A role for ETR1 in hydrogen peroxide signaling in stomatal guard cells
A role for ETR1 in hydrogen peroxide signaling in stomatal guard cells
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DOI:
10.1104/pp.104.056994
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发表时间:
2005-03-01
期刊:
影响因子:
7.4
通讯作者:
Neill, SJ
中科院分区:
文献类型:
--
作者:
Desikan, R;Hancock, JT;Neill, SJ
Signaling through the redox active molecule hydrogen peroxide (H2O2) is important for several processes in plants, such as stomatal closure, root growth, gravitropism, and responses to pathogen challenge (Neill et al., 2002; Laloi et al., 2004). Although oxidative modification of reactive Cys residues within proteins has been suggested as a means by which H2O2 signaling can activate responses such as gene expression and reversible protein phosphorylation (Cooper et al., 2002; Danon, 2002), the linkage of H2O2 perception to intracellular signaling remains to be elucidated. Here, we report genetic and physiological data that demonstrate a previously uncharacterized function for the Arabidopsis (Arabidopsis thaliana) ethylene receptor ETR1, that of mediating H2O2 signaling in stomatal guard cells. Stomata in the loss-of-function etr1-7 mutant do not close in response to H2O2, and mutation of a Cys residue in the N-terminal region of ETR1 disrupts H2O2 signaling in both plants and in yeast (Saccharomyces cerevisiae).Large-scale analyses of H2O2-modulated gene expression in Arabidopsis and tobacco have shown that expression of genes encoding elements of both twocomponent signal transduction pathways and ethylene signaling are up-regulated by exogenous H2O2 (Desikan et al., 2001; Vandenabeele et al., 2003), suggesting that these phenomena may be linked. His kinases (HKs) are part of two-component systems that transduce environmental signals into cellular responses. Some of them are known to function as cytokinin and ethylene receptors in plants (Hwang et al., 2002). Hybrid HKs consist of an N-terminal signal input domain (with some having hydrophobic transmembrane regions, such as ETR1), a HK domain, and a C-terminal response regulator domain. During typical HK signaling, the HK domain is autophosphorylated on a His residue, with subsequent transfer of the phosphate group onto an Asp residue in the response