Cloning and characterization of Lotus japonicus formate dehydrogenase: A possible correlation with hypoxia

Andreadeli, Aggeliki; Flemetakis, Emmanouil; Axarli, Irene; Dimou, Maria; Udvardi, Michael K.; Katinakis, Panagiotis; Labrou, Nikolaos E.

doi:10.1016/j.bbapap.2009.02.009

Cited by 30 publications

(21 citation statements)

References 45 publications

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“…In maritime pine, the biosynthesis of FDH is enhanced during a drought [23]. An increase in the level of FDH mRNA was also observed in Lotus japonicиs plants cultivated under conditions of hypoxia [10]. …”

Section: Discovery History Localization  and Physiological Role Of mentioning

confidence: 99%

“…Thus, all necessary conditions for the performance of systematic studies of FDHs from A. thaliana and soybean G. max were provided, including genetic engineering experiments and X-ray diffraction determination of the structure. The experiments were successfully carried out for the expression of FDH from L. japonicas in E. coli cells [10]. …”

Section: Obtainment Of Plant Formate Dehydrogenasesmentioning

confidence: 99%

“…Recent studies have revealed that FDH also belongs to stress proteins in plants, similar to those found in pathogenic microorganisms. FDH synthesis strongly increases under the following conditions: drought, with abrupt changes in temperature, irradiation with hard ultraviolet light, through the action of chemical agents [7–9], hypoxia [10], and action of pathogenic microorganisms [11]. The significance of the physiological role of this enzyme gives rise to the necessity of studying plant FDHs.…”

Section: Introductionmentioning

confidence: 99%

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NAD+-dependent Formate Dehydrogenase from Plants

2011

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NAD+-dependent formate dehydrogenase (FDH, EC 1.2.1.2) widely occurs in nature. FDH consists of two identical subunits and contains neither prosthetic groups nor metal ions. This type of FDH was found in different microorganisms (including pathogenic ones), such as bacteria, yeasts, fungi, and plants. As opposed to microbiological FDHs functioning in cytoplasm, plant FDHs localize in mitochondria. Formate dehydrogenase activity was first discovered as early as in 1921 in plant; however, until the past decade FDHs from plants had been considerably less studied than the enzymes from microorganisms. This review summarizes the recent results on studying the physiological role, properties, structure, and protein engineering of plant formate dehydrogenases.

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Section: Discovery History Localization  and Physiological Role Of mentioning

confidence: 99%

Section: Obtainment Of Plant Formate Dehydrogenasesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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NAD+-dependent Formate Dehydrogenase from Plants

2011

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“…; Andreadeli et al . ). Based on the amino acid sequence, Arabidopsis FDH was predicted to possess dual signals for targeting to chloroplasts and mitochondria (Olson et al .…”

Section: Introductionmentioning

confidence: 97%

C1 metabolism and the Calvin cycle function simultaneously and independently during HCHO metabolism and detoxification in Arabidopsis thaliana treated with HCHO solutions

Song

Xiao

You

et al. 2013

Plant Cell & Environment

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“…We also identified other proteins associated with energy metabolism, such as D-2-hydroxyglutarate dehydrogenase (D-2HGDH), which catalyzes the formation of 2-ketoglutarate from D-2-hydroxyglutarate in the mitochondria and releases energy [52], and formate dehydrogenase (FDH), which catalyzes the oxidation of formic acid to CO 2 and reduces NAD + to NADH [53, 54]. Our proteomic study indicated that these two proteins were down-regulated in the IS at 10 DPA.…”

Section: Discussionmentioning

confidence: 99%

iTRAQ-based proteome profile analysis of superior and inferior Spikelets at early grain filling stage in japonica Rice

You

Chen

et al. 2017

BMC Plant Biol

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BackgroundLarge-panicle rice varieties often fail to achieve their yield potential due to poor grain filling of late-flowering inferior spikelets (IS). The physiological and molecular mechanisms of poor IS grain filling, and whether an increase in assimilate supply could regulate protein abundance and consequently improve IS grain filling for japonica rice with large panicles is still partially understood.ResultsA field experiment was performed with two spikelet removal treatments at anthesis in the large-panicle japonica rice line W1844, including removal of the top 1/3 of spikelets (T1) and removal of the top 2/3 of spikelets (T2), with no spikelet removal as a control (T0). The size, weight, setting rate, and grain filling rate of IS were significantly increased after spikelet removing. The biological functions of the differentially expressed proteins (DEPs) between superior and inferior spikelets as well as the response of IS to the removal of superior spikelets (SS) were investigated by using iTRAQ at 10 days post anthesis. A total of 159, 87, and 28 DEPs were identified from group A (T0-SS/T0-IS), group B (T0-SS/T2-IS), and group C (T2-IS/T0-IS), respectively. Among these, 104, 63, and 22 proteins were up-regulated, and 55, 24, and 6 proteins were down-regulated, respectively. Approximately half of these DEPs were involved in carbohydrate metabolism (sucrose-to-starch metabolism and energy metabolism) and protein metabolism (protein synthesis, folding, degradation, and storage).ConclusionsReduced endosperm cell division and decreased activities of key enzymes associated with sucrose-starch metabolism and nitrogen metabolism are mainly attributed to the poor sink strength of IS. In addition, due to weakened photosynthesis and respiration, IS are unable to obtain a timely supply of materials and energy after fertilization, which might be resulted in the stagnation of IS development. Finally, an increased abundance of 14–3-3 protein in IS could be involved in the inhibition of starch synthesis. The removal of SS contributed to transfer of assimilates to IS and enhanced enzymatic activities of carbon metabolism (sucrose synthase, starch branching enzyme, soluble starch synthase, and pullulanase) and nitrogen metabolism (aspartate amino transferase and alanine amino transferase), promoting starch and protein synthesis in IS. In addition, improvements in energy metabolism (greater abundance of pyrophosphate-fructose 6-phosphate 1-phosphotransferase) might be played a vital role in inducing the initiation of grain filling. These results collectively demonstrate that carbohydrate supply is the main cause of poor IS grain filling.Electronic supplementary materialThe online version of this article (doi:10.1186/s12870-017-1050-2) contains supplementary material, which is available to authorized users.

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Cloning and characterization of Lotus japonicus formate dehydrogenase: A possible correlation with hypoxia

Cited by 30 publications

References 45 publications

NAD+-dependent Formate Dehydrogenase from Plants

NAD+-dependent Formate Dehydrogenase from Plants

C1 metabolism and the Calvin cycle function simultaneously and independently during HCHO metabolism and detoxification in Arabidopsis thaliana treated with HCHO solutions

iTRAQ-based proteome profile analysis of superior and inferior Spikelets at early grain filling stage in japonica Rice

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