Characterisation of a Zeta Class Glutathione Transferase from Arabidopsis thaliana with a Putative Role in Tyrosine Catabolism

2000 ◽  
Vol 384 (2) ◽  
pp. 407-412 ◽  
Author(s):  
David P Dixon ◽  
David J Cole ◽  
Robert Edwards
Keyword(s):  
Arabidopsis Thaliana ◽  
Glutathione Transferase ◽  
Putative Role

Dehydrin ERD14 activates glutathione transferase Phi9 in Arabidopsis thaliana under osmotic stress

2020 ◽  
Vol 1864 (3) ◽  
pp. 129506 ◽  
Author(s):  
Phuong N. Nguyen ◽  
Maria-Armineh Tossounian ◽  
Denes S. Kovacs ◽  
Tran T. Thu ◽  
Benoit Stijlemans ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Osmotic Stress ◽  
Glutathione Transferase

scholarly journals Exogenous salicylic acid-triggered changes in the glutathione transferases and peroxidases are key factors in the successful salt stress acclimation of Arabidopsis thaliana

2015 ◽  
Vol 42 (12) ◽  
pp. 1129 ◽  
Author(s):  
Edit Horváth ◽  
Szilvia Brunner ◽  
Krisztina Bela ◽  
Csaba Papdi ◽  
László Szabados ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Salicylic Acid ◽  
Salt Stress ◽  
Glutathione Transferase ◽  
Nacl Stress ◽  
Guaiacol Peroxidase ◽  
Stress Injury ◽  
Stress Acclimation ◽  
Enhanced Expression ◽  
Sequential Treatments

Salicylic acid (SA) applied exogenously is a potential priming agent during abiotic stress. In our experiments, the priming effect of SA was tested by exposing Arabidopsis thaliana (L.) Heynh. plants to 2-week-long 10−9–10−5 M SA pretreatments in a hydroponic medium, followed by 1 week of 100 mM NaCl stress. The levels of reactive oxygen species and H2O2, changes in antioxidant enzyme activity and the expression of selected glutathione transferase (GST) genes were investigated. Although 10−9–10−7 M SA pretreatment insufficiently induced defence mechanisms during the subsequent salt stress, 2-week pretreatments with 10−6 and 10−5 M SA alleviated the salinity-induced H2O2 and malondialdehyde accumulation, and increased superoxide dismutase, guaiacol peroxidase, GST and glutathione peroxidase (GPOX) activity. Our results indicate that long-term 10−6 and 10−5 M SA treatment mitigated the salt stress injury in this model plant. Enhanced expression of AtGSTU19 and AtGSTU24 may be responsible for the induced GST and GPOX activity, which may play an important role in acclimation. Modified GST expression suggested altered signalling in SA-hardened plants during salt stress. The hydroponic system applied in our experiments proved to be a useful tool for studying the effects of sequential treatments in A. thaliana.

scholarly journals Redox‐regulated methionine oxidation of Arabidopsis thaliana glutathione transferase Phi9 induces H‐site flexibility

2018 ◽  
Author(s):  
Maria‐Armineh Tossounian ◽  
Khadija Wahni ◽  
Inge Van Molle ◽  
Didier Vertommen ◽  
Leonardo Astolfi Rosado ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Glutathione Transferase ◽  
Methionine Oxidation

scholarly journals Disulfide bond formation protects Arabidopsis thaliana glutathione transferase tau 23 from oxidative damage

2018 ◽  
Vol 1862 (3) ◽  
pp. 775-789 ◽  
Author(s):  
Maria-Armineh Tossounian ◽  
Inge Van Molle ◽  
Khadija Wahni ◽  
Silke Jacques ◽  
Kris Gevaert ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Oxidative Damage ◽  
Disulfide Bond ◽  
Glutathione Transferase ◽  
Bond Formation ◽  
Disulfide Bond Formation

scholarly journals Arabidopsis thaliana dehydroascorbate reductase 2: Conformational flexibility during catalysis

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Nandita Bodra ◽  
David Young ◽  
Leonardo Astolfi Rosado ◽  
Anna Pallo ◽  
Khadija Wahni ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Active Site ◽  
Glutathione Transferase ◽  
Normal Mode Analysis ◽  
Conformational Flexibility ◽  
Dehydroascorbate Reductase ◽  
Mode Analysis ◽  
Direct Role ◽  
Active Site Motif ◽  
Catalytic Cysteine

Abstract Dehydroascorbate reductase (DHAR) catalyzes the glutathione (GSH)-dependent reduction of dehydroascorbate and plays a direct role in regenerating ascorbic acid, an essential plant antioxidant vital for defense against oxidative stress. DHAR enzymes bear close structural homology to the glutathione transferase (GST) superfamily of enzymes and contain the same active site motif, but most GSTs do not exhibit DHAR activity. The presence of a cysteine at the active site is essential for the catalytic functioning of DHAR, as mutation of this cysteine abolishes the activity. Here we present the crystal structure of DHAR2 from Arabidopsis thaliana with GSH bound to the catalytic cysteine. This structure reveals localized conformational differences around the active site which distinguishes the GSH-bound DHAR2 structure from that of DHAR1. We also unraveled the enzymatic step in which DHAR releases oxidized glutathione (GSSG). To consolidate our structural and kinetic findings, we investigated potential conformational flexibility in DHAR2 by normal mode analysis and found that subdomain mobility could be linked to GSH binding or GSSG release.

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