Literature summary for 1.8.5.1 extracted from

Rahantaniaina, M.S.; Li, S.; Chatel-Innocenti, G.; Tuzet, A.; Mhamdi, A.; Vanacker, H.; Noctor, G.
Glutathione oxidation in response to intracellular H2O2 key but overlapping roles for dehydroascorbate reductases (2017), Plant Signal. Behav., 12, e1356531 .

Search for more literature for 1.8.5.1

Activating Compound

Activating Compound	Comment	Organism	Structure
3-aminotriazole	3-AT, decreased catalase to very low levels while inducing ascorbate peroxidase (APX) and DHAR activities	Arabidopsis thaliana

Protein Variants

Protein Variants	Comment	Organism
additional information	construction of a complete set of single, double and triple mutants carrying T-DNAs in isozymes DHAR1, DHAR2, and DHAR3	Arabidopsis thaliana
additional information	construction of a complete set of single, double and triple mutants carrying T-DNAs in isozymes DHAR1, DHAR2, and DHAR3. No effect on phenotype is observed in the absence of stress. When the different dhar mutant combinations are introduced into a catalase-deficient background (cat2), the combined presence of dhar1 and dhar2 decreased GSSG and total glutathione accumulation. When all 3 DHARs are knocked out, cat2-triggered glutathione oxidation is almost completely inhibited	Arabidopsis thaliana

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
chloroplast	-	Arabidopsis thaliana	9507	-
cytosol	-	Arabidopsis thaliana	5829	-
mitochondrion	-	Arabidopsis thaliana	5739	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2 glutathione + dehydroascorbate	Arabidopsis thaliana	-	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	Arabidopsis thaliana Col-0	-	glutathione disulfide + ascorbate	-	?

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	Q8LE52	-	-
Arabidopsis thaliana	Q9FRL8	-	-
Arabidopsis thaliana	Q9FWR4	-	-
Arabidopsis thaliana Col-0	Q8LE52	-	-
Arabidopsis thaliana Col-0	Q9FRL8	-	-
Arabidopsis thaliana Col-0	Q9FWR4	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
leaf	-	Arabidopsis thaliana	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2 glutathione + dehydroascorbate	-	Arabidopsis thaliana	glutathione disulfide + ascorbate	-	?
2 glutathione + dehydroascorbate	-	Arabidopsis thaliana Col-0	glutathione disulfide + ascorbate	-	?

Synonyms

Synonyms	Comment	Organism
dehydroascorbate reductase	-	Arabidopsis thaliana
DHAR	-	Arabidopsis thaliana
DHAR1	-	Arabidopsis thaliana
DHAR2	-	Arabidopsis thaliana
DHAR3	-	Arabidopsis thaliana

General Information

General Information	Comment	Organism
malfunction	multiple loss of DHAR functions markedly decreases glutathione oxidation triggered by catalase deficiency. No evidence is obtained that either GRs or MDHARs are upregulated in plants lacking DHAR function. 3-Aminotriazole (3-AT) decreases catalase to very low levels while inducing ascorbate peroxidase (APX) and DHAR activities. These effects are accompanied by extensive leaf bleaching, and glutathione oxidation is evident as marked accumulation of GSSG. No difference is observed in bleaching or glutathione contents between the wild-type control and any of the mutants. Loss-of-function mutants for DHAR suggest that ascorbate regeneration is the major route leading to GSSG accumulation in response to intracellular H2O2. No effect on phenotype is observed in the absence of stress. When the different dhar mutant combinations are introduced into a catalase-deficient background (cat2), the combined presence of dhar1 and dhar2 decreased GSSG and total glutathione accumulation. When all 3 DHAR isozymes (DHAR1-3) are knocked out, cat2-triggered glutathione oxidation is almost completely inhibited. Similar effects are observed in dhar1/dhar2 and dhar1/dhar2/dhar3 mutants using 3-AT to inhibit catalase. The major contribution to both lesion formation and glutathione oxidation triggered by catalase deficiency appears to come from DHAR1 and DHAR2 with a minor but significant contribution from chloroplastic DHAR3	Arabidopsis thaliana
malfunction	multiple loss of DHAR functions markedly decreases glutathione oxidation triggered by catalase deficiency. No evidence is obtained that either GRs or MDHARs are upregulated in plants lacking DHAR function. 3-Aminotriazole (3-AT) decreases catalase to very low levels while inducing ascorbate peroxidase (APX) and DHAR activities. These effects are accompanied by extensive leaf bleaching, and glutathione oxidation is evident as marked accumulation of GSSG. No difference is observed in bleaching or glutathione contents between the wild-type control and any of the mutants. Loss-of-function mutants for DHAR suggest that ascorbate regeneration is the major route leading to GSSG accumulation in response to intracellular H2O2. No effect on phenotype is observed in the absence of stress. When the different dhar mutant combinations are introduced into a catalase-deficient background (cat2), the combined presence of dhar1 and dhar2 decreased GSSG and total glutathione accumulation. When all 3 DHAR isozymes (DHAR1-3) are knocked out, cat2-triggered glutathione oxidation is almost completely inhibited. Similar effects were observed in dhar1/dhar2 and dhar1/dhar2/dhar3 mutants using 3-AT to inhibit catalase. The major contribution to both lesion formation and glutathione oxidation triggered by catalase deficiency appears to come from DHAR1 and DHAR2 with a minor but significant contribution from chloroplastic DHAR3	Arabidopsis thaliana
metabolism	glutathione is a pivotal molecule in oxidative stress, during which it is potentially oxidized by several pathways linked to H2O2 detoxification. Response and functional importance of 3 potential routes for glutathione oxidation pathways mediated by glutathione S-transferases (GST), glutaredoxin-dependent peroxiredoxins (PRXII), and dehydroascorbate reductases (DHAR) in Arabidopsis during oxidative stress, overview. Interplay between different DHARs appears to be necessary to couple ascorbate and glutathione pools and to allow glutathione-related signaling during enhanced H2O2 metabolism	Arabidopsis thaliana

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Release 2023.1 (January 2023)