Identification of the Arabidopsis calmodulin-dependent NAD+ kinase that sustains the elicitor-induced oxidative burst
Langue
en
Article de revue
Ce document a été publié dans
Plant Physiology. 2019-09-14, vol. 181, n° 4, p. 1449-1458
Oxford University Press ; American Society of Plant Biologists
Résumé en anglais
17 NADP(H) is an essential cofactor of multiple metabolic processes in all living organisms. In plants, 18 NADP(H) is required as the substrate of Ca 2+-dependent NADPH oxidases which catalyze a reactive 19 oxygen species ...Lire la suite >
17 NADP(H) is an essential cofactor of multiple metabolic processes in all living organisms. In plants, 18 NADP(H) is required as the substrate of Ca 2+-dependent NADPH oxidases which catalyze a reactive 19 oxygen species burst in response to various stimuli. While NADP + production in plants has long been 20 known to involve a Calmodulin and Calcium (CaM)/Ca 2+-dependent NAD + kinase, the nature of the 21 enzyme catalyzing this activity has remained enigmatic, as well as its role in plant physiology. Here, 22 thanks to a combination of proteomics, biochemistry, molecular biology and in vivo studies, we have 23 identified an Arabidopsis protein that catalyzes NADP + production exclusively in the presence of 24 CaM/Ca 2+. This new enzyme (NADKc) has a CaM-binding peptide located in its N-terminal region and 25 displays peculiar biochemical properties as well as different domain organization compared to known 26 plant NAD + kinases. In response to a pathogen elicitor, activity of NADKc, which is associated with the 27 mitochondrial periphery, contributes to an increase in the cellular NADP + concentration and to the 28 amplification of the elicitor-induced oxidative burst. Based on a phylogenetic analysis and enzymatic 29 assays, we propose that the CaM/Ca 2+-dependent NAD + kinase activity found in photosynthetic 30< Réduire
Project ANR
Mediterranean Center for Environment and Biodiversity - ANR-10-LABX-0004
Infrastructure Française de Protéomique - ANR-10-INBS-0008
Infrastructure Française de Protéomique - ANR-10-INBS-0008
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