Acanthamoeba castellanii medusavirus
Ontology highlight
ABSTRACT:
PROVIDER: PRJDB11502 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| Other | ||||
| DRR286080_1.fastq.gz | Fastqsanger.gz | |||
| DRR286080_2.fastq.gz | Fastqsanger.gz | |||
| DRR286082_1.fastq.gz | Fastqsanger.gz | |||
| DRR286082_2.fastq.gz | Fastqsanger.gz |
Items per page: 5 1 - 5 of 7 |
Similar Datasets
Project description:STAT (signal transducers and activators of transcription) proteins are one of the important mediators of phosphotyrosine-regulated signaling in metazoan cells. We described the presence of STAT protein in a unicellular, free-living amoebae with a simple life cycle, Acanthamoeba castellanii. A. castellanii is the only, studied to date, Amoebozoan that does not belong to Mycetozoa but possesses STATs. A sequence of the A. castellanii STAT protein includes domains similar to those of the Dictyostelium STAT proteins: a coiled coil (characteristic for Dictyostelium STAT coiled coil), a STAT DNA-binding domain and a Src-homology domain. The search for protein sequences homologous to A. castellanii STAT revealed 17 additional sequences from lower eukaryotes. Interestingly, all of these sequences come from Amoebozoa organisms that belong to either Mycetozoa (slime molds) or Centramoebida. We showed that there are four separated clades within the slime mold STAT proteins. The A. castellanii STAT protein branches next to a group of STATc proteins from Mycetozoa. We also demonstrate that Amoebozoa form a distinct monophyletic lineage within the STAT protein world that is well separated from the other groups.
| S-EPMC4206453 | biostudies-literature
Project description:Acanthamoeba castellanii Raw sequence reads
| PRJNA422304 | ENA
Project description:An EST project has begun for this protist
| PRJNA12783 | ENA
Project description:RNAseq data from Acanthamoeba castellanii
| PRJNA794325 | ENA
Project description:A phagocytic environmental protozoan found in aquatic biofilms and in soil, that can be an opportunistic pathogen.
| PRJNA12731 | ENA
Project description:To investigate the interaction of intra-amoebal C. jejuni with the transient host A. castellanii. We then performed gene expression profiling analysis using data obtained from RNA-seq of control and intra-amoebal C. jejuni.
2022-11-02 | GSE206909 | GEO
Project description:1. Chemiluminescence of Acanthomoeba castellanii in the presence of O2 was of similar intensity in organisms harvested early or late during exponential growth [when cyanide (1 mM) stimulates or inhibits respiration respectively]. 2. Cyanide (up to 1.5 mM) stimulated photoemission in both types of organism by 250--300 photons/s per 10(7) cells above the value observed under aerobic conditions. 3. 'Dibromothymoquinone' (2,5-dibromo-6-isopropyl-3-methyl-p-benzoquinone) (up to 80 microM) further increased chemiluminescence. 4. Similar responses were also demonstrated in whole homogenates and in subcellular fractions; 36% of the chemiluminescence was provided by a fraction sedimenting at 100000g-min, and 20% in that fraction that was non-sedimentable at 200000g-min. 5. Mitochondrial substrates (succinate, 2-oxoglutarate, NADH) in the presence or absence of ADP and Pi or peroxisomal substrates (glycollate, urate or ethanol) gave no increases in light emission by whole homogenates or in any of the fractions. 6. It is suggested that reactions responsible for production of chemiluminescence are those primarily producing superoxide anions and leading to lipid peroxidation and singlet-oxygen formation. Photoemission enhancement and superoxide dismutase inhibition showed similar cyanide concentration-dependencies.
| S-EPMC1161685 | biostudies-other
Project description:1. Low-temperature difference spectra of gradient-purified mitochondria of Acanthamoeba castellanii reveal the presence of cytochromes b-555, b-562 and c-549, with a-type cytochromes having a broad asymmetrical maximum at 602 nm; these components were also observed in specta of whole cells. 2. The a-type cytochromes are unusual in that they have split Soret absorption maxima (at 442 and 449 nm) and an uncharacteristic CO difference spectrum. 3. CO difference spectra of whole cells and 'microsomal' membranes show large amounts of cytochrome P-420 compared with cytochrome P-450. 4. Difference spectra in the presence of cyanide indicate the presence of an a-type cytochrome and two cyanide-reacting components, one of which may be cytochrome a3. 5. Whole-cell respiration in a N2/O2 (19:1) atmosphere was decreased by 50%, suggesting the presence of a low-affinity oxidase. This lowered respiration is inhibited by 50% by CO, and the inhibition is partially light-reversible; photochemical action spectra suggest that cytochrome a3 contributes to this release of inhibition. Other CO-reacting oxidases are also present. 6. The results are discussed with the view that cytochrome a3 is present in A. castellanii, but its identification in CO difference spectra is obscured by other component(s).
| S-EPMC1184122 | biostudies-other
Project description:unclassified medusavirus genome
| PRJDB10270 | ENA
Project description:A culture of Acanthamoeba castellanii cells was infected with mimivirus. At specified times after infection, infected cells aliquots were subjected to total RNA extraction. Cy3 labeled cDNA was hybridized on custom designed Agilent oligonucleotide tiling microarrays covering both strands of the mimivirus genome.
2010-03-18 | E-MTAB-187 | biostudies-arrayexpress