scholarly journals Physiological Roles of Plant Methionine Sulfoxide Reductases in Redox Homeostasis and Signaling

Antioxidants ◽  
2018 ◽  
Vol 7 (9) ◽  
pp. 114 ◽  
Author(s):  
Pascal Rey ◽  
Lionel Tarrago
Keyword(s):  
Current Knowledge ◽  
Expression Patterns ◽  
Redox Homeostasis ◽  
Methionine Sulfoxide ◽  
Protective Role ◽  
Crop Species ◽  
Related Information ◽  
Methionine Sulfoxide Reductases ◽  
Oxidation Of Methionine ◽  
Mutant Phenotypes

Oxidation of methionine (Met) leads to the formation of two S- and R-diastereoisomers of Met sulfoxide (MetO) that are reduced back to Met by methionine sulfoxide reductases (MSRs), A and B, respectively. Here, we review the current knowledge about the physiological functions of plant MSRs in relation with subcellular and tissue distribution, expression patterns, mutant phenotypes, and possible targets. The data gained from modified lines of plant models and crop species indicate that MSRs play protective roles upon abiotic and biotic environmental constraints. They also participate in the control of the ageing process, as shown in seeds subjected to adverse conditions. Significant advances were achieved towards understanding how MSRs could fulfil these functions via the identification of partners among Met-rich or MetO-containing proteins, notably by using redox proteomic approaches. In addition to a global protective role against oxidative damage in proteins, plant MSRs could specifically preserve the activity of stress responsive effectors such as glutathione-S-transferases and chaperones. Moreover, several lines of evidence indicate that MSRs fulfil key signaling roles via interplays with Ca2+- and phosphorylation-dependent cascades, thus transmitting ROS-related information in transduction pathways.

scholarly journals Peptide-Bound Methionine Sulfoxide (MetO) Levels and MsrB2 Abundance Are Differentially Regulated during the Desiccation Phase in Contrasted Acer Seeds

Antioxidants ◽  
2020 ◽  
Vol 9 (5) ◽  
pp. 391 ◽  
Author(s):  
Natalia Wojciechowska ◽  
Shirin Alipour ◽  
Ewelina Stolarska ◽  
Karolina Bilska ◽  
Pascal Rey ◽  
...  
Keyword(s):  
Desiccation Tolerance ◽  
Methionine Sulfoxide ◽  
Redox Status ◽  
Embryonic Axes ◽  
Seed Desiccation ◽  
Methionine Sulfoxide Reductases ◽  
Norway Maple ◽  
Orthodox Seeds ◽  
Oxidation Of Methionine ◽  
Reduced Forms

Norway maple and sycamore produce desiccation-tolerant (orthodox) and desiccation-sensitive (recalcitrant) seeds, respectively. Drying affects reduction and oxidation (redox) status in seeds. Oxidation of methionine to methionine sulfoxide (MetO) and reduction via methionine sulfoxide reductases (Msrs) have never been investigated in relation to seed desiccation tolerance. MetO levels and the abundance of Msrs were investigated in relation to levels of reactive oxygen species (ROS) such as hydrogen peroxide, superoxide anion radical and hydroxyl radical (•OH), and the levels of ascorbate and glutathione redox couples in gradually dried seeds. Peptide-bound MetO levels were positively correlated with ROS concentrations in the orthodox seeds. In particular, •OH affected MetO levels as well as the abundance of MsrB2 solely in the embryonic axes of Norway maple seeds. In this species, MsrB2 was present in oxidized and reduced forms, and the latter was favored by reduced glutathione and ascorbic acid. In contrast, sycamore seeds accumulated higher ROS levels. Additionally, MsrB2 was oxidized in sycamore throughout dehydration. In this context, the three elements •OH level, MetO content and MsrB2 abundance, linked together uniquely to Norway maple seeds, might be considered important players of the redox network associated with desiccation tolerance.

scholarly journals Involvement of the MetO/Msr System in Two Acer Species That Display Contrasting Characteristics during Germination

2020 ◽  
Vol 21 (23) ◽  
pp. 9197
Author(s):  
Natalia Wojciechowska ◽  
Shirin Alipour ◽  
Ewelina Stolarska ◽  
Karolina Bilska ◽  
Pascal Rey ◽  
...  
Keyword(s):  
Hydroxyl Radicals ◽  
Superoxide Anion ◽  
Redox Homeostasis ◽  
Methionine Sulfoxide ◽  
Redox System ◽  
Oxygen Species ◽  
Embryonic Axes ◽  
Methionine Sulfoxide Reductases ◽  
Germination Process ◽  
Norway Maple

