Identification in vitro of a post-translational regulatory site in the hinge 1 region of Arabidopsis nitrate reductase.

Su, Wenpei; Huber, Steven C.; Crawford, Nigel M.

doi:10.1105/tpc.8.3.519

Cited by 96 publications

(92 citation statements)

References 50 publications

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“…For example, H 2 O 2 is required for the activation of mitogen-activated protein kinase (MAPK) 6, which can subsequently increase NR activity by phosphorylation of NIA2 at Ser-627 (Wang et al, 2010a). Also, NIA2 can be phosphorylated by a calcium-dependent protein kinase at Ser-534 in the hinge 1 region in response to light and other environmental signals (Su et al, 1996). Therefore, increased cellular H 2 O 2 concentrations following exposure to high light might also increase NR activity through the phosphorylation of either Ser-627 or Ser-534.…”

Section: Discussionmentioning

confidence: 99%

Nitric Oxide and ProteinS-Nitrosylation Are Integral to Hydrogen Peroxide-Induced Leaf Cell Death in Rice

et al. 2011

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Nitric oxide (NO) is a key redox-active, small molecule involved in various aspects of plant growth and development. Here, we report the identification of an NO accumulation mutant, nitric oxide excess1 (noe1), in rice (Oryza sativa), the isolation of the corresponding gene, and the analysis of its role in NO-mediated leaf cell death. Map-based cloning revealed that NOE1 encoded a rice catalase, OsCATC. Furthermore, noe1 resulted in an increase of hydrogen peroxide (H 2 O 2 ) in the leaves, which consequently promoted NO production via the activation of nitrate reductase. The removal of excess NO reduced cell death in both leaves and suspension cultures derived from noe1 plants, implicating NO as an important endogenous mediator of H 2 O 2 -induced leaf cell death. Reduction of intracellular S-nitrosothiol (SNO) levels, generated by overexpression of rice S-nitrosoglutathione reductase gene (GSNOR1), which regulates global levels of protein S-nitrosylation, alleviated leaf cell death in noe1 plants. Thus, S-nitrosylation was also involved in light-dependent leaf cell death in noe1. Utilizing the biotin-switch assay, nanoliquid chromatography, and tandem mass spectrometry, S-nitrosylated proteins were identified in both wild-type and noe1 plants. NO targets identified only in noe1 plants included glyceraldehyde 3-phosphate dehydrogenase and thioredoxin, which have been reported to be involved in S-nitrosylation-regulated cell death in animals. Collectively, our data suggest that both NO and SNOs are important mediators in the process of H 2 O 2 -induced leaf cell death in rice.

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Section: Discussionmentioning

confidence: 99%

Nitric Oxide and ProteinS-Nitrosylation Are Integral to Hydrogen Peroxide-Induced Leaf Cell Death in Rice

et al. 2011

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“…Evidence for inactivation of NR from other plant sources by the same mechanism has been obtained for squash (Lillo, 1993), cabbage (Kojima et al, 1995), maize (Huber et al, 1994;Li and Oaks, 1994), barley (Decires et al, 1993), Nicotiana plumbaginifolia (Nussaume et al, 1995), pea (Glaab and Kaiser, 1993), and Arabidopsis (Labrie and Crawford, 1994;Su et al, 1996). The precise mechanism of NR inactivation is as yet poorly understood because a complete structural model of the NR molecule is still lacking.…”

mentioning

confidence: 93%

A Conserved Acidic Motif in the N-Terminal Domain of Nitrate Reductase Is Necessary for the Inactivation of the Enzyme in the Dark by Phosphorylation and 14-3-3 Binding1

