scholarly journals Arabidopsis dehydroascorbate reductase 1 and 2 modulate redox states of ascorbate-glutathione cycle in the cytosol in response to photooxidative stress

2016 ◽  
Vol 81 (3) ◽  
pp. 523-533 ◽  
Author(s):  
Masahiro Noshi ◽  
Hiroki Yamada ◽  
Risa Hatanaka ◽  
Noriaki Tanabe ◽  
Masahiro Tamoi ◽  
...  
2018 ◽  
Vol 15 (2) ◽  
pp. 138-144
Author(s):  
I. M. Buzduga ◽  
R. A. Volkov ◽  
I. I. Panchuk

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


2016 ◽  
Vol 473 (6) ◽  
pp. 717-731 ◽  
Author(s):  
Pierre-Alexandre Lallement ◽  
Thomas Roret ◽  
Pascale Tsan ◽  
José M. Gualberto ◽  
Jean-Michel Girardet ◽  
...  

The resolution of a NMR structure of a poplar dehydroascorbate reductase (DHAR) coupled to kinetic analysis and GSSG-mediated oxidation treatments revealed that DHARs are highly specialized for dehydroascorbate reduction and adopt different redox states depending on the number of cysteine residues.


Genome ◽  
2005 ◽  
Vol 48 (5) ◽  
pp. 770-780 ◽  
Author(s):  
Wenchun Zhou ◽  
Frederic L Kolb ◽  
Dean E Riechers

Fusarium head blight (FHB) caused by Fusarium graminearum is a destructive disease of wheat and barley. It causes economic losses due to reduction in both yield and quality. Although FHB resistance has been well documented and resistant cultivars have been developed to reduce incidence and severity of FHB, there is a limited understanding of the molecular mechanisms involved in plant resistance against the infection and spread of F. graminearum. In the current study, 2-dimensional displays of proteins extracted from wheat spikelets infected with F. graminearum were compared with those from spikelets inoculated with sterile H2O. Fifteen protein spots were detected that were either induced (qualitatively different) or upregulated (quantitatively increased) following F. graminearum infection of spikelets of 'Ning7840', a resistant cultivar. These proteins were identified by LC-MS/MS analysis. Proteins with an antioxidant function such as superoxide dismutase, dehydroascorbate reductase, and glutathione S-transferases (GSTs) were upregulated or induced 5 d after inoculation with F. graminearum, indicating an oxidative burst of H2O2 inside the tissues infected by FHB. An ascorbate-glutathione cycle is likely involved in reduction of H2O2. Expression of proteins with highest similarity to dehydroascorbate reductase and TaGSTF5 (a glutathione S-transferase) differed following FHB infection in susceptible and resistant cultivars. A 14-3-3 protein homolog was also upregulated in FHB-infected spikelets. In addition, a PR-2 protein (β-1, 3 glucanase) was upregulated in FHB-infected spikes, which is in accord with a previous study that analyzed transcript accumulation.Key words: Fusarium head blight, scab, 2-dimensional electrophoresis, LC-MS/MS, protein, wheat, Triticum aestivum.


2009 ◽  
Vol 33 (4) ◽  
pp. 696-701
Author(s):  
Jian-Min MA ◽  
Lin-Lin CAI ◽  
Ling-Wei HU ◽  
Tong-Xia JIN ◽  
Xiao-Yu LI ◽  
...  

Author(s):  
Olivier Van Aken

Abstract Plant mitochondria are indispensable for plant metabolism and are tightly integrated into cellular homeostasis. This review provides an update on the latest research concerning the organisation and operation of plant mitochondrial redox systems, and how they affect cellular metabolism and signalling, plant development and stress responses. New insights into the organisation and operation of mitochondrial energy systems such as the tricarboxylic acid (TCA) cycle and mitochondrial electron chain (mtETC) are discussed. The mtETC produces reactive oxygen and nitrogen species, which can act as signals or lead to cellular damage, and are thus efficiently removed by mitochondrial antioxidant systems, including Mn-superoxide dismutase, ascorbate-glutathione cycle and thioredoxin-dependent peroxidases. Plant mitochondria are tightly connected with photosynthesis, photorespiration and cytosolic metabolism, thereby providing redox-balancing. Mitochondrial proteins are targets of extensive post-translational modifications, but their functional significance and how they are added or removed remains unclear. To operate in sync with the whole cell, mitochondria can communicate their functional status via mitochondrial retrograde signalling to change nuclear gene expression, and several recent breakthroughs here are discussed. At a whole organism level, plant mitochondria thus play crucial roles from the first minutes after seed imbibition, supporting meristem activity, growth and fertility, until senescence of darkened and aged tissue. Finally, plant mitochondria are tightly integrated with cellular and organismal responses to environmental challenges such as drought, salinity, heat and submergence, but also threats posed by pathogens. Both the major recent advances and outstanding questions are reviewed, which may help future research efforts on plant mitochondria.


2021 ◽  
Vol 26 (7) ◽  
pp. 763-774
Author(s):  
Ke Zuo ◽  
Henri-Baptiste Marjault ◽  
Kara L. Bren ◽  
Giulia Rossetti ◽  
Rachel Nechushtai ◽  
...  

AbstractThe NEET proteins constitute a unique class of [2Fe–2S] proteins. The metal ions bind to three cysteines and one histidine. The proteins’ clusters exist in two redox states; the oxidized protein (containing two FeIII ions) can transfer the cluster to apo-acceptor protein(s), while the reduced form (containing one ferrous ion) remains bound to the protein frame. Here, we perform in silico and in vitro studies on human NEET proteins in both reduced and oxidized forms. Quantum chemical calculations on all available human NEET proteins structures suggest that reducing the cluster weakens the Fe–NHis and Fe–SCys bonds, similar to what is seen in other Fe–S proteins (e.g., ferredoxin and Rieske protein). We further show that the extra electron in the [2Fe–2S]+ clusters of one of the NEET proteins (mNT) is localized on the His-bound iron ion, consistently with our previous spectroscopic studies. Kinetic measurements demonstrate that the mNT [2Fe–2S]+ is released only by an increase in temperature. Thus, the reduced state of human NEET proteins [2Fe–2S] cluster is kinetically inert. This previously unrecognized kinetic inertness of the reduced state, along with the reactivity of the oxidized state, is unique across all [2Fe–2S] proteins. Finally, using a coevolutionary analysis, along with molecular dynamics simulations, we provide insight on the observed allostery between the loop L2 and the cluster region. Specifically, we show that W75, R76, K78, K79, F82 and G85 in the latter region share similar allosteric characteristics in both redox states. Graphic abstract


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