinin antagonises this effect. In etr, MAP kinase activity is lower than in wild type but in ctr activity was enhanced. Hence, it is proposed that ethylene signal transduction, at least in part, involves small GTP-binding proteins in the mediation of a MAP kinase cascade.
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Smith, A.R., Moshkov, I.E., Novikova, G.V., Hall, M.A. (1999). The Effect of Ethylene and Cytokinin on GTP Binding and Map Kinase Activity in Arabidopsis thaliana . In: Kanellis, A.K., Chang, C., Klee, H., Bleecker, A.B., Pech, J.C., Grierson, D. (eds) Biology and Biotechnology of the Plant Hormone Ethylene II. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-4453-7_15
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DOI: https://doi.org/10.1007/978-94-011-4453-7_15
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