Reactive oxygen species modulate the differential expression of methionine sulfoxide reductase genes inChlamydomonas reinhardtiiunder high light illumination

2013 ◽  
Vol 150 (4) ◽  
pp. 550-564 ◽  
Author(s):  
Hsueh-Ling Chang ◽  
Yu-Lu Tseng ◽  
Kuan-Lin Ho ◽  
Shu-Chiu Shie ◽  
Pei-Shan Wu ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Differential Expression ◽  
Reactive Oxygen ◽  
Methionine Sulfoxide ◽  
High Light ◽  
Methionine Sulfoxide Reductase ◽  
Light Illumination ◽  
Oxygen Species

scholarly journals Myristoylated methionine sulfoxide reductase A protects the heart from ischemia-reperfusion injury

2011 ◽  
Vol 301 (4) ◽  
pp. H1513-H1518 ◽  
Author(s):  
Hang Zhao ◽  
Junhui Sun ◽  
Anne M. Deschamps ◽  
Geumsoo Kim ◽  
Chengyu Liu ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Ischemia Reperfusion ◽  
Reactive Oxygen ◽  
Methionine Sulfoxide ◽  
Methionine Sulfoxide Reductase ◽  
Rate Pressure Product ◽  
Oxygen Species ◽  
Hydrophobic Domain ◽  
Methionine Sulfoxide Reductase A ◽  
Reperfusion Damage

Methionine sulfoxide reductase A (MsrA) catalytically scavenges reactive oxygen species and also repairs oxidized methionines in proteins. Increasing MsrA protects cells and organs from a variety of oxidative stresses while decreasing MsrA enhances damage, but the mechanisms of action have not been elucidated. A single gene encodes MsrA of which ∼25% is targeted to the mitochondria, a major site of reactive oxygen species production. The other ∼75% is targeted to the cytosol and is posttranslationally modified by myristoylation. To determine the relative importance of MsrA in each compartment in protecting against ischemia-reperfusion damage, we created a series of transgenic mice overexpressing MsrA targeted to the mitochondria or the cytosol. We used a Langendorff model of ischemia-reperfusion and assayed both the rate pressure product and infarct size following ischemia and reperfusion as measures of injury. While the mitochondrially targeted MsrA was expected to be protective, it was not. Notably, the cytosolic form was protective but only if myristoylated. The nonmyristoylated, cytosolic form offered no protection against injury. We conclude that cytosolic MsrA protects the heart from ischemia-reperfusion damage. The requirement for myristoylation suggests that MsrA must interact with a hydrophobic domain to provide protection.

scholarly journals DNA damage and reactive oxygen species cause cell death in the rice local lesions 1 mutant under high light and high temperature

2019 ◽  
Vol 222 (1) ◽  
pp. 349-365 ◽  
Author(s):  
Zhennan Qiu ◽  
Li Zhu ◽  
Lei He ◽  
Dongdong Chen ◽  
Dali Zeng ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Dna Damage ◽  
Cell Death ◽  
High Temperature ◽  
Reactive Oxygen ◽  
High Light ◽  
Oxygen Species ◽  
Local Lesions

scholarly journals Photosynthesis-independent production of reactive oxygen species in the rice bundle sheath during high light is mediated by NADPH oxidase

2021 ◽  
Vol 118 (25) ◽  
pp. e2022702118
Author(s):  
Haiyan Xiong ◽  
Lei Hua ◽  
Ivan Reyna-Llorens ◽  
Yi Shi ◽  
Kun-Ming Chen ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Nadph Oxidase ◽  
Messenger Rna ◽  
Photosynthetic Apparatus ◽  
Reactive Oxygen ◽  
Bundle Sheath ◽  
High Light ◽  
Oxygen Species ◽  
Mesophyll Cells ◽  
Excess Light

When exposed to high light, plants produce reactive oxygen species (ROS). In Arabidopsis thaliana, local stress such as excess heat or light initiates a systemic ROS wave in phloem and xylem cells dependent on NADPH oxidase/respiratory burst oxidase homolog (RBOH) proteins. In the case of excess light, although the initial local accumulation of ROS preferentially takes place in bundle-sheath strands, little is known about how this response takes place. Using rice and the ROS probes diaminobenzidine and 2′,7′-dichlorodihydrofluorescein diacetate, we found that, after exposure to high light, ROS were produced more rapidly in bundle-sheath strands than mesophyll cells. This response was not affected either by CO2 supply or photorespiration. Consistent with these findings, deep sequencing of messenger RNA (mRNA) isolated from mesophyll or bundle-sheath strands indicated balanced accumulation of transcripts encoding all major components of the photosynthetic apparatus. However, transcripts encoding several isoforms of the superoxide/H2O2-producing enzyme NADPH oxidase were more abundant in bundle-sheath strands than mesophyll cells. ROS production in bundle-sheath strands was decreased in mutant alleles of the bundle-sheath strand preferential isoform of OsRBOHA and increased when it was overexpressed. Despite the plethora of pathways able to generate ROS in response to excess light, NADPH oxidase–mediated accumulation of ROS in the rice bundle-sheath strand was detected in etiolated leaves lacking chlorophyll. We conclude that photosynthesis is not necessary for the local ROS response to high light but is in part mediated by NADPH oxidase activity.

scholarly journals The Oxidized Protein Repair Enzymes Methionine Sulfoxide Reductases and Their Roles in Protecting against Oxidative Stress, in Ageing and in Regulating Protein Function