The levels of methionine sulfoxide (MetO) and the abundances of methionine sulfoxide reductases (Msrs) were reported as important for the desiccation tolerance of Acer seeds. To determine whether the MetO/Msrs system is related to reactive oxygen species (ROS) and involved in the regulation of germination in orthodox and recalcitrant seeds, Norway maple and sycamore were investigated. Changes in water content, MetO content, the abundance of MsrB1 and MsrB2 in relation to ROS content and the activity of reductases depending on nicotinamide adenine dinucleotides were monitored. Acer seeds differed in germination speed—substantially higher in sycamore—hydration dynamics, levels of hydrogen peroxide, superoxide anion radicals (O2•−) and hydroxyl radicals (•OH), which exhibited peaks at different stages of germination. The MetO level dynamically changed, particularly in sycamore embryonic axes, where it was positively correlated with the levels of O2•− and the abundance of MsrB1 and negatively with the levels of •OH and the abundance of MsrB2. The MsrB2 abundance increased upon sycamore germination; in contrast, it markedly decreased in Norway maple. We propose that the ROS–MetO–Msr redox system, allowing balanced Met redox homeostasis, participates in the germination process in sycamore, which is characterized by a much higher speed compared to Norway maple.

scholarly journals In Vivo Effects of Methionine Sulfoxide Reductase Deficiency in Drosophila melanogaster

Antioxidants ◽  
2018 ◽  
Vol 7 (11) ◽  
pp. 155 ◽  
Author(s):  
Lindsay Bruce ◽  
Diana Singkornrat ◽  
Kelsey Wilson ◽  
William Hausman ◽  
Kelli Robbins ◽  
...  
Keyword(s):  
Methionine Sulfoxide ◽  
Methionine Sulfoxide Reductase ◽  
Model Organisms ◽  
Methionine Sulfoxide Reductase A ◽  
Methionine Sulfoxide Reductases ◽  
Methionine Residues ◽  
Oxidation Of Methionine ◽  
And Function ◽  
In Vivo Effects

The deleterious alteration of protein structure and function due to the oxidation of methionine residues has been studied extensively in age-associated neurodegenerative disorders such as Alzheimer’s and Parkinson’s Disease. Methionine sulfoxide reductases (MSR) have three well-characterized biological functions. The most commonly studied function is the reduction of oxidized methionine residues back into functional methionine thus, often restoring biological function to proteins. Previous studies have successfully overexpressed and silenced MSR activity in numerous model organisms correlating its activity to longevity and oxidative stress. In the present study, we have characterized in vivo effects of MSR deficiency in Drosophila. Interestingly, we found no significant phenotype in animals lacking either methionine sulfoxide reductase A (MSRA) or methionine sulfoxide reductase B (MSRB). However, Drosophila lacking any known MSR activity exhibited a prolonged larval third instar development and a shortened lifespan. These data suggest an essential role of MSR in key biological processes.

scholarly journals Methionine Redox Homeostasis in Protein Quality Control

2021 ◽  
Vol 8 ◽  
Author(s):  
Laurent Aussel ◽  
Benjamin Ezraty
Keyword(s):  
Oxidative Stress ◽  
Quality Control ◽  
Protein Function ◽  
Protein Quality ◽  
Redox Homeostasis ◽  
Protein Quality Control ◽  
Methionine Sulfoxide ◽  
Methionine Sulfoxide Reductases ◽  
Methionine Residues ◽  
And Function

Bacteria live in different environments and are subject to a wide variety of fluctuating conditions. During evolution, they acquired sophisticated systems dedicated to maintaining protein structure and function, especially during oxidative stress. Under such conditions, methionine residues are converted into methionine sulfoxide (Met-O) which can alter protein function. In this review, we focus on the role in protein quality control of methionine sulfoxide reductases (Msr) which repair oxidatively protein-bound Met-O. We discuss our current understanding of the importance of Msr systems in rescuing protein function under oxidative stress and their ability to work in coordination with chaperone networks. Moreover, we highlight that bacterial chaperones, like GroEL or SurA, are also targeted by oxidative stress and under the surveillance of Msr. Therefore, integration of methionine redox homeostasis in protein quality control during oxidative stress gives a complete picture of this bacterial adaptive mechanism.

scholarly journals The Role of Methionine Sulfoxide Reductases in Oxidative Stress Tolerance and Virulence of Staphylococcus aureus and Other Bacteria

