A broadly conserved fungal alcohol oxidase (AOX) facilitates fungal invasion of plants
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA874732 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR21299492_1.fastq.gz | Fastqsanger.gz | |||
| SRR21299492_2.fastq.gz | Fastqsanger.gz | |||
| SRR21299493_1.fastq.gz | Fastqsanger.gz | |||
| SRR21299493_2.fastq.gz | Fastqsanger.gz | |||
| SRR21299494_1.fastq.gz | Fastqsanger.gz |
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Similar Datasets
Project description:Alcohol oxidases are ecologically important enzymes which facilitate a number of plant-fungal interactions. Within Ascomycota they are primarily associated with methylotrophy, as a peroxisomal alcohol oxidase (AOX) catalyzing the conversion of methanol to formaldehyde in methylotrophic yeast. In this study we demonstrate that AOX orthologs are phylogenetically conserved proteins which are common in the genomes of non-methylotrophic, plant-associating fungi. Additionally, AOX orthologs are highly expressed during infection in a range of diverse pathosystems. To study the role of AOX in plant colonization, AOX knockout mutants were generated in the broad host range pathogen Sclerotinia sclerotiorum. Disease assays in soybean showed that these mutants had a significant virulence defect as evidenced by markedly reduced stem lesions and mortality rates. Chemical genomics suggest that SsAOX may function as an aromatic alcohol oxidase, and growth assays demonstrate that ΔSsAOX is incapable of properly utilizing plant extract as a nutrient source. Profiling of known aromatic alcohols point towards the monolignol coniferyl alcohol (CoA) as a possible substrate for SsAOX. As CoA and other monolignols are ubiquitous among land plants, the presence of highly conserved AOX orthologs throughout Ascomycota imply that this is a broadly conserved protein used by ascomycete fungi during plant colonization.
2022-12-02 | GSE212269 | GEO
Project description: Not available
| S-EPMC9742500 | biostudies-literature
Project description:In higher plants, various developmental and environmental conditions enhance expression of the mitochondrial alternative oxidase (AOX). In this work transgenic Arabidopsis thaliana plants were generated that either overexpress AOX or inhibit its synthesis. Gene expression following antimycin A treatment, which inhibits the cytochrome pathway in mitochondria, was studied in an AOX overexpressor line. An accumulation of AOX protein blocked normal responses of a number of genes, including some AOX genes. This result indicates that AOX can generate feedback to inhibit induction of its own synthesis. Keywords: stress response
2006-02-02 | GSE4141 | GEO
Project description:In higher plants, various developmental and environmental conditions enhance expression of the mitochondrial alternative oxidase (AOX). In this work transgenic Arabidopsis thaliana plants were generated that either overexpress AOX or inhibit its synthesis. Gene expression following antimycin A treatment, which inhibits the cytochrome pathway in mitochondria, was studied in an AOX overexpressor line. The role of AOX in regulation of reactive oxygen species (ROS) in leaves was studied in the transgenic lines. The transgenic lines were also used to investigate the mitochondria-chloroplasts interaction in assays performed at three-times growth light. For most of the parameters measured AOX antisense lines and WT plants showed a very similar response whereas AOX sense lines differed in several aspects. An unexpected result was that AOX overexpressors had higher cellular ATP/ADP ratios as compared to WT and antisense lines. This was linked to decreased photosynthetic CO2-assimilation and O2-evolution, closed PSII reaction centers and altered Calvin cycle metabolite contents. We conclude that increased mitochondrial AOX capacity can lead to a drain of electrons from the chloroplasts causing an unfavorable redox status and thereby inhibit photosynthesis. Keywords: Genetic modification
2006-01-31 | GSE4113 | GEO
Project description:In higher plants, various developmental and environmental conditions enhance expression of the mitochondrial alternative oxidase (AOX). In this work transgenic Arabidopsis thaliana plants were generated that either overexpress AOX or inhibit its synthesis. Gene expression following antimycin A treatment, which inhibits the cytochrome pathway in mitochondria, was studied in an AOX overexpressor line. The role of AOX in regulation of reactive oxygen species (ROS) in leaves was studied in the transgenic lines. The transgenic lines were also used to investigate the mitochondria-chloroplasts interaction in assays performed at three-times growth light. For most of the parameters measured AOX antisense lines and WT plants showed a very similar response whereas AOX sense lines differed in several aspects. An unexpected result was that AOX overexpressors had higher cellular ATP/ADP ratios as compared to WT and antisense lines. This was linked to decreased photosynthetic CO2-assimilation and O2-evolution, closed PSII reaction centers and altered Calvin cycle metabolite contents. We conclude that increased mitochondrial AOX capacity can lead to a drain of electrons from the chloroplasts causing an unfavorable redox status and thereby inhibit photosynthesis.
