Abstract
Ethylene receptors from Arabidopsis contain domains with similarity to the two-component signal transduction systems originally identified in bacteria. The ETR1 ethylene receptor, for example, has both histidine kinase and response regulator domains. We are interested in how the two-component system has been adapted for signal transduction in eukaryotes and, more specifically, ethylene signal transduction in plants. In order to biochemically characterize the histidine kinase domain of ETR1, this portion of the protein was transgenically expressed in yeast. Auto-phosphorylation was observed upon incubation with radiolabeled ATP. Based on the acid/base stability of the phospho-amino acid and site-directed mutagenesis, ETR1 was demonstrated to contain histidine kinase activity. In addition to its enzymatic function, the histidine kinase domain of ETR1 bound CTR1, a Raf-like protein kinase that acts in the ethylene signal transduction pathway. This interaction occurred in ETR1 mutants that lacked residues required for histidine kinase activity. These data suggest that the histidine kinase domain of ETR1 performs both an enzymatic and a physical role in ethylene signal transduction.
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© 1999 Springer Science+Business Media Dordrecht
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Gamble, R.L., Coonfield, M.L., Randlett, M.D., Schaller, G.E. (1999). The Role of Two-Component Systems in Ethylene Perception. 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_12
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DOI: https://doi.org/10.1007/978-94-011-4453-7_12
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