The coronatine-insensitive 1 mutation reveals the hormonal signaling interaction between abscisic acid and methyl jasmonate in Arabidopsis guard cells. Specific impairment of ion channel activation and second messenger production.
Methyl jasmonate (MeJA) elicits stomatal closing similar to abscisic acid (ABA), but whether the two compounds use similar or different signaling mechanisms in guard cells remains to be clarified. We investigated the effects of MeJA and ABA on second messenger production and ion channel activation in guard cells of wild-type Arabidopsis (Arabidopsis thaliana) and MeJA-insensitive coronatine-insensitive 1 (coi1) mutants. The coi1 mutation impaired MeJA-induced stomatal closing but not ABA-induced stomatal closing. MeJA as well as ABA induced production of reactive oxygen species (ROS) and nitric oxide (NO) in wild-type guard cells, whereas MeJA did not induce production of ROS and NO in coi1 guard cells. The experiments using an inhibitor and scavengers demonstrated that both ROS and NO are involved in MeJA-induced stomatal closing as well as ABA-induced stomatal closing. Not only ABA but also MeJA activated slow anion channels and Ca(2+) permeable cation channels in the plasma membrane of wild-type guard cell protoplasts. However, in coi1 guard cell protoplasts, MeJA did not elicit either slow anion currents or Ca(2+) permeable cation currents, but ABA activated both types of ion channels. Furthermore, to elucidate signaling interaction between ABA and MeJA in guard cells, we examined MeJA signaling in ABA-insensitive mutant ABA-insensitive 2 (abi2-1), whose ABA signal transduction cascade has some disruption downstream of ROS production and NO production. MeJA also did not induce stomatal closing but stimulated production of ROS and NO in abi2-1. These results suggest that MeJA triggers stomatal closing via a receptor distinct from the ABA receptor and that the coi1 mutation disrupts MeJA signaling upstream of the blanch point of ABA signaling and MeJA signaling in Arabidopsis guard cells.
Munemasa
Shintaro
S
Graduate School of Natural Science and Technology, Okayama University, Tsushima-Naka, Okayama 700-8530, Japan.
Oda
Kenji
K
Watanabe-Sugimoto
Megumi
M
Nakamura
Yoshimasa
Y
Shimoishi
Yasuaki
Y
Murata
Yoshiyuki
Y
D000040:Abscisic Acid / Q000378:metabolism* / Q000494:pharmacology; D000085:Acetates / Q000378:metabolism* / Q000494:pharmacology; D017360:Arabidopsis / Q000166:cytology / Q000235:genetics / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D002118:Calcium / Q000378:metabolism; D003517:Cyclopentanes / Q000378:metabolism* / Q000494:pharmacology; D007473:Ion Channels / Q000378:metabolism*; D009154:Mutation; D009569:Nitric Oxide / Q000378:metabolism; D054883:Oxylipins; D010749:Phosphoprotein Phosphatases / Q000235:genetics; D017382:Reactive Oxygen Species / Q000378:metabolism; D015398:Signal Transduction
D000085:Acetates; D029681:Arabidopsis Proteins; C112279:COI1 protein, Arabidopsis; D003517:Cyclopentanes; D007473:Ion Channels; D054883:Oxylipins; D017382:Reactive Oxygen Species; D009569:Nitric Oxide; D000040:Abscisic Acid; C072239:methyl jasmonate; C106443:ABI2 protein, Arabidopsis; D010749:Phosphoprotein Phosphatases; D002118:Calcium