ArticlePlant signaling & behavior2013
Further insights into the isoenzyme composition and activity of glutamate dehydrogenase in Arabidopsis thaliana.
Article in Plant signaling & behavior, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 40 citations in OpenAlex.
- ArabidopsisPhysiology and molecular biology of plants : an international journal of functional plant biology · 2024Article
- The Key Role of Glutamate Dehydrogenase 2 (GDH2) in the Control of Kernel Production in Maize (Plants (Basel, Switzerland) · 2023Article
- Structural and mechanistic insights into the bifunctional HISN2 enzyme catalyzing the second and third steps of histidine biosynthesis in plants.Scientific reports · 2021Article
- Structural Studies of Glutamate Dehydrogenase (Isoform 1) FromFrontiers in plant science · 2020Article
- Heterologous expression of Oenococcus oeni sHSP20 confers temperature stress tolerance in Escherichia coli.Cell stress & chaperones · 2018Article
- Reassimilation of Photorespiratory Ammonium in Lotus japonicus Plants Deficient in Plastidic Glutamine Synthetase.PloS one · 2015Article
- Respiratory electron transfer pathways in plant mitochondria.Frontiers in plant science · 2014Review
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Authors and funding
7 authors at 4 institutions in 4 countries.
Funding
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Abstract
Following the discovery that in Arabidopsis, a third isoenzyme of NADH-dependent glutamate dehydrogenase (GDH) is expressed in the mitochondria of the root companion cells, we have re-examined the GDH isoenzyme composition. By analyzing the NADH-GDH isoenzyme composition of single, double and triple mutants deficient in the expression of the three genes encoding the enzyme, we have found that the α, β and γ polypeptides that comprise the enzyme can be assembled into a complex combination of heterohexamers in roots. Moreover, we observed that when one or two of the three root isoenzymes were missing from the mutants, the remaining isoenzymes compensated for this deficiency. The significance of such complexity is discussed in relation to the metabolic and signaling function of the NADH-GDH enzyme. Although it has been shown that a fourth gene encoding a NADPH-dependent enzyme is present in Arabidopsis, we were not able to detect corresponding enzyme activity, even in the triple mutant totally lacking NADH-GDH activity.
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