Abstract

Nitric oxide synthase-like activity contributes to the production of nitric oxide in plants, which controls plant responses to stress. This study investigates if changes in ascorbate peroxidase enzymatic activity and glycine betaine content in response to inhibition of nitric oxide synthase-like activity are associated with transcriptional regulation by analyzing transcript levels of genes (betaine aldehyde dehydrogenase) involved in glycine betaine biosynthesis and those encoding antioxidant enzymes (ascorbate peroxidase and catalase) in leaves of maize seedlings treated with an inhibitor of nitric oxide synthase-like activity. In seedlings treated with a nitric oxide synthase inhibitor, transcript levels of betaine aldehyde dehydrogenase were decreased. In plants treated with the nitric oxide synthase inhibitor, the transcript levels of ascorbate peroxidase-encoding genes were down-regulated. We thus conclude that inhibition of nitric oxide synthase-like activity suppresses the expression of ascorbate peroxidase and betaine aldehyde dehydrogenase genes in maize leaves. Furthermore, catalase activity was suppressed in leaves of plants treated with nitric oxide synthase inhibitor; and this corresponded with the suppression of the expression of catalase genes. We further conclude that inhibition of nitric oxide synthase-like activity, which suppresses ascorbate peroxidase and catalase enzymatic activities, results in increased H2O2 content.

Highlights

  • Nitric oxide (NO) is a signaling molecule which regulates biochemical, metabolic and physiological processes that are beneficial to plants[1,2,3]

  • We previously showed that application of L-NAME significantly decreased NOcontent, which resulted in a reduction of the content of glycine betaine (GB) in maize roots and leaves[14]

  • The first oxidation step is catalyzed by choline monooxygenase (CMO, EC 1.14.15.7), with further oxidation to GB being catalyzed by betaine aldehyde dehydrogenase (BADH, EC 1.2.1.81)[20]

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Summary

Introduction

Nitric oxide (NO) is a signaling molecule which regulates biochemical, metabolic and physiological processes that are beneficial to plants[1,2,3]. We previously showed that application of L-NAME (an analogue of L-arginine, which functions as a competitive inhibitor of animal NOS-mediated NOsynthesis) significantly decreased NOcontent, which resulted in a reduction of the content of glycine betaine (GB) in maize roots and leaves[14]. This NOS inhibition was associated with decreased activity of APX. This suggests that the key determining enzyme in the biosynthesis of GB accumulation is BADH

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