The redox-sensitive regulatory module of cyclophilin 20-3, 2-cysteine peroxiredoxin and cysteine synthase in the high light acclimation response in Arabidopsis thaliana
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ABSTRACT:
ORGANISM(S): Arabidopsis thaliana
PROVIDER: GSE94327 | GEO | 2017/07/31
SECONDARY ACCESSION(S): PRJNA369384
REPOSITORIES: GEO
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Project description:The redox-sensitive regulatory module of cyclophilin 20-3, 2-cysteine peroxiredoxin and cysteine synthase in the high light acclimation response in Arabidopsis thaliana
| PRJNA369384 | ENA
Project description:Equine myofibrillar myopathy (MFM) causes exertional muscle pain and is characterized by myofibrillar disarray and ectopic protein aggregates of unknown origin. To investigate the pathophysiology of MFM, we compared the skeletal muscle proteome and 3 h post-exercise transcriptome of gluteal muscle in MFM and control Arabian horses using iTRAQ and RNA-sequencing analyses. Differential expression (DE) was evaluated using edgeR and pathway analysis using Cytoscape and Cluego. Proteome analysis revealed significantly lower antioxidant peroxiredoxin 6 content (PRDX6, ↓4.14 log2 fold change [FC]), sarcomere protein tropomyosin (TPM2, ↓3.24x) and higher fatty acid transport enzyme carnitine palmitoyl transferase (CPT1B, ↑3.49x) in MFM vs. control muscle at rest. Three hours after exercise, 191 genes were DE in MFM vs. control muscle with a remarkably focused > 1.5 log2FC in genes involved in sulfur compound/ cysteine metabolism such as cystathionine-beta-synthase [CBS, ↑4.51] and a cysteine and neutral amino acid membrane transporter [SLC7A10, ↑1.79]. In MFM vs. control at rest, 284 genes were DE with > 1.5 log2 FC in pathways for structure morphogenesis, fiber organization, tissue development and cell differentiation including> 2 log2 FC in alpha actin-cardiac [↑ ACTC1], cytoskeletal desmoplakin [↑ DSP], basement membrane usherin [↓ USH2A] and delta like non-canonical Notch ligand 1, [↓ DLK1]. In conclusion, myofibrillar disarray and protein aggregation in MFM horses was embodied by DE expression in pathways of structure/fiber organization and tissue regeneration. Reduced antioxidant capacity as a potential etiology for MFM was supported by diminished cysteine rich antioxidant peroxiredoxin 6 with compensatory increased cysteine synthesis following exercise.
2019-11-12 | PXD009362 | Pride
Project description:Light controls control a vast array of biological processes, including cell and organelle motility, stress responses, organismal development and the entrainment of circadian rhythms, that maintain diurnal cycles of activity in organisms from cyanobacteria to humans. Recent studies indicate that a type of antioxidant and signaling proteins, peroxiredoxins, sustain circadian rhythms independent of characterized circadian pacemakers in organisms from all the three kingdoms of life, suggesting a role for H2O2 production in circadian clocks. Whereas many circadian clocks involve photosensitive pigments such as melanopsin and cryptochromes it is unclear whether peroxiredoxins can respond to light stimuli and how they interact with global signaling networks regulating e.g. clocks and aging, such as cyclic AMP (cAMP)/protein kinase A (PKA). In yeast, that lacks decidated photoreceptors, blue light induces cAMP-PKA-dependent, nuclear accumulation of a transcription factor, Msn2. However, the mechanism by which light represses pathway activity to stimulate Msn2 nuclear translocation is unknown. Here we identify increased H2O2–production via a conserved peroxisomal oxidase as the cause of light-induced Msn2 nuclear concentration. The H2O2 signal is transduced by the catalytic cysteines of the peroxiredoxin Tsa1 that relieve Msn2 from inhibitory PKA phosphorylation causing its nuclear accumulation. We propose that yeast senses light via H2O2 and a peroxiredoxin to inhibit cAMP/PKA activity and our data form a framework for the study of light responses in cells lacking dedicated light receptors and cAMP-controlled biological rhythms in multicellular organisms.
