Mitochondria and TSWV
Ontology highlight
ABSTRACT:
PROVIDER: PRJEB50064 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:We report here lead optimisation efforts of a new series of cytochrome bc1 oxidase inhibitors, the quinazoline derivatives. Four derivatives showed mild to no cytotoxicity as potent in vitro and ex vivo activity in infected THP-1 macrophages against M. tuberculosis. Isolation of resistant mutants to one of the derivatives in M. tuberculosis revealed mutations in both QcrA and QcrB of the cytochrome bc1 oxidase, one of two terminal oxidases of the mycobacterial electron transport chain. Cross-resistance studies, transcriptomic analyses and bioenergetics flux assays provide further evidence of the cytochrome bc1 as the target of the quinazolines compounds. The transcriptomic and bioenergetic profiles obtained when M. tuberculosis was treated with 11626252 are similar to transcriptomic and respiratory signatures of other cytochrome bc1 oxidase inhibitors.
2019-08-01 | GSE119158 | GEO
Project description:Viruses are obligate intracellular pathogens that depend on host factors to complete their infection cycle. Very little is known of which plant factors are required for successful Tomato spotted wilt orthotospovirus (TSWV) infection. The viral ribonucleoprotein (RNP) fraction from TSWV infected Nicotiana benthamiana plants was purified and its protein composition was analysed by proteomics by mass spectrometry to identify host proteins that co-purify with viral RNPs. Related, we expressed a TSWV replicon system in a non-host system, Bakers’ yeast (Saccharomyces cerevisiae), and purified as well the RNP fraction from yeast. Comparative proteomics was used to find common enriched proteins observed in both yeast and plant RNP fractions.
2021-11-10 | PXD026246 | Pride
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 purple α-proteobacterium Rhodobacter sphaeroides is a long-established model organism owing to its ability to switch between aerobic, anaerobic and phototrophic metabolism. This organism is also of great interest because of its phylogenetic relationship with the bacterial progenitor of the mitochondrion in eukaryotes. A component of the electron transport chain in both bacteria and mitochondria is the cytochrome bc1 (cytbc1) complex, a quinol:cytochrome c oxidoreductase that translocates protons across energy-transducing membranes. The resulting proton motive force is then utilized to drive ATP synthesis. Cytbc1 comprises three core subunits together with, in some organisms, one or more additional subunits. In Rhodobacter sphaeroides, the one additional subunit (subunit IV) is not fully characterized in terms of both structure and function. In this project, proteomic analysis is used to confirm the presence of all four subunits in a cytbc1 preparation isolated in SMA nanodiscs for structural analysis by cryo-EM.
2023-03-14 | PXD039340 | Pride
Project description:Despite the advancement of structural and functional research on TSWV NSs, its protein-interacting targets in host plants are still largely unknown. In this research, we investigated the NSs-interacting proteins in Nicotiana benthamiana via affinity purification and mass spectrometry (AP-MS) analysis.
2021-01-04 | PXD022401 | Pride
Project description:Bacteria modify expression of different types of terminal oxidase in response to oxygen availability. Corynebacterium glutamicum, a facultative anaerobic bacterium in Actinobacteria, possesses aa3-type cytochrome c oxidase and cytochrome bd-type quinol oxidase, the latter of which is induced upon oxygen limitation. We report here that an extracytoplasmic function sigma factor, SigC, is unprecedentedly responsible for the regulation. Chromatin immunoprecipitation in conjunction with microarray (ChIP-chip) analysis detected eight SigC-binding regions in the genome, leading to identification of a consensus promoter sequence for SigC recognition. The promoter sequences were found upstream of genes for cytochrome bd, heme a synthesis enzymes, and uncharacterized membrane proteins, all of which were upregulated by sigC overexpression. In contrast, that found on the antisense strand upstream of an operon encoding the cytochrome bc1 complex conferred a SigC-dependent negative effect on the operon expression. The SigC regulon was induced by cytochrome aa3 deficiency without modification of expression of sigC itself, but not by deficiency of the bc1 complex. These findings suggest that SigC is activated in response to impairment of electron transfer via cytochrome aa3, not directly to shift in oxygen levels. Our results provide a novel paradigm for transcriptional regulation of the aerobic respiratory system in bacteria.
2016-08-22 | GSE72452 | GEO
Project description:Bacteria modify expression of different types of terminal oxidase in response to oxygen availability. Corynebacterium glutamicum, a facultative anaerobic bacterium in Actinobacteria, possesses aa3-type cytochrome c oxidase and cytochrome bd-type quinol oxidase, the latter of which is induced upon oxygen limitation. We report here that an extracytoplasmic function sigma factor, SigC, is unprecedentedly responsible for the regulation. Chromatin immunoprecipitation in conjunction with microarray (ChIP-chip) analysis detected eight SigC-binding regions in the genome, leading to identification of a consensus promoter sequence for SigC recognition. The promoter sequences were found upstream of genes for cytochrome bd, heme a synthesis enzymes, and uncharacterized membrane proteins, all of which were upregulated by sigC overexpression. In contrast, that found on the antisense strand upstream of an operon encoding the cytochrome bc1 complex conferred a SigC-dependent negative effect on the operon expression. The SigC regulon was induced by cytochrome aa3 deficiency without modification of expression of sigC itself, but not by deficiency of the bc1 complex. These findings suggest that SigC is activated in response to impairment of electron transfer via cytochrome aa3, not directly to shift in oxygen levels. Our results provide a novel paradigm for transcriptional regulation of the aerobic respiratory system in bacteria.
