Methionine Redox Homeostasis in Protein Quality Control

Aussel, Laurent; Ezraty, Benjamin

doi:10.3389/fmolb.2021.665492

Cited by 16 publications

(19 citation statements)

References 48 publications

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“…Despite the progress in deciphering possible interactions between Met sulfoxidation and protein carbonylation or protein phosphorylation [27,[95][96][97], the molecular mechanisms coupling oxidative signals to changes in phosphorylation in seeds still remain poorly understood. Interestingly, two of identified proteins containing oxidized Met and a phosphorylation site corresponded to an elongation factor and an inhibitor of serine proteases (Table 2), and were previously demonstrated to be substrates for MSRB1 [23] and periplasmic MSR [98], respectively. Hence, 2Dd-CNBr-based results might provide initial information toward a better understanding of the interplay between different types of post-translational protein modifications in targeted proteins.…”

Section: Discussionmentioning

confidence: 95%

Are Methionine Sulfoxide-Containing Proteins Related to Seed Longevity? A Case Study of Arabidopsis thaliana Dry Mature Seeds Using Cyanogen Bromide Attack and Two-Dimensional-Diagonal Electrophoresis

Kalemba

Valot

Job

et al. 2022

Plants

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In recent years, several reports pointed out the role of protein oxidation in seed longevity, notably regarding the oxidation of methionine (Met) residues to methionine sulfoxide (MetO) in proteins. To further consider this question, we present a handy proteomic method based on the use of two-dimensional diagonal electrophoresis (2Dd) and cyanogen bromide (CNBr) cleavage, which we refer to as 2Dd-CNBr. CNBr treatment of proteins causes the non-enzymatic hydrolysis of peptide bonds on the carboxyl side of reduced Met residues. However, Met oxidation causes a lack of cleavage, thus modifying the electrophoretic mobility of CNBr-induced peptides. This approach was first validated using bovine serum albumin as a model protein, which confirmed the possibility of distinguishing between oxidized and non-oxidized forms of Met-containing peptides in gels. Then, the 2Dd-CNBr method was applied to the Arabidopsis thaliana seed protein extract in a control (non-oxidized) condition and in an oxidized one (as obtained following hypochlorous acid treatment). Twenty-four oxidized Met residues in 19 proteins identified by mass spectrometry were found to be surface exposed in these proteins. In the three-dimensional environment of the oxidized Met, we detected amino acid residues that could be converted by oxidation (carbonylation) or by phosphorylation, suggesting a possible interplay between Met oxidation and the other protein modifications. The identification of the proteins oxidatively modified in Met residues revealed the finding that MetO-containing proteins are related to seed longevity. Based on these results, we suggest that the method presently described also has the potential for wider applications.

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Section: Discussionmentioning

confidence: 95%

Are Methionine Sulfoxide-Containing Proteins Related to Seed Longevity? A Case Study of Arabidopsis thaliana Dry Mature Seeds Using Cyanogen Bromide Attack and Two-Dimensional-Diagonal Electrophoresis

Kalemba

Valot

Job

et al. 2022

Plants

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“…Moreover, the PPO gene downregulation was observed for the melatonin-treated litchi samples. On the contrary, several studies have shown that the Msr-related genes regulated oxidative stress by mediating sulfoxylation of methionine, participated in the redox regulation in the organisms ( Jiang et al, 2017 , 2018 ; Moskovitz and Smith, 2021 ), and also repaired oxidatively damaged protein ( Aussel and Ezraty, 2021 ; Xiao et al, 2021b ).…”

Section: Discussionmentioning

confidence: 99%

Melatonin treatment improves postharvest quality and regulates reactive oxygen species metabolism in “Feizixiao” litchi based on principal component analysis

et al. 2022

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Postharvest quality of litchi reduces rapidly during storage at room temperature. This study aimed to investigate the effect of melatonin treatment on postharvest quality and oxidative stress markers of litchi fruit during cold storage. The “Feizixiao” litchi was treated with melatonin solution concentrations of 0.2 and 0.6 mmol·L−1 and then stored at 4°C for 12 days. The results confirmed that the melatonin treatment effectively maintained the appearance and color of the litchi fruit, suppressed the peel browning, and improved the litchi quality. The treatment also significantly enhanced the levels of endogenous melatonin, antioxidant components (total phenolics, flavonoids, and anthocyanin), and antioxidant enzyme activities of the fruit. It also inhibited the other oxidative stress markers, such as O2−, H2O2, MDA, and protein carbonyl content, and upregulated the expressions of antioxidant and Msr-related genes. Correlation and principal component analyses further confirmed that the melatonin treatment effectively delayed the fruit senescence by enhancing the antioxidant enzyme activities and modulating peel browning and reactive oxygen species metabolism of the litchi fruit via regulating gene expression of the related enzymes (SOD and PPO). These findings suggested that the exogenous application of melatonin to litchi during the postharvest is an ideal way to preserve the fruit quality and delay fruit senescence.

