Over-expression of chickpea glutaredoxin (CaGrx) provides tolerance to heavy metals by reducing metal accumulation and improved physiological and antioxidant defence system.
Antioxidants
/ metabolism
Arabidopsis
/ drug effects
Ascorbate Peroxidases
/ metabolism
Catalase
/ metabolism
Cicer
/ enzymology
Glutaredoxins
/ genetics
Glutathione
/ metabolism
Glutathione Peroxidase
/ metabolism
Glutathione Reductase
/ metabolism
Metals, Heavy
/ toxicity
Oxidative Stress
Oxidoreductases
/ metabolism
Superoxide Dismutase
/ metabolism
Antioxidant
Arabidopsis thaliana
Glutaredoxin
Glutathione
Heavy metals
ROS
Journal
Ecotoxicology and environmental safety
ISSN: 1090-2414
Titre abrégé: Ecotoxicol Environ Saf
Pays: Netherlands
ID NLM: 7805381
Informations de publication
Date de publication:
01 Apr 2020
01 Apr 2020
Historique:
received:
11
10
2019
revised:
23
01
2020
accepted:
24
01
2020
pubmed:
6
2
2020
medline:
15
5
2020
entrez:
5
2
2020
Statut:
ppublish
Résumé
Glutaredoxins (Grxs) are small multifunctional redox proteins. Grxs have glutathione-dependent oxidoreductase activity in the presence of glutathione reductase and NADPH. The role of Grxs is well studied in heavy metal tolerance in prokaryotic and mammalian systems but not in plant genera. In the present study, a chickpea glutaredoxin (CaGrx) gene (LOC101493651) has been investigated against metal stress based on its primary screening in chickpea which revealed higher up-regulation of CaGrx gene under various heavy metals (AsIII-25 μM, AsV-250 μM, Cr(VI)-300 μM, and Cd-500 μM) stress. This CaGrx gene was overexpressed in Arabidopsis thaliana and investigated various biochemical and physiological performances under each metal stress. Transgenic plants showed significant up-regulation of the CaGrx gene during qRT-PCR analysis as well as longer roots, higher seed germination, and survival efficiency during each metal stress. The levels of stress markers, TBARS, H
Identifiants
pubmed: 32014725
pii: S0147-6513(20)30091-9
doi: 10.1016/j.ecoenv.2020.110252
pii:
doi:
Substances chimiques
Antioxidants
0
Glutaredoxins
0
Metals, Heavy
0
Oxidoreductases
EC 1.-
Ascorbate Peroxidases
EC 1.11.1.11
Catalase
EC 1.11.1.6
Glutathione Peroxidase
EC 1.11.1.9
Superoxide Dismutase
EC 1.15.1.1
Glutathione Reductase
EC 1.8.1.7
glutathione dehydrogenase (ascorbate)
EC 1.8.5.1
Glutathione
GAN16C9B8O
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
110252Informations de copyright
Copyright © 2020 Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest This is to state that all the authors declare no conflict of interest.