Antioxidants ◽  
2018 ◽  
Vol 7 (12) ◽  
pp. 191 ◽  
Author(s):  
Sofia Lourenço dos Santos ◽  
Isabelle Petropoulos ◽  
Bertrand Friguet
Keyword(s):  
Oxidative Stress ◽  
Reactive Oxygen Species ◽  
Protein Function ◽  
Methionine Sulfoxide ◽  
Methionine Sulfoxide Reductase ◽  
Methionine Oxidation ◽  
Oxygen Species ◽  
Sulfenic Acid ◽  
Protein Repair ◽  
Methionine Sulfoxide Reductases

Cysteine and methionine residues are the amino acids most sensitive to oxidation by reactive oxygen species. However, in contrast to other amino acids, certain cysteine and methionine oxidation products can be reduced within proteins by dedicated enzymatic repair systems. Oxidation of cysteine first results in either the formation of a disulfide bridge or a sulfenic acid. Sulfenic acid can be converted to disulfide or sulfenamide or further oxidized to sulfinic acid. Disulfide can be easily reversed by different enzymatic systems such as the thioredoxin/thioredoxin reductase and the glutaredoxin/glutathione/glutathione reductase systems. Methionine side chains can also be oxidized by reactive oxygen species. Methionine oxidation, by the addition of an extra oxygen atom, leads to the generation of methionine sulfoxide. Enzymatically catalyzed reduction of methionine sulfoxide is achieved by either methionine sulfoxide reductase A or methionine sulfoxide reductase B, also referred as to the methionine sulfoxide reductases system. This oxidized protein repair system is further described in this review article in terms of its discovery and biologically relevant characteristics, and its important physiological roles in protecting against oxidative stress, in ageing and in regulating protein function.

scholarly journals The rice bundle sheath produces reactive oxygen species during high light stress via NADPH oxidase

2020 ◽  
Author(s):  
Haiyan Xiong ◽  
Lei Hua ◽  
Ivan Reyna-Llorens ◽  
Yi Shi ◽  
Kun-Ming Chen ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Nadph Oxidase ◽  
Light Stress ◽  
Photosynthetic Apparatus ◽  
Reactive Oxygen ◽  
Bundle Sheath ◽  
High Light ◽  
Ros Production ◽  
Oxygen Species ◽  
Mesophyll Cells

AbstractWhen exposed to high light plants produce reactive oxygen species (ROS). In Arabidopsis thaliana local accumulation of ROS preferentially takes place in bundle sheath strands, but little is known about how this response takes place. Using rice and the ROS probes diaminobenzidine and 2’,7’-dichlorodihydrofluorescein diacetate, we found that after exposure to high light, ROS were produced more rapidly in bundle sheath strands than mesophyll cells. This response was not affected either by CO2 supply or photorespiration. Consistent with these findings, deep sequencing of mRNA isolated from mesophyll or bundle sheath strands indicated balanced accumulation of transcripts encoding all major components of the photosynthetic apparatus. However, transcripts encoding several isoforms of the superoxide/H2O2-producing enzyme NADPH oxidase were more abundant in bundle sheath strands than mesophyll cells. ROS production in bundle sheath strands was reduced by blocking NADPH oxidase activity pharmacologically, but increased when the bundle sheath preferential RBOHA isoform of NADPH oxidase was over-expressed. NADPH oxidase mediated accumulation of ROS in the rice bundle sheath was detected in etiolated leaves lacking chlorophyll indicating that high light and NADPH oxidase-dependent ROS production is not dependent on photosynthesis.

scholarly journals Light-harvesting mutants show differential gene expression upon shift to high light as a consequence of photosynthetic redox and reactive oxygen species metabolism

2014 ◽  
Vol 369 (1640) ◽  
pp. 20130229 ◽  
Author(s):  
Mikko Tikkanen ◽  
Peter J. Gollan ◽  
Nageswara Rao Mekala ◽  
Janne Isojärvi ◽  
Eva-Mari Aro
Keyword(s):  
Gene Expression ◽  
Reactive Oxygen Species ◽  
Energy Transfer ◽  
Excitation Energy ◽  
Light Harvesting ◽  
Expression Profiles ◽  
Excitation Energy Transfer ◽  
Reactive Oxygen ◽  
High Light ◽  
Oxygen Species

The amount of light energy that is harvested and directed to the photosynthetic machinery is regulated in order to control the production of reactive oxygen species (ROS) in leaf tissues. ROS have important roles as signalling factors that instigate and mediate a range of cellular responses, suggesting that the mechanisms regulating light-harvesting and photosynthetic energy transduction also affect cell signalling. In this study, we exposed wild-type (WT) Arabidopsis and mutants impaired in the regulation of photosynthetic light-harvesting ( stn7 , tap38 and npq4 ) to transient high light (HL) stress in order to study the role of these mechanisms for up- and downregulation of gene expression under HL stress. The mutants, all of which have disturbed regulation of excitation energy transfer and distribution, responded to transient HL treatment with surprising similarity to the WT in terms of general ‘abiotic stress-regulated’ genes associated with hydrogen peroxide and 12-oxo-phytodienoic acid signalling. However, we identified distinct expression profiles in each genotype with respect to induction of singlet oxygen and jasmonic acid-dependent responses. The results of this study suggest that the control of excitation energy transfer interacts with hormonal regulation. Furthermore, the photosynthetic pigment–protein complexes appear to operate as receptors that sense the energetic balance between the photosynthetic light reactions and downstream metabolism.

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