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HERO ID
4302038
Reference Type
Journal Article
Title
Involvement of copper amine oxidase (CuAO)-dependent hydrogen peroxide synthesis in ethylene-induced stomatal closure in Vicia faba
Author(s)
Song, XG; She, XP; Yue, M; Liu, YE; Wang, YX; Zhu, X; Huang, AX
Year
2014
Is Peer Reviewed?
1
Journal
Russian Journal of Plant Physiology
ISSN:
1021-4437
EISSN:
1608-3407
Volume
61
Issue
3
Page Numbers
390-396
DOI
10.1134/S1021443714020150
Web of Science Id
WOS:000335144400015
Abstract
Ethylene promotes stomatal closure via inducing hydrogen peroxide (H2O2) generation. H2O2 can be catalytically synthesized by several enzymes in plants. Here, by means of stomatal bioassay, the analysis of enzyme activity and using laser-scanning confocal microscopy based on the H2O2-sensitive probe 2',7'-dichlorodihydrofluorescein diacetate (H2DCF-DA), the roles of copper amine oxidase (CuAO) in ethylene-induced H2O2 production in guard cells and stomatal closure in Vicia faba L. were investigated. 1-aminocyclopropane-1-carboxylic acid (ACC), an immediate precursor of ethylene synthesis, and ethylene gas significantly activated CuAO in intercellular washing fluid from leaves, the production of H2O2 in guard cells, and stomatal closure. These effects of ACC and ethylene gas were largely prevented by both aminoguanidine and 2-bromoethylamine, which are irreversible inhibitors of CuAO. Among major catalyzed and metabolized products of CuAO, only H2O2 could markedly promote stomatal closure and evidently reversed the effect of CuAO inhibitor on stomatal closure by ACC and ethylene gas. The data described above show that CuAO-mediated H2O2 production is involved in ethylene-induced stomatal closure.
Keywords
Vicia faba; copper amine oxidase; ethylene; hydrogen peroxide; stomatal closure
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