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1.
J Exp Bot ; 56(422): 3223-8, 2005 Dec.
Article in English | MEDLINE | ID: mdl-16263901

ABSTRACT

Previous studies suggest that abscisic acid (ABA) stimulates the activities of antioxidant enzymes under normal and chilling temperature and enhanced chilling resistance in Stylosanthes guianensis. The objective of this study was to test whether nitric oxide (NO) is involved in the ABA-induced activities of the antioxidant enzymes in Stylosanthes guianensis due to its nature as a second messenger in stress responses. Plants were treated with NO donors, ABA, ABA in combination with NO scavengers or the nitric oxide synthase (NOS) inhibitor and their effects on the activity of antioxidant enzymes and NO production were compared. The results showed that ABA increased the activities of superoxide dismutase (SOD), catalase (CAT), and ascorbate peroxidase (APX). The effect of ABA on antioxidant enzyme activities was suppressed by the NOS inhibitor, N(omega)-nitro-L-arginine (L-NNA), and the NO scavenger, 2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl3-oxide (PTIO). NO content increased after 5 h of ABA treatment. The NO-scavenger, PTIO, and the NOS-inhibitor, L-NNA, inhibited the accumulation of NO in ABA-treated Stylosanthes guianensis. NO donor treatment enhanced the activities of SOD, CAT, and APX. The results suggested that NO was involved in the ABA-induced activities of SOD, CAT, and APX in Stylosanthes guianensis. ABA triggered NO production that may lead to the stimulation of antioxidant enzyme activities.


Subject(s)
Abscisic Acid/pharmacology , Antioxidants/metabolism , Fabaceae/enzymology , Nitric Oxide/physiology , Ascorbate Peroxidases , Catalase/metabolism , Cyclic N-Oxides/pharmacology , Enzyme Inhibitors/pharmacology , Fabaceae/drug effects , Free Radical Scavengers/pharmacology , Imidazoles/pharmacology , Nitric Oxide/metabolism , Nitric Oxide Donors/pharmacology , Nitric Oxide Synthase/antagonists & inhibitors , Nitroarginine/pharmacology , Peroxidases/metabolism , Superoxide Dismutase/metabolism
2.
Plant Sci ; 162(2): 239-44, 2002 Feb.
Article in English | MEDLINE | ID: mdl-11989489

ABSTRACT

ADP-glucose pyrophosphorylase (AGPase, EC2.7.7.27) is a key regulatory enzyme in starch biosynthesis. The enzyme is a heterotetramer with two S and two B subunits. In tomato, there are three multiple forms of the S subunit gene. Agp S1, S2 and B are highly expressed in fruit from 10 to 25 days after anthesis. Agp S3 is only weakly expressed in fruit. Sucrose significantly elevates expression of Agp S1, S2 and B in both leaves and fruits. Agp S1 exhibits the highest degree of regulation by sucrose. In fact, sucrose may be required for Agp S1 expression. For excised leaves incubated in water, no transcripts for Agp S1 could be detected in the absence of sucrose, whereas it took up to 16 h in water before transcripts were no longer detectable for Agp S2 and B. Neither Agp S3 nor the tubulin gene is affected by sucrose, demonstrating that this response is specifically regulated by a carbohydrate metabolic signal, and is not due to a general increase in metabolism caused by sucrose treatment. Truncated versions of the promoter for Agp S1 indicate that a specific region 1.3-3.0 kb upstream from the transcription site is responsible for sucrose sensitivity. This region of the S1 promoter contains several cis-acting elements present in the promoters of other genes that are also regulated by sucrose.


Subject(s)
Fruit/genetics , Gene Expression Regulation, Plant/drug effects , Nucleotidyltransferases/genetics , Plant Leaves/genetics , Solanum lycopersicum/genetics , Sucrose/pharmacology , Fruit/enzymology , Fruit/growth & development , Glucose-1-Phosphate Adenylyltransferase , Glucuronidase/genetics , Solanum lycopersicum/enzymology , Solanum lycopersicum/growth & development , Plant Leaves/enzymology , Plant Leaves/growth & development , Plants, Genetically Modified , Nicotiana/enzymology , Nicotiana/genetics , Transcription, Genetic
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