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Methionine Oxidation - DOAJ

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Last Updated: 13 May 2022

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Susceptibility of Protein Methionine Oxidation in Response to Hydrogen Peroxide Treatment–Ex Vivo Versus In Vitro: A Computational Insight

Methionine oxidation is a key component of cell signaling. We recently developed a database containing thousands of proteins that have been identified as sulfoxidation targets. Proteins oxidized in both cell-free and inside living cells were rich in methionines and intrinsically disordered regions, which we discovered. However, proteins that oxidized ex vivo were larger and less abundant than those that were oxidized in vitro. In a network based on gene ontology networks, the nodes corresponding with ex vivo and in vitro oxidized proteins showed an associative mixing, implying that ex vivo oxidized proteins were present in various biological functions and biological processes. Proteins from the ex vivo set were co-regulated more often than anticipated by chance, according to this report. We also investigated the sequence of oxidation sites. In comparison, tyrosine, tryptophan, and histidine were practically forbidden, but only in the ex vivo sites.

Source link: https://doi.org/10.3390/antiox9100987


Time-course proteomics dataset to monitor protein-bound methionine oxidation in Bacillus cereus ATCC 14579

ROS convert protein-bound methionine residues into methionine sulfoxide, which converts protein-bound methionine residues into methionine sulfoxide. Methionine sulfoxide reductases reduce the oxidation of methionine sulfoxide to methionine in proteins by methionine sulfoxide reductases. BRClin15 and its variant, for which the methionine sulfoxide reductase AB gene has been activated, has been activated, are listed [1]. Given the importance of methionine oxidation in several key cell processes and its impact on medical and food microbiology, this paper may be helpful for more comprehensive redox studies in B. cereus and its many relatives.

Source link: https://doi.org/10.1016/j.dib.2018.03.030


Structural and functional characteristics of cGMP-dependent methionine oxidation in Arabidopsis thaliana proteins

Background information: Post-translational methionine oxidation of proteins is not limited to cell injury, but it can provide the cell with insight into the cell's cellular oxidative status. In addition, previous research shows that oxidation of methionine residues in signaling molecules may play a role in stress responses because these specific structural changes can in turn change protein biological functions. Findings Here we use tandem mass spectrometry-based proteomics to show that treating Arabidopsis thaliana cells with a non-oxidative signaling molecule, the cell-permeant second messenger analogue, 8-bromo-3,5-cyclic phosphate, results in a time-dependent rise in the amount of oxidised methionine residues. Interestingly, the group of proteins impacted by cGMP-dependent methionine oxidation is specifically enriched for stress response proteins.

Source link: https://doi.org/10.1186/1478-811X-11-1


Effect of Methionine Oxidation and Substitution of α-Conotoxin TxID on α3β4 Nicotinic Acetylcholine Receptor

However, TxID is vulnerable to change because of a methionine residue that easily produces methionine sulfoxide in an oxidative environment. The results revealed that most TxID analogues had substantially reduced activity on α3β4 nAChR, with more than 10-fold potency loss, and 5 of them showed no resistance to α3β4 nAChR, with more than 10-fold potency loss, and 5 of them had no inhibition on α3β4 nAChR;3β4 nAChR Met's replacement in TxID with a hydrophobic moderate-sized Ile is an alternative to minimize Met oxidation's effects, according to the results, which may help to restore conotoxins containing methionine residues.

Source link: https://doi.org/10.3390/md16060215


A machine learning approach for predicting methionine oxidation sites

Background Information The oxidation of protein-bound methionine to produce methionine sulfoxide has traditionally been thought of as an oxidative threat. Some proteomic research has arisen after the finding that methionine sulfoxidation can be a key to the redox regulation of a variety of biological processes. In addition, computational techniques developed to forecast methionine oxidation sites are a popular alternative. Among the most notable properties were the solvent accessible area of the methionine residue, the number of residues between the analyzed methionine and the next methionine, which culminated towards the N-terminus, and the spatial distance between the atom of sulfur from the analyzed methionine and the nearest aromatic residue. Conclusions We present the first predictive models that can be used to analyze methionine sites in vivo that can become oxidized in vivo as a result of oxidative signals. These models provide insight into the cultural context in which a methionine residue becomes either oxidation-resistant or oxidation-prone.

Source link: https://doi.org/10.1186/s12859-017-1848-9

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions

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* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions