Ontology highlight
ABSTRACT:
PROVIDER: PRJNA1276298 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:We characterized the mechanisms that allow yeast cells to survive under conditions of thiol peroxidase deficiency. Two thiol peroxidase null yeast (delta8) strains independently acquired a second copy of chromosome XI and increased expression of genes encoded by it. Delta-8 strains were compared to the Wt-M11 strain, which is characterized by duplication of chr-XI.
2015-10-10 | GSE70036 | GEO
Project description:Mycothiol (AcCys-GlcN-Ins, MSH) is the major thiol-redox buffer in Actinomycetes, including Mycobacterium and Corynebacterium species. ). Protein S-mycothiolation controls the activities of several redox enzymes that function in detoxification of ROS and methionine sulfoxides, including the thiol peroxidase Tpx, the mycothiol peroxidase Mpx and the methionine sulfoxide reductase MsrA. Here we investigated the level of protein S-mycothiolation in Mycobacterium smegmatis under oxidative stress as well as its NaOCl stress response.
2017-06-30 | PXD003303 | Pride
Project description:Mycothiol (AcCys-GlcN-Ins, MSH) is the major thiol-redox buffer in Actinomycetes, including Mycobacterium and Corynebacterium species. Protein S-mycothiolation controls the activities of several redox enzymes that function in detoxification of ROS and methionine sulfoxides, including the thiol peroxidase Tpx, the mycothiol peroxidase Mpx and the methionine sulfoxide reductase MsrA. Here we investigated the level of protein S-mycothiolation in Corynebacterium diphtheriae DSM43989 under oxidative stress as well as its NaOCl stress response.
2017-07-17 | PXD003321 | Pride
Project description:Adaptive aneuploidy protects against thiol peroxidase deficiency by increasing respiration via key mitochondrial proteins
| PRJNA287520 | ENA
Project description:Bacteria are constantly exposed to fluctuations in reactive oxygen species (ROS). In particular, pathogenic bacteria encounter elevated ROS-levels during host infection. In our present study we investigated the intricate regulatory interplay of the LysR-type transcriptional regulators LsrB and OxyR in Agrobacterium tumefaciens. OxyR is a widespread thiol-based redox sensor in bacteria, while LsrB is unique to Rhizobiales. Using phenotypic assays and RNA-sequencing under oxidative stress, we unveiled a central role for both regulators in co-regulating key antioxidant pathways, including katG encoding a bifunctional catalase/peroxidase. Furthermore, we provide novel insights into the mechanism of LsrB activation, suggesting that LsrB also functions as a thiol-based redox sensor. In summary, our findings illuminate the LsrB-OxyR system as a critical component of A. tumefaciens' defense against oxidative stress
2025-04-28 | PXD055627 | Pride
Project description:The thiol redox state is a decisive functional characteristic of proteins in cell biology. Plasmatic cell compartments maintain a thiol-based redox regulatory network linked to the glutathione/glutathione disulfide couple (GSH/GSSG) and the NAD(P)H system. The basic network constituents are known and in vivo cell imaging with gene-encoded probes have revealed insight into the dynamics of the [GSH]2/[GSSG] redox potential, H2O2 and NAD(P)H+H+ in dependence on the metabolic and environmental conditions. Highly limited is our understanding of the contribution and interaction of the components in the network, also because of compensatory reactions in genetic approaches. Reconstituting the cytosolic network in vitro from fifteen recombinant proteins at in vivo concentrations, namely glutathione peroxidase-like (GPXL), peroxiredoxins (PRX), glutaredoxins (GRX), thioredoxins (TRX), NADPH-dependent thioredoxin reductase A (NTRA) and glutathione reductase (GR) and applying GRX1-roGFP2 or roGFP2-ORP1 as dynamic sensors, allows for monitoring the response to a single H2O2 pulse. The major change in thiol oxidation as visualized by targeted proteomics occurred in relevant peptides of GPXL, and to a lesser extent of PRX, while other Cys-containing peptides only showed small changes in redox state and protection. Titration of ascorbate peroxidase (APX2) into the system together with dehydroascorbate reductase (DHAR1) lowered the oxidation of the fluorescent sensors in the network, but was unable to suppress it. The results demonstrate the power of the network to detoxify H2O2, the partially independent branches of electron flow with significance for specific cell signaling and the importance of APX to modulate the signaling without suppressing it and shifting the burden to glutathione oxidation.
2025-01-21 | PXD048374 | JPOST Repository
Project description:Haemophilus parasuis D74 genome sequencing
| PRJNA295561 | ENA