2016-08-22 | GSE72451 | GEO
Project description:Bacteria modify expression of different types of terminal oxidase in response to oxygen availability. Corynebacterium glutamicum, a facultative anaerobic bacterium in Actinobacteria, possesses aa3-type cytochrome c oxidase and cytochrome bd-type quinol oxidase, the latter of which is induced upon oxygen limitation. We report here that an extracytoplasmic function sigma factor, SigC, is unprecedentedly responsible for the regulation. Chromatin immunoprecipitation in conjunction with microarray (ChIP-chip) analysis detected eight SigC-binding regions in the genome, leading to identification of a consensus promoter sequence for SigC recognition. The promoter sequences were found upstream of genes for cytochrome bd, heme a synthesis enzymes, and uncharacterized membrane proteins, all of which were upregulated by sigC overexpression. In contrast, that found on the antisense strand upstream of an operon encoding the cytochrome bc1 complex conferred a SigC-dependent negative effect on the operon expression. The SigC regulon was induced by cytochrome aa3 deficiency without modification of expression of sigC itself, but not by deficiency of the bc1 complex. These findings suggest that SigC is activated in response to impairment of electron transfer via cytochrome aa3, not directly to shift in oxygen levels. Our results provide a novel paradigm for transcriptional regulation of the aerobic respiratory system in bacteria.
2016-08-22 | GSE72450 | GEO
Project description:Bacteria modify expression of different types of terminal oxidase in response to oxygen availability. Corynebacterium glutamicum, a facultative anaerobic bacterium in Actinobacteria, possesses aa3-type cytochrome c oxidase and cytochrome bd-type quinol oxidase, the latter of which is induced upon oxygen limitation. We report here that an extracytoplasmic function sigma factor, SigC, is unprecedentedly responsible for the regulation. Chromatin immunoprecipitation in conjunction with microarray (ChIP-chip) analysis detected eight SigC-binding regions in the genome, leading to identification of a consensus promoter sequence for SigC recognition. The promoter sequences were found upstream of genes for cytochrome bd, heme a synthesis enzymes, and uncharacterized membrane proteins, all of which were upregulated by sigC overexpression. In contrast, that found on the antisense strand upstream of an operon encoding the cytochrome bc1 complex conferred a SigC-dependent negative effect on the operon expression. The SigC regulon was induced by cytochrome aa3 deficiency without modification of expression of sigC itself, but not by deficiency of the bc1 complex. These findings suggest that SigC is activated in response to impairment of electron transfer via cytochrome aa3, not directly to shift in oxygen levels. Our results provide a novel paradigm for transcriptional regulation of the aerobic respiratory system in bacteria. Comparison of gene expression profiles of the wild type before and after sigC overexpression at the exponential phase. Three independent experiments were performed.
2016-08-22 | E-GEOD-72451 | biostudies-arrayexpress
Project description:Bacteria modify expression of different types of terminal oxidase in response to oxygen availability. Corynebacterium glutamicum, a facultative anaerobic bacterium in Actinobacteria, possesses aa3-type cytochrome c oxidase and cytochrome bd-type quinol oxidase, the latter of which is induced upon oxygen limitation. We report here that an extracytoplasmic function sigma factor, SigC, is unprecedentedly responsible for the regulation. Chromatin immunoprecipitation in conjunction with microarray (ChIP-chip) analysis detected eight SigC-binding regions in the genome, leading to identification of a consensus promoter sequence for SigC recognition. The promoter sequences were found upstream of genes for cytochrome bd, heme a synthesis enzymes, and uncharacterized membrane proteins, all of which were upregulated by sigC overexpression. In contrast, that found on the antisense strand upstream of an operon encoding the cytochrome bc1 complex conferred a SigC-dependent negative effect on the operon expression. The SigC regulon was induced by cytochrome aa3 deficiency without modification of expression of sigC itself, but not by deficiency of the bc1 complex. These findings suggest that SigC is activated in response to impairment of electron transfer via cytochrome aa3, not directly to shift in oxygen levels. Our results provide a novel paradigm for transcriptional regulation of the aerobic respiratory system in bacteria. ChIP-chip analyses using a strain expressing the FLAG-tagged SigC in the background of the wild type at two growth phases (exporenatial and stationary phases). Two independent experiments were performed.
2016-08-22 | E-GEOD-72452 | biostudies-arrayexpress