Aix-Marseille Univ, CNRS, Laboratoire de Chimie Bactérienne, Institut de Microbiologie de la Méditerranée, Marseille, France. Electronic address:
Published: November 2020
AI Article Synopsis
Article Abstract
The oxidation of free methionine (Met) and Met residues inside proteins leads to the formation of methionine sulfoxide (Met-O). The reduction of Met-O to Met is catalysed by a ubiquitous enzyme family: the methionine sulfoxide reductases (Msr). The importance of Msr systems in bacterial physiology and virulence has been reported in many species. Salmonella Typhimurium, a facultative intracellular pathogen, contains four cytoplasmic Msr. Recently, a periplasmic Msr enzyme (MsrP) has been identified in Escherichia coli. In the present study, the STM14_4072 gene from Salmonella was shown to encode the MsrP protein (StMsrP). We describe the experimental procedure and precautions for the production of this molybdo-enzyme. StMsrP was also demonstrated to reduce free Met-O and to catalyse the complete repair of an oxidized protein. More importantly, this study provides for the first time access to the exhaustive list of the Msr systems of a pathogen, including four cytoplasmic enzymes (MsrA, MsrB, MsrC, BisC) and one periplasmic enzyme (MsrP).
The stability of the precursor is essential for producing high-quality perovskite films with minimal non-radiative recombination. In this study, methionine sulfoxide (MTSO), which features multiple electron-donation sites, is strategically chosen as a precursor stabilizer and crystal growth mediator for inverted perovskite solar cells (PSCs). MTSO stabilizes the precursor by inhibiting the oxidation of iodide ions and passivates charged traps through coordination and hydrogen bonding interactions.
Background: As two of the most impactful abiotic stresses, salt and drought strongly affect tomato growth and development, especially at the seedling stage. However, dissection of the genetic basis underlying salt/drought tolerance at seedling stage in tomato remains limited in scope.
Results: Here, we reported an analysis of major quantitative trait locus (QTL) and potential causal genetic variations in seedling stage salt/drought tolerance in recombinant inbred lines (n = 201) of S.
Polyphenols are well-known for their antioxidant properties, but their prooxidative activity remain less understood. This study quantitatively examined the formation of hydrogen peroxide (HO) during the autooxidation of nine different polyphenols in model systems, investigating how it impacts protein oxidation and protein-polyphenol covalent adduct formation. Polyphenols (4 mM) generated HO in the range of 0.
Virus and Prion Research Unit, National Animal Disease Center, Agricultural Research Service, United States Department of Agriculture, Ames, IA 50010, USA.
Chronic wasting disease (CWD) is a prion disease that impacts both wild and farmed elk, where infectious proteins cause normal proteins to misfold.
A study used mass spectrometry to analyze prion proteins from elk inoculated with CWD, focusing on various peptides to measure prion quantity and composition.
Results indicated differing amounts of prion proteins in the elk's brain tissue and highlighted the presence of methionine oxidation, demonstrating how mass spectrometry can help identify prion strains on a molecular level.
MsrB1 is a thiol-dependent enzyme that reduces protein methionine--sulfoxide and regulates inflammatory response in macrophages. Therefore, MsrB1 could be a promising therapeutic target for the control of inflammation. To identify MsrB1 inhibitors, we construct a redox protein-based fluorescence biosensor composed of MsrB1, a circularly permutated fluorescent protein, and the thioredoxin1 in a single polypeptide chain.
