title: Inositol polyphosphate 5-phosphatase7 regulates the production of reactive oxygen species and salt tolerance in Arabidopsis.
abstract: Plants possess remarkable ability to adapt to adverse environmental conditions. The adaptation process involves the removal of many molecules from organelles, especially membranes, and replacing them with new ones. The process is mediated by an intracellular vesicle-trafficking system regulated by phosphatidylinositol (PtdIns) kinases and phosphatases. Although PtdIns comprise a fraction of membrane lipids, they function as major regulators of stress signaling. We analyzed the role of PtdIns 5-phosphatases (5PTases) in plant salt tolerance. The Arabidopsis (Arabidopsis thaliana) genome contains 15 At5PTases. We analyzed salt sensitivity in nine At5ptase mutants and identified one (At5ptase7) that showed increased sensitivity, which was improved by overexpression. At5ptase7 mutants demonstrated reduced production of reactive oxygen species (ROS). Supplementation of mutants with exogenous PtdIns dephosphorylated at the D5' position restored ROS production, while PtdIns(4,5)P(2), PtdIns(3,5)P(2), or PtdIns(3,4,5)P(3) were ineffective. Compromised salt tolerance was also observed in mutant NADPH Oxidase, in agreement with the low ROS production and salt sensitivity of PtdIns 3-kinase mutants and with the inhibition of NADPH oxidase activity in wild-type plants. Localization of green fluorescent protein-labeled At5PTase7 occurred in the plasma membrane and nucleus, places that coincided with ROS production. Analysis of salt-responsive gene expression showed that mutants failed to induce the RD29A and RD22 genes, which contain several ROS-dependent elements in their promoters. Inhibition of ROS production by diphenylene iodonium suppressed gene induction. In summary, our results show a nonredundant function of At5PTase7 in salt stress response by regulating ROS production and gene expression.
authors.affiliation: Department of Plant and Environmental Sciences, Hebrew University of Jerusalem, Givat-Ram Campus, Jerusalem 91904, Israel.
authors.forename: Yuval
authors.initials: Y
authors.lastname: Kaye
authors.forename: Yael
authors.initials: Y
authors.lastname: Golani
authors.forename: Yaniv
authors.initials: Y
authors.lastname: Singer
authors.forename: Yehoram
authors.initials: Y
authors.lastname: Leshem
authors.forename: Gil
authors.initials: G
authors.lastname: Cohen
authors.forename: Mustafa
authors.initials: M
authors.lastname: Ercetin
authors.forename: Glenda
authors.initials: G
authors.lastname: Gillaspy
authors.forename: Alex
authors.initials: A
authors.lastname: Levine
mesh_terms: D017360:Arabidopsis / Q000201:enzymology / Q000378:metabolism / Q000502:physiology*; D001483:Base Sequence; D017931:DNA Primers; D015971:Gene Expression Regulation, Enzymologic; D018506:Gene Expression Regulation, Plant; D000072181:Inositol Polyphosphate 5-Phosphatases; D009154:Mutation; D010744:Phosphoric Monoester Hydrolases / Q000235:genetics / Q000378:metabolism*; D017382:Reactive Oxygen Species / Q000378:metabolism*; D060888:Real-Time Polymerase Chain Reaction; D055051:Salt-Tolerant Plants / Q000378:metabolism / Q000502:physiology*; D013379:Substrate Specificity
chemical_list: D017931:DNA Primers; D017382:Reactive Oxygen Species; D010744:Phosphoric Monoester Hydrolases; D000072181:Inositol Polyphosphate 5-Phosphatases