A Redox-Mediated Modulation of Stem Bolting in Transgenic<i>Nicotiana sylvestris</i>Differentially Expressing the External Mitochondrial NADPH Dehydrogenase

Liu, Yun-Jun; Nunes‐Nesi, Adriano; Wallström, Sabá V.; Lager, Ida; Michalecka, Agnieszka M.; Norberg, Fredrik E.B.; Widell, Susanne; Fredlund, Kenneth M.; Fernie, Alisdair R.; Rasmusson, Allan G.

doi:10.1104/pp.109.136242

Cited by 41 publications

(33 citation statements)

References 81 publications

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“…Recent studies of Arabidopsis knock-out mutants of the constituent enzymes of these pathway as well as of the external NAD(P)H dehydrogenases have highlighted the importance of pyridine nucleotides in a broad range of processes including germination (74), bolting (75), adaptation to osmotic stress (76), and senescence (77), suggesting that the NDTs may also play an important role in these processes.…”

Section: Discussionmentioning

confidence: 99%

Molecular Identification and Functional Characterization of Arabidopsis thaliana Mitochondrial and Chloroplastic NAD+ Carrier Proteins

Palmieri

Rieder

Ventrella

et al. 2009

Journal of Biological Chemistry

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157

172

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The Arabidopsis thaliana L. genome contains 58 membrane proteins belonging to the mitochondrial carrier family. Two mitochondrial carrier family members, here named AtNDT1 and AtNDT2, exhibit high structural similarities to the mitochondrial nicotinamide adenine dinucleotide (NAD ؉ ) carrierScNDT1 from bakers' yeast. Expression of AtNDT1 or AtNDT2 restores mitochondrial NAD ؉ transport activity in a yeast mutant lacking ScNDT. Localization studies with green fluorescent protein fusion proteins provided evidence that AtNDT1 resides in chloroplasts, whereas only AtNDT2 locates to mitochondria. Heterologous expression in Escherichia coli followed by purification, reconstitution in proteoliposomes, and uptake experiments revealed that both carriers exhibit a submillimolar affinity for NAD ؉ and transport this compound in a counterexchange mode. Among various substrates ADP and AMP are the most efficient counter-exchange substrates for NAD ؉ .Atndt1-and Atndt2-promoter-GUS plants demonstrate that both genes are strongly expressed in developing tissues and in particular in highly metabolically active cells. The presence of both carriers is discussed with respect to the subcellular localization of de novo NAD ؉ biosynthesis in plants and with respect to both the NAD ؉ -dependent metabolic pathways and the redox balance of chloroplasts and mitochondria.Nucleotides are metabolites of enormous importance for all living cells. They are the essential building blocks for DNA and RNA synthesis, energize most anabolic and many catabolic reactions, and fulfill critical functions in intracellular signal transduction (1, 2). Moreover, nucleotides serve as cofactors for a wide number of enzymes and are, with water, the most highly connected compounds within the metabolic network (3). Among these co-factors nicotinamide adenine dinucleotides are widely used for reductive/oxidative processes, playing important roles in the operation and control of a wide range of dehydrogenase activities. Accordingly, nucleotides are essential in nearly all cell organelles, and transport of these solutes into mitochondria, plastids, the endoplasmic reticulum, the Golgi apparatus, and peroxisomes has been observed (4 -7).Two types of nucleotide transport proteins have been identified to date at the molecular level: nucleotide transporter (NTT) 2 type carriers and members of the mitochondrial carrier family. The former transporters occur in plastids from all plants (8) and in a limited number of intracellular pathogenic bacteria (9). Most NTT-type carrier proteins catalyze an ATP/ADPϩP i counter-exchange mode of transport (10 -13), but several bacterial NTT proteins mediate either H ϩ /nucleotide transport or NAD ϩ /ADP counter-exchange (12,14,15). With the exception of the bacterial NAD ϩ /ADP carrier (14), all NTT proteins exhibit 12 predicted trans-membrane domains, whereas none of the NTT proteins share structural or domain similarities to members of the mitochondrial carrier family (11).Carriers belonging to the mitochondrial carrier family (MC...

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Section: Discussionmentioning

confidence: 99%

Molecular Identification and Functional Characterization of Arabidopsis thaliana Mitochondrial and Chloroplastic NAD+ Carrier Proteins

Palmieri

Rieder

Ventrella

et al. 2009

Journal of Biological Chemistry

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157

172

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“…The type II NAD(P)H dehydrogenases are located on the internal and external sides of the inner mitochondrial membrane and oxidize NADH or NADPH from the mitochondrial matrix or the cytosol (206,276,277). These reactions bypass the first energy conservation step maintained by the proton pumping complex I, which oxidizes matrix NADH.…”

