Induction of Stomatal Closure by Vanadate or a Light/Dark Transition Involves Ca2+-Calmodulin-Dependent Protein Phosphorylations.
Previous studies indicate that a continual source of adenosine 5[prime]-triphosphate is required for both opening and closing of stomata. However, vanadate (Na3VO4 at 500 [mu]M) as well as a light/dark transition induced stomatal closing in epidermal peels of Commelina communis L., showing that the stoppage or even the decrease of the activity of the plasma membrane H+-adenosine 5[prime]-triphosphatase is sufficient to induce stomatal closure. Furthermore, stomatal closing in response to Na3VO4 or a light/dark transition was suppressed by inhibitors of metabolism (10 [mu]M carbonyl cyanide m-chlorophenylhydrazone) and of protein kinases (20 [mu]M 1-[5-iodonaphthalene-1-sulfonyl]-1H-hexa-hydro-1,4-diaz-epine), calmodulin antagonists (20 [mu]M N-[6-aminohexyl]-5-chloro-1-naphthalenesulfonamide), and the anion channel blocker 5-nitro-2,3-phenylpropyllamino benzoic acid (50 [mu]M). These data suggest that the slow, outward rectifying anion channel, whose opening would be related to the membrane potential, and at least one step requiring a protein phosphorylation by a Ca2+-calmodulin-dependent protein kinase of the myosin light chain kinase type might be implicated in the induction of stomatal closing by vanadate or a light/dark transition.
Cousson
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Commissariat a l'Energie Atomique (France), Departement d'Ecophysiologie Vegetale et de Microbiologie, Centre d'Etudes Nucleaires de Cadarache, 13108, Saint-Paul-lez-Durance Cedex, France.
Cotelle
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Vavasseur
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