1999

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We found that the deletion of a conserved stretch of acidic residues led to an active NR protein that was more thermosensitive than the wild-type enzyme, but it was relatively insensitive to the inactivation by phosphorylation in the dark. Therefore, the removal of this acidic stretch seems to have the same effects on NR activation state as the deletion of the N-terminal domain. A hypothetical explanation for these observations is that a specific factor that impedes inactivation remains bound to the truncated enzyme. A synthetic peptide derived from this acidic protein motif was also found to be a good substrate for casein kinase II.Most higher plants obtain the nitrogen metabolites needed for growth and development by taking up and assimilating nitrate. After active transport into the cell, nitrate is reduced to nitrite by NR (EC 1.6.6.1-2), a cytosolic enzyme. Subsequently, nitrite is reduced to ammonium by nitrite reductase, which is localized in the chloroplast.The expression of the NR gene is highly regulated at the transcriptional level by many endogenous and environmental factors, including hormones, light, nitrogen source, and carbohydrates (for review, see Hoff et al., 1994;Crawford, 1995). These transcriptional regulations probably determine the long-term fluctuations in the NR protein level. On the other hand, a reversible posttranslational regulation of the NR protein involving protein phosphorylation allows short-term modulation of the enzyme activity in response to light-dark transitions, variations in photosynthetic activity, CO 2 level, intracellular pH, or oxygen availability (Kaiser and Fö rster, 1989;

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“…In higher plants, NR inactivation is mediated by the phosphorylation of a conserved serine residue (S534) (supplemental Table S3) and binding of 14 -3-3 proteins in the presence of divalent cations or polyamines (81). Mutation of this phosphorylation site in Arabidopsis to aspartate (82) results in the complete abolition of activation/inactivation in response to light/dark transitions or other treatments known to regulate the activation state of NR. In agreement with this finding, we observed a strong morning-phased oscillation in the phosphorylation state of this regulatory residue (S534) in nitrate reductase 2 (NIA2) that is antiphasic to the maximum of NR activity (80).…”

Section: Phospho-oscillations In Key Elements Of Carbohydrate and Nitmentioning

confidence: 99%

Quantitative Circadian Phosphoproteomic Analysis of Arabidopsis Reveals Extensive Clock Control of Key Components in Physiological, Metabolic, and Signaling Pathways

Choudhary

Nomura

Wang

et al. 2015

Molecular & Cellular Proteomics

121

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The circadian clock provides adaptive advantages to an organism, resulting in increased fitness and survival. The phosphorylation events that regulate circadian-dependent signaling and the processes which post-translationally respond to clock-gated signals are largely unknown. To better elucidate post-translational events tied to the circadian system we carried out a survey of circadianregulated protein phosphorylation events in Arabidopsis seedlings. A large-scale mass spectrometry-based quantitative phosphoproteomics approach employing TiO2-based phosphopeptide enrichment techniques identified and quantified 1586 phosphopeptides on 1080 protein groups. A total of 102 phosphopeptides displayed significant changes in abundance, enabling the identification of specific patterns of response to circadian rhythms. Our approach was sensitive enough to quantitate oscillations in the phosphorylation of low abundance clock proteins (EARLY FLOWERING4; ELF4 and PSEUDORESPONSE REGULATOR3; PRR3) as well as other transcription factors and kinases. During constant light, extensive cyclic changes in phosphorylation status occurred in critical regulators, implicating direct or indirect regulation by the circadian system. These included proteins influencing transcriptional regulation, translation, metabolism, stress and phytohormones-mediated responses. We validated our analysis using the elf4 -211 allele, in which an S45L transition removes the phosphorylation herein identified. We show that removal of this phosphorylatable site diminishes interaction with EARLY FLOWERING3 (ELF3), a key partner in a tripartite evening complex required for circadian cycling. elf4 -211 lengthens period, which increases with increasing temperature, relative to the wild type, resulting in a more stable temperature compensation of circadian period over a wider temperature range. Molecular

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Identification in vitro of a post-translational regulatory site in the hinge 1 region of Arabidopsis nitrate reductase.

Cited by 96 publications

References 50 publications

Nitric Oxide and ProteinS-Nitrosylation Are Integral to Hydrogen Peroxide-Induced Leaf Cell Death in Rice

Nitric Oxide and ProteinS-Nitrosylation Are Integral to Hydrogen Peroxide-Induced Leaf Cell Death in Rice

A Conserved Acidic Motif in the N-Terminal Domain of Nitrate Reductase Is Necessary for the Inactivation of the Enzyme in the Dark by Phosphorylation and 14-3-3 Binding1

Quantitative Circadian Phosphoproteomic Analysis of Arabidopsis Reveals Extensive Clock Control of Key Components in Physiological, Metabolic, and Signaling Pathways

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