2018-07-03 | PXD001853 | Pride
Project description:We have found that cyclophilin B (CypB) expression is important for malignant glioblastoma multiforme (GBM) cell proliferation. To identify molecular mechanisms that could explain CypB-dependent survival in human GBM cells, a microarray analysis was performed using RNA prepared from U251MG GBM cells transduced with lentiviral CypB shRNA. These data revealed that about 130 genes were more than 2-fold affected by CypB depletion. Significant alterations in the expression of genes related to cell death, cell proliferation and cell migration were found in the shCypB cells. U251 glioblastoma cells transduced with lentivirus expressing non-target control shRNA (shCON) were compared to cells transduced with lentivirus expressing shRNA sequence against cyclophilin B (shCypB). Cells transduced with the lentiviral shRNA (shCON VS shCypB) for 5 days before total RNA extraction. Three biological replicates of cells treated with each shRNA (shCON or shCypB) were profiled.
2013-09-12 | E-GEOD-50756 | biostudies-arrayexpress
Project description:The isomerase activity of Cyclophilin A is important for midbody abscission during cell division, however to date, midbody substrates remain unknown. In this study, we report that the GTP-binding protein Septin 2 interacts with Cyclophilin A. We highlight a dynamic series of Septin 2 phenotypes at the midbody, previously undescribed in human cells. Furthermore, Cyclophilin A depletion or loss of isomerase activity is sufficient to induce phenotypic Septin 2 defects at the midbody. Structural and molecular analysis reveals that Septin 2 proline 259 is important for interaction with Cyclophilin A. Moreover, an isomerisation-deficient EGFP-Septin 2 proline 259 mutant displays defective midbody localisation, and undergoes impaired abscission, consistent with data from cells with loss of Cyclophilin A expression or activity. Collectively, this data reveals Septin 2 as a novel interacting partner and isomerase substrate of Cyclophilin A at the midbody that is required for abscission during cytokinesis in cancer cells.
2023-10-24 | PXD042822 | Pride
Project description:Cysteine occupies a central position in plant metabolism due to its biochemical functions. Arabidopsis thaliana cells contain different O-acetylserine(thiol)lyase (OASTL) enzymes that catalyze the biosynthesis of cysteine. Because they are localized in the cytosol, plastids and mitochondria, this results in multiple subcellular cysteine pools. Much progress has been made on the most abundant OASTL enzymes; however, information on the less abundant OASTL-like proteins has been scarce. To unequivocally establish the enzymatic reaction catalyzed by the minor cytosolic OASTL isoform CS-LIKE (AT5G28030), we expressed this enzyme in bacteria and characterized the purified recombinant protein. Our results demonstrate that CS-LIKE catalyzes the desulfuration of L-cysteine to sulfide plus ammonia and pyruvate. Thus, CS-LIKE is a novel L-cysteine desulfhydrase (EC 4.4.1.1), and we propose to designate it DES1. The impact and functionality of DES1 in cysteine metabolism was revealed by the phenotype of the T-DNA insertion mutants des1-1 and des1-2. Mutation of the DES1 gene leads to premature leaf senescence, as demonstrated by the increased expression of senescence-associated genes and transcription factors. Also, the absence of DES1 significantly reduces the total cysteine desulfuration activity in leaves, and there is a concomitant increase in the total cysteine content. As a consequence, the expression levels of sulfur-responsive genes are de-regulated, and the mutant plants show enhanced antioxidant defenses and tolerance to conditions that promote oxidative stress. Our results suggest that DES1 from Arabidopsis is an L-cysteine desulfhydrase involved in maintaining cysteine homeostasis, mainly at late developmental stages or under environmental perturbations. Using the Affymetrix ATH1 GeneChips, we performed a comparative transcriptomic analysis on leaves of the des1-1 and wild type plants grown on soil for three weeks. Three biological replicates were performed for each sample and hybridized to the chips. We made the comparison of des1-1 leaves versus wild-type leaves to classify the differently expressed genes in the mutant plant.
