Dataset Information

Proteome wide analysis of hydrogen peroxide-induced protein carbonylation in Arabidopsis thaliana

ABSTRACT: Protein carbonylation is a non-enzymatic and irreversible post-translational modification that occurs naturally in living organisms under the direct or indirect effect of reactive oxygen species (ROS). In this study, we analyzed proteins that are responsive to carbonylation by exogenous hydrogen peroxide (H2O2) by profiling the carbonylated proteome extracted from Arabidopsis thaliana leaves after H2O2 treatment. Carbonylated proteins were enriched at the peptide level and analyzed by liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS). The results revealed that most of the carbonylated proteins identified in the H2O2-treated plant samples are related to sulphate adenylyl transferases and amidophosphoribosyl transferases involved in the immune system response, defense response, and external stimulus-response.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Arabidopsis Thaliana (ncbitaxon:3702)

SUBMITTER: Tagnon Missihoun

PROVIDER: MSV000090540 | MassIVE | Mon Oct 17 10:59:00 BST 2022

SECONDARY ACCESSION(S): PXD037515

REPOSITORIES: MassIVE

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Proteome-wide analysis of hydrogen peroxide-induced protein carbonylation in <i>Arabidopsis thaliana</i>.

Fangue-Yapseu Georges Yannick GY Tola Adesola Julius AJ Missihoun Tagnon D TD

Frontiers in plant science 20221205

<h4>Introduction</h4>Protein carbonylation is a non-enzymatic and irreversible post-translational modification that occurs naturally in living organisms under the direct or indirect effect of reactive oxygen species (ROS). In animals, signaling pathways involving numerous carbonylated proteins have been identified, highlighting the dual role of these molecules in ROS signal transduction. In plants, studies on phytohormone signaling (auxin, methyl jasmonate, abscisic acid) have shown that reactiv ...[more]

PMID: 36544875

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Project description:Oxidative Stress Protection and the Repair Response To Hydrogen Peroxide in the Hyperthermophilic Archaeon Pyrococcus furiosus Pyrococcus furiosus is a shallow marine, anaerobic archaeon that grows optimally at 100Â°C. Addition of H2O2 (0.5 mM) to a growing culture resulted in cessation of growth with a 2 hour lag before normal growth resumed. Whole genome transcriptional profiling revealed that the main response occurs within 30 min of peroxide addition, with the up-regulation of 62 open reading frames (ORFs), 36 of which are part of 10 potential operons. More than half of the up-regulated ORFs are of unknown function while some others encode proteins that are involved potentially in sequestering iron and sulfide, in DNA repair and in generating NADPH. This response is thought to involve primarily damage repair rather than protection, since cultures exposed to sub-toxic levels of H2O2 were not more resistant to the subsequent addition of H2O2 (0.5 â 5.0 mM). Consequently, there is little if any induced protective response to peroxide, rather, the organism maintains a constitutive protective mechanism involving high levels of oxidoreductase-type enzymes such as superoxide reductase, rubrerythrin and alkyl hydroperoxide reductase I. The related hyperthermophiles P. woesei and Thermococcus kodakaraensis were more sensitive to peroxide than P. furiosus, apparently due to the lack of several of its peroxide-responsive ORFs. Pyrococcus furiosus (DSM 3638) was grown at 95Â°C in a 20-liter fermentor using maltose as the carbon and energy source. An exponential-phase culture of P. furiosus that had undergone three successive transfers in the experimental medium was used to inoculate the 20-liter fermentor. The culture was shocked with 0.5 mM of hydrogen peroxide (H2O2) when cell density was in mid-exponential phase (~ 5.0 Â´ 107 cells/ml, as determined by direct microscopic cell count). To obtain RNA for microarray and for quantitative PCR (QPCR) analyses, samples (2 liter) were rapidly removed from the fermentor and cooled to 4Â°C. Total RNA was extracted using acid-phenol and stored at -80Â°C until needed. A total of 3 biological replicates in triplicate (3 copies on the same slide) was used in the data set.

Dataset Information

Proteome wide analysis of hydrogen peroxide-induced protein carbonylation in Arabidopsis thaliana

Publications

Proteome-wide analysis of hydrogen peroxide-induced protein carbonylation in <i>Arabidopsis thaliana</i>.

Similar Datasets

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