Section: The Metcmentioning

confidence: 99%

Metabolic Control of Redox and Redox Control of Metabolism in Plants

Geigenberger

Fernie

2014

Antioxidants & Redox Signaling

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142

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Significance: Reduction-oxidation (Redox) status operates as a major integrator of subcellular and extracellular metabolism and is simultaneously itself regulated by metabolic processes. Redox status not only dominates cellular metabolism due to the prominence of NAD(H) and NADP(H) couples in myriad metabolic reactions but also acts as an effective signal that informs the cell of the prevailing environmental conditions. After relay of this information, the cell is able to appropriately respond via a range of mechanisms, including directly affecting cellular functioning and reprogramming nuclear gene expression. Recent Advances: The facile accession of Arabidopsis knockout mutants alongside the adoption of broad-scale post-genomic approaches, which are able to provide transcriptomic-, proteomic-, and metabolomic-level information alongside traditional biochemical and emerging cell biological techniques, has dramatically advanced our understanding of redox status control. This review summarizes redox status control of metabolism and the metabolic control of redox status at both cellular and subcellular levels. Critical Issues: It is becoming apparent that plastid, mitochondria, and peroxisome functions influence a wide range of processes outside of the organelles themselves. While knowledge of the network of metabolic pathways and their intraorganellar redox status regulation has increased in the last years, little is known about the interorganellar redox signals coordinating these networks. A current challenge is, therefore, synthesizing our knowledge and planning experiments that tackle redox status regulation at both inter-and intracellular levels. Future Directions: Emerging tools are enabling ever-increasing spatiotemporal resolution of metabolism and imaging of redox status components. Broader application of these tools will likely greatly enhance our understanding of the interplay of redox status and metabolism as well as elucidating and characterizing signaling features thereof. We propose that such information will enable us to dissect the regulatory hierarchies that mediate the strict coupling of metabolism and redox status which, ultimately, determine plant growth and development.

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“…In addition to complex II (succinate dehydrogenase), nonphosphorylating alternative NAD(P)H dehydrogenases (type II dehydrogenases), located on the inner and outer surfaces of the inner mitochondrial membrane, are essential for plant growth and metabolism (Liu et al, 2009;Wallström et al, 2014). Their activity depends on plant metabolic status, such as NADH and Ca 2+ concentration (Rasmusson et al, 2008).…”

Section: Lack Of the Ndufs8 Subunit Results In Holo-ci Misassembly Anmentioning

confidence: 99%

“…8A). Overreduction of the NAD pool in mutants might stem from the induction of alternative NAD(P)H dehydrogenase activities (Liu et al, 2009;Rasmusson and Wallström, 2010;Wallström et al, 2014) and/or the activation of redox shuttles (Shen et al, 2006). A redox effect may have then resulted in alterations of the circadian clock (Stangherlin and Reddy, 2013;Shim and Imaizumi, 2015).…”

Section: Signaling Mechanisms Possibly Involved In the Impaired Ld Acmentioning

confidence: 99%

Photoperiod Affects the Phenotype of Mitochondrial Complex I Mutants

Pétriacq

Bont²,

Genestout³

et al. 2016

Plant Physiol.

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Plant mutants for genes encoding subunits of mitochondrial complex I (CI; NADH:ubiquinone oxidoreductase), the first enzyme of the respiratory chain, display various phenotypes depending on growth conditions. Here, we examined the impact of photoperiod, a major environmental factor controlling plant development, on two Arabidopsis (Arabidopsis thaliana) CI mutants: a new insertion mutant interrupted in both ndufs8.1 and ndufs8.2 genes encoding the NDUFS8 subunit and the previously characterized ndufs4 CI mutant. In the long day (LD) condition, both ndufs8.1 and ndufs8.2 single mutants were indistinguishable from Columbia-0 at phenotypic and biochemical levels, whereas the ndufs8.1 ndufs8.2 double mutant was devoid of detectable holo-CI assembly/activity, showed higher alternative oxidase content/activity, and displayed a growth retardation phenotype similar to that of the ndufs4 mutant. Although growth was more affected in ndufs4 than in ndufs8.1 ndufs8.2 under the short day (SD) condition, both mutants displayed a similar impairment of growth acceleration after transfer to LD compared with the wild type. Untargeted and targeted metabolomics showed that overall metabolism was less responsive to the SD-to-LD transition in mutants than in the wild type. The typical LD acclimation of carbon and nitrogen assimilation as well as redox-related parameters was not observed in ndufs8.1 ndufs8. Similarly, NAD(H) content, which was higher in the SD condition in both mutants than in Columbia-0, did not adjust under LD. We propose that altered redox homeostasis and NAD(H) content/redox state control the phenotype of CI mutants and photoperiod acclimation in Arabidopsis.Complex I (CI; NADH:ubiquinone oxidoreductase; EC 1.6.5.3), the first enzyme of the respiratory chain of most eukaryotes, including plants, couples electron transfer to proton translocation through the inner mitochondrial membrane (Klodmann et al., 2010). CI is an L-shaped multimeric enzyme of around 1 MD in size composed of a matrix-faced peripheral arm carrying the NADH-oxidizing activity (N module), a connecting module (Q module transferring electrons to the quinonebinding site), and a hydrophobic intramembrane arm carrying the proton translocation activity (P module). Eukaryotic CI comprises more than 40 subunits, 434

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A Redox-Mediated Modulation of Stem Bolting in TransgenicNicotiana sylvestrisDifferentially Expressing the External Mitochondrial NADPH Dehydrogenase

Cited by 41 publications

References 81 publications

Molecular Identification and Functional Characterization of Arabidopsis thaliana Mitochondrial and Chloroplastic NAD+ Carrier Proteins

Molecular Identification and Functional Characterization of Arabidopsis thaliana Mitochondrial and Chloroplastic NAD+ Carrier Proteins

Metabolic Control of Redox and Redox Control of Metabolism in Plants

Photoperiod Affects the Phenotype of Mitochondrial Complex I Mutants

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