2011-11-23 | E-GEOD-19244 | biostudies-arrayexpress
Project description:Cysteine occupies a central position in plant metabolism due to its biochemical functions. Arabidopsis thaliana cells contain different O-acetylserine(thiol)lyase (OASTL) enzymes that catalyze the biosynthesis of cysteine. Because they are localized in the cytosol, plastids and mitochondria, this results in multiple subcellular cysteine pools. Much progress has been made on the most abundant OASTL enzymes; however, information on the less abundant OASTL-like proteins has been scarce. To unequivocally establish the enzymatic reaction catalyzed by the minor cytosolic OASTL isoform CS-LIKE (AT5G28030), we expressed this enzyme in bacteria and characterized the purified recombinant protein. Our results demonstrate that CS-LIKE catalyzes the desulfuration of L-cysteine to sulfide plus ammonia and pyruvate. Thus, CS-LIKE is a novel L-cysteine desulfhydrase (EC 4.4.1.1), and we propose to designate it DES1. The impact and functionality of DES1 in cysteine metabolism was revealed by the phenotype of the T-DNA insertion mutants des1-1 and des1-2. Mutation of the DES1 gene leads to premature leaf senescence, as demonstrated by the increased expression of senescence-associated genes and transcription factors. Also, the absence of DES1 significantly reduces the total cysteine desulfuration activity in leaves, and there is a concomitant increase in the total cysteine content. As a consequence, the expression levels of sulfur-responsive genes are de-regulated, and the mutant plants show enhanced antioxidant defenses and tolerance to conditions that promote oxidative stress. Our results suggest that DES1 from Arabidopsis is an L-cysteine desulfhydrase involved in maintaining cysteine homeostasis, mainly at late developmental stages or under environmental perturbations.
2011-11-23 | GSE19244 | GEO
Project description:First experiment: Cells were cultured in sulfur amino acid-free DMEM supplemented with 0.1 mM methionine + 0.1 mM cysteine (complete) or supplemented only with 0.1 mM methionine (cysteine-free). Cells were cultured in either medium for 42 h (Long + Cys; Long -Cys) or in cysteine-free medium for 36 h followed by 6 h in complete medium (Short +Cys) Second experiment: C3A/HepG2 cells were cultured in sulfur amino acid-free DMEM supplemented with 0.1 mM Met and 0.1 mM Cys (complete) or supplemented only with 0.1 mM Met (cysteine-devoid). Cells were cultured in complete medium for 42 h (Long +Cys) or in complete medium for 36 h followed by cysteine-devoid medium for 6 h (Short -Cys). Keywords: amino acid deprivation
2007-12-13 | GSE9517 | GEO
Project description:The human pathogenic fungus Aspergillus fumigatus is readily eradicated by the innate immunity of immunocompetent human hosts, but can cause severe infections, such as invasive aspergillosis (IA), in immunocompromised individuals. During infection, the fungal redox homeostasis can be challenged by reactive oxygen (ROS) species, either derived from the oxidative burst of innate immune cells or the action of antifungal drugs. The peroxiredoxin Asp f3 was found to be essential to cause IA in mice, but how Asp f3 integrates to fungal redox homeostasis remains unknown. Here, we show that in vivo, Asp f3 acts as a sensor for ROS. While global transcription in fungal hyphae under minimal growth conditions was fully independent of Asp f3, a robust induction of the oxidative stress response required the presence of the peroxiredoxin. Hyphae devoid of Aspf 3 failed to activate several redox active genes, like members of the gliotoxin biosynthesis gene cluster and integral members of the Afyap1 regulon, the central activator of the ROS defence machinery in fungi. Upon deletion of the asp f3 gene Afyap1 displayed significantly reduced nuclear localization during ROS exposure, indicating that Asp f3 can act as an intracellular redox sensor for several target proteins
2021-06-03 | GSE173349 | GEO
Project description:Excess cysteine (and cystine) is known to be toxic in organisms. Due to the absence of cysteine dioxygenase (involved in degradation of excess cysteine in humans and pathogenic fungi) in non pathogenic fungi such as S. cerevisiae, mechanism of cysteine (and cystine) tolerance is yet to be addressed.
2017-06-13 | GSE87794 | GEO