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“…The pivotal role of methionine sulfoxide reductases in protecting living cells from oxidative stress has long been recognized; however, the role of these enzymes in enhancing the survival of bacterial pathogens in the host is still not fully understood [ 1 , 2 , 3 , 4 ]. Bacterial pathogens inhabit an environment that promotes oxidative stress, in which enzymes of the host innate immune response such as NADPH oxidase, superoxide dismutase and myeloperoxidase produce superoxide radicals, hydrogen peroxide and hypochlorite, respectively [ 5 ].…”

Section: Introductionmentioning

confidence: 99%

“…Oxidation of methionine residues can lead to a loss of biological function by disrupting protein structure, and methionine sulfoxide reductases are required to reverse oxidative damage to free and protein-bound methionine residues [ 1 , 2 ]. The cytoplasmic peptide-methionine sulfoxide reductases MsrA and MsrB that use a thiol-based redox relay for catalysis and reduce the S- and R- stereoisomers of methionine sulfoxide (MetSO), respectively, are particularly well studied [ 2 , 3 , 6 ]. However, periplasmic or outer-membrane-associated methionine sulfoxide reductases have recently been shown to play a pivotal role in protecting various bacterial pathogens from exogenous oxidative stress.…”

Section: Introductionmentioning

confidence: 99%

The Peptide Methionine Sulfoxide Reductase (MsrAB) of Haemophilus influenzae Repairs Oxidatively Damaged Outer Membrane and Periplasmic Proteins Involved in Nutrient Acquisition and Virulence

et al. 2022

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Sulfoxide-damage repair mechanisms are emerging as essential for the virulence of bacterial pathogens, and in the human respiratory pathogen Haemophilus influenzae the periplasmic MsrAB peptide methionine sulfoxide reductase is necessary for resistance to reactive chlorine species such as hypochlorite. Additionally, this enzyme has a role in modulating the host immune response to infection. Here, we have analysed the enzymatic properties of MsrAB, which revealed that both domains of the protein are catalytically active, with the turnover number of the MsrA domain being 50% greater than that for the MsrB domain. MsrAB was active with small molecular sulfoxides as well as oxidised calmodulin, and maximal activity was observed at 30°C, a temperature close to that found in the natural niche of H. influenzae, the nasopharynx. Analyses of differential methionine oxidation identified 29 outer membrane and periplasmic proteins that are likely substrates for MsrAB. These included the LldD lactate dehydrogenase and the lipoprotein eP4 that is involved in NAD and hemin metabolism in H. influenzae. Subsequent experiments showed that H. influenzae MsrAB can repair oxidative damage to methionines in purified eP4 with up to 100% efficiency. Our work links MsrAB to the maintenance of different adhesins and essential metabolic processes in the H. influenzae, such as NAD metabolism and access to L-lactate, which is a key growth substrate for H. influenzae during infection.

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Methionine Redox Homeostasis in Protein Quality Control

Cited by 16 publications

References 48 publications

Are Methionine Sulfoxide-Containing Proteins Related to Seed Longevity? A Case Study of Arabidopsis thaliana Dry Mature Seeds Using Cyanogen Bromide Attack and Two-Dimensional-Diagonal Electrophoresis

Are Methionine Sulfoxide-Containing Proteins Related to Seed Longevity? A Case Study of Arabidopsis thaliana Dry Mature Seeds Using Cyanogen Bromide Attack and Two-Dimensional-Diagonal Electrophoresis

Melatonin treatment improves postharvest quality and regulates reactive oxygen species metabolism in “Feizixiao” litchi based on principal component analysis

The Peptide Methionine Sulfoxide Reductase (MsrAB) of Haemophilus influenzae Repairs Oxidatively Damaged Outer Membrane and Periplasmic Proteins Involved in Nutrient Acquisition and Virulence

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