Antioxidants ◽  
2018 ◽  
Vol 7 (10) ◽  
pp. 128 ◽  
Author(s):  
Vineet Singh ◽  
Kuldeep Singh ◽  
Kyle Baum
Keyword(s):  
Oxidative Stress ◽  
Staphylococcus Aureus ◽  
Cell Wall ◽  
Regulatory Network ◽  
Current Knowledge ◽  
Methionine Sulfoxide ◽  
Oxidative Stress Tolerance ◽  
Methionine Sulfoxide Reductases ◽  
Encoding Genes

Methionine sulfoxide reductases (MSRA1 and MSRB) are proteins overproduced in Staphylococcus aureus during exposure with cell wall-active antibiotics. Later studies identified the presence of two additional MSRA proteins (MSRA2 and MSRA3) in S. aureus. These MSR proteins have been characterized in many other bacteria as well. This review provides the current knowledge about the conditions and regulatory network that mimic the expression of these MSR encoding genes and their role in defense from oxidative stress and virulence.

scholarly journals Methionine Sulfoxide Reductases Contribute to Anaerobic Fermentative Metabolism in Bacillus cereus

Antioxidants ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 819
Author(s):  
Catherine Duport ◽  
Jean-Paul Madeira ◽  
Mahsa Farjad ◽  
Béatrice Alpha-Bazin ◽  
Jean Armengaud
Keyword(s):  
Bacillus Cereus ◽  
Oxidant Stress ◽  
Physiological Role ◽  
Methionine Sulfoxide ◽  
Wild Type ◽  
Fermentative Metabolism ◽  
Methionine Sulfoxide Reductases ◽  
Mutant Strains ◽  
Oxidation Of Methionine

Reversible oxidation of methionine to methionine sulfoxide (Met(O)) is a common posttranslational modification occurring on proteins in all organisms under oxic conditions. Protein-bound Met(O) is reduced by methionine sulfoxide reductases, which thus play a significant antioxidant role. The facultative anaerobe Bacillus cereus produces two methionine sulfoxide reductases: MsrA and MsrAB. MsrAB has been shown to play a crucial physiological role under oxic conditions, but little is known about the role of MsrA. Here, we examined the antioxidant role of both MsrAB and MrsA under fermentative anoxic conditions, which are generally reported to elicit little endogenous oxidant stress. We created single- and double-mutant Δmsr strains. Compared to the wild-type and ΔmsrAB mutant, single- (ΔmsrA) and double- (ΔmsrAΔmsrAB) mutants accumulated higher levels of Met(O) proteins, and their cellular and extracellular Met(O) proteomes were altered. The growth capacity and motility of mutant strains was limited, and their energy metabolism was altered. MsrA therefore appears to play a major physiological role compared to MsrAB, placing methionine sulfoxides at the center of the B. cereus antioxidant system under anoxic fermentative conditions.

scholarly journals Pharmacological Targeting of Heme Oxygenase-1 in Osteoarthritis

Antioxidants ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. 419
Author(s):  
Yohei Sanada ◽  
Sho Joseph Ozaki Tan ◽  
Nobuo Adachi ◽  
Shigeru Miyaki
Keyword(s):  
Heme Oxygenase ◽  
Redox Homeostasis ◽  
Synovial Fibroblasts ◽  
Protective Role ◽  
Joint Disease ◽  
Heme Oxygenase 1 ◽  
Transcriptional Level ◽  
Related Factor ◽  
Mobility Limitations ◽  
Therapeutic Implications

Osteoarthritis (OA) is a common aging-associated disease that clinically manifests as joint pain, mobility limitations, and compromised quality of life. Today, OA treatment is limited to pain management and joint arthroplasty at the later stages of disease progression. OA pathogenesis is predominantly mediated by oxidative damage to joint cartilage extracellular matrix and local cells such as chondrocytes, osteoclasts, osteoblasts, and synovial fibroblasts. Under normal conditions, cells prevent the accumulation of reactive oxygen species (ROS) under oxidatively stressful conditions through their adaptive cytoprotective mechanisms. Heme oxygenase-1 (HO-1) is an iron-dependent cytoprotective enzyme that functions as the inducible form of HO. HO-1 and its metabolites carbon monoxide and biliverdin contribute towards the maintenance of redox homeostasis. HO-1 expression is primarily regulated at the transcriptional level through transcriptional factor nuclear factor erythroid 2 (NF-E2)-related factor 2 (Nrf2), specificity protein 1 (Sp1), transcriptional repressor BTB-and-CNC homology 1 (Bach1), and epigenetic regulation. Several studies report that HO-1 expression can be regulated using various antioxidative factors and chemical compounds, suggesting therapeutic implications in OA pathogenesis as well as in the wider context of joint disease. Here, we review the protective role of HO-1 in OA with a focus on the regulatory mechanisms that mediate HO-1 activity.

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