2007-06-28 | E-GEOD-4113 | biostudies-arrayexpress
Project description:In higher plants, various developmental and environmental conditions enhance expression of the mitochondrial alternative oxidase (AOX). In this work transgenic Arabidopsis thaliana plants were generated that either overexpress AOX or inhibit its synthesis. Gene expression following antimycin A treatment, which inhibits the cytochrome pathway in mitochondria, was studied in an AOX overexpressor line. An accumulation of AOX protein blocked normal responses of a number of genes, including some AOX genes. This result indicates that AOX can generate feedback to inhibit induction of its own synthesis. Two wild type replicates: Poly-A RNA from two batches of plants were labeled with dye-swaps then hybridized to custom-designed arrays containing two sets of spotted DNA elements. Two S5 replicates: Poly-A RNA from two batches of plants were labeled with dye-swaps then hybridized to custom-designed arrays containing three sets of spotted DNA elements.
2010-07-01 | E-GEOD-4141 | biostudies-arrayexpress
Project description:Ciona intestinalis alternative oxidase (AOX) is a mitochondrial respiratory enzyme that acts as an alternative electron sink for ubiquinol (reduced quinone) when the cytochrome bc1 complex (complex III) and/or cytochrome c oxidase (complex IV) are inhibited or impaired (El-Khoury et al., 2014). AOX thus enables electron flux through the mitochondrial electron transport chain (ETC) and thereby prevents reverse electron transport from succinate dehydrogenase (complex II) to NADH:ubiquinone oxidoreductase (complex I) and mitochondrial ROS production, restores redox balance and Krebs cycle activity. As a non-proton-motive enzyme, however, AOX does not directly support ATP production. Previously, a mouse model was generated that despite ubiquitous expression of AOX revealed no deviations from normal physiology and which now is used as model to test mitochondrial disease paradigms (Szibor et al., 2017).
2019-12-13 | PXD014016 | Pride
Project description:The ultimate goal of immunometabolism is to modulate metabolic pathways to enhance immunity. Here, we investigate the potential of an alternative oxidase (AOX) to counteract cytochrome c oxidase (COX) deficiency in T cells. COX is vital for oxidative phosphorylation (OXPHOS), and its deficiency leads to redox imbalances, impaired metabolism, reactive oxygen species (ROS), and apoptosis, resulting in T cell immunodeficiency. We introduced an AOX into COX-deficient T cells, which revealed a normalization of genes involved in redox balance, apoptosis, and metabolic pathways. Mitochondrial function, glycolysis and TCA cycle function were also restored. AOX-enhanced T cells showed improved activation, proliferation, differentiation, and memory formation, resulting in better immune responses against viral challenges. These findings suggest that targeting the ubiquinol pool could be a promising therapeutic strategy for enhancing T cell function in conditions characterized by COX dysfunction and compromised immune responses.
2024-10-02 | GSE269797 | GEO
Project description:The conversion of nitrate to ammonium, known as nitrate reduction, consumes large amounts of reductants in plants. Previous studies have observed that mitochondrial alternative oxidase (AOX) is upregulated under conditions of limited nitrate reduction, such as low or no nitrate availability, or when ammonium serves as the sole nitrogen (N) source. Electron transfer from ubiquinone to AOX bypasses the proton-pumping complexes III and IV, thereby consuming reductants efficiently. Therefore, the upregulation of AOX under conditions of limited nitrate reduction may help dissipate excessive reductants and mitigate oxidative stress. However, firm evidence supporting this hypothesis is lacking due to the absence of experimental systems capable of directly analyzing the relationship between nitrate reduction and AOX. To address this gap, we developed a novel culturing system that allows for the manipulation of nitrate reduction and AOX activities separately, without inducing N starvation, ammonium toxicity, or disrupting the nitrate signal. Using this system, we investigated genome-wide gene expression with RNA-seq to gain insight into the relationship between AOX and nitrate reduction.
2024-04-23 | E-MTAB-14027 | biostudies-arrayexpress
Project description:The objective of this study was to test how restoration of mitochondrial respiration using AOX affects the development of cardiac ischemia-reperfusion (IR) injuries in C57BL/ 6J mice. AOX transgenic mice have Ciona intestinalis AOX coding sequence knocked into the Rosa26 locus with AOX expression controlled by a CAG promoter as described elsewhere (Szibor et al. (2017) Dis Model Mech 10: 163–171). Consequences of 45 min of cardiac ischemia were studied 3 and 9 weeks after reperfusion in both wild-type and AOX litter mates.
2020-01-30 | PXD014061 | Pride