scholarly journals Erratum: 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 ◽  
Conformational Flexibility ◽  
Dehydroascorbate Reductase

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.

scholarly journals Influence of sodium chloride on the dehydroascorbate reductase activity in Arabidopsis thaliana catalase 2 knokout mutant

2018 ◽  
Vol 15 (2) ◽  
pp. 138-144
Author(s):  
I. M. Buzduga ◽  
R. A. Volkov ◽  
I. I. Panchuk
Keyword(s):  
Arabidopsis Thaliana ◽  
Antioxidant Enzymes ◽  
Salt Stress ◽  
Sodium Chloride ◽  
Reductase Activity ◽  
Dehydroascorbate Reductase ◽  
Knock Out ◽  
Stress Treatment ◽  
Response To Stress ◽  
Glutathione Cycle

Aim. To better understand the mechanisms of abiotic stress resistance in plants, it is important to clarify the role of individual antioxidant enzymes from the same multiproteinic family in the response to stress. It is known that the loss of some isoforms of antioxidant enzymes can be compensated by activation of other enzymes. However, the functional interaction of the ascorbate-glutathione cycle enzymes with catalase under salt stress still remains unexplored. Respectively, we determined the activity of DHAR in knock-out mutants of Arabidopsis thaliana under salt stress. Methods. The DHAR activity was determined in the knock-out line cat2 and in wild-type (WT) Arabidopsis plants after various regimes of treatment with sodium chloride. Results. After treatment with 200 mM sodium chloride in the dark, activation of DHAR was found after 8 hours in WT plants and after 4 hours in the knock-out line cat2. However stress treatment under illumination resulted in significant increase in DHAR activity after 8 hours in both studied lines. In this case, DHAR activity in cat2 was lower than in WT, whereas in non-treated plants or upon stress treatment in the dark no difference between the tested lines was detected. Conclusions. The obtained data indicate that under salt stress conditions, changes in the DHAR activity are included into functional rearrangements of the antioxidant system in cat2 line, which compensate the loss of activity of CAT2 isoenzyme.Keywords: dehydroascorbate reductase, antioxidants, reactive oxygen species (ROS), salt stress, Arabidopsis thaliana

Stable genetic transformation of Arabidopsis thaliana by Agrobacterium inoculation in planta

1994 ◽  
Vol 5 (4) ◽  
pp. 551-558 ◽  
Author(s):  
Seok So Chang ◽  
Soon Ki Park ◽  
Byung Chul Kim ◽  
Bong Joong Kang ◽  
Dal Ung Kim ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Genetic Transformation ◽  
In Planta

The effect of daylength on the transition to flowering in phytochrome-deficient, late-flowering and double mutants of Arabidopsis thaliana

1995 ◽  
Vol 95 (2) ◽  
pp. 260-266 ◽  
Author(s):  
Maarten Koornneef ◽  
Corrie Hanhart ◽  
Patty van Loenen-Martinet ◽  
Hetty Blankestijn de Vries
Keyword(s):  
Arabidopsis Thaliana ◽  
Late Flowering ◽  
Transition To Flowering

Identification of a single-copy gene encoding a Type I chlorophyll a/b-binding polypeptide of photosystem I in Arabidopsis thaliana

1992 ◽  
Vol 84 (4) ◽  
pp. 561-567 ◽  
Author(s):  
Poul E. Jensen ◽  
Michael Kristensen ◽  
Tine Hoff ◽  
Jan Lehmbeck ◽  
Bjarne M. Stummann ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Chlorophyll A ◽  
Photosystem I ◽  
Single Copy ◽  
Type I ◽  
Single Copy Gene ◽  
Gene Encoding ◽  
Copy Gene

Ammonium uptake and cellular alkalisation in roots of Arabidopsis thaliana: The involvement of cytoplasmic calcium

2000 ◽  
Vol 110 (4) ◽  
pp. 518 ◽  
Author(s):  
Christoph Plieth ◽  
Burkhard Sattelmacher ◽  
Marc R. Knight
Keyword(s):  
Arabidopsis Thaliana ◽  
Ammonium Uptake ◽  
Cytoplasmic Calcium

Flavonoid profiling by LC-MS IN 14 – 3-3ν knockout mutants of Arabidopsis thaliana during drought stress conditions

Planta Medica ◽  
2014 ◽  
Vol 80 (10) ◽  
Author(s):  
F Nabbie ◽  
O Shperdheja ◽  
J Millot ◽  
J Lindberg ◽  
B Peethambaran
Keyword(s):  
Arabidopsis Thaliana ◽  
Drought Stress ◽  
Stress Conditions ◽  
Knockout Mutants
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