Chlorobaculum
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA609807 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| Other | ||||
| SRR8483032_1.fastq.gz | Fastqsanger.gz | |||
| SRR8483032_2.fastq.gz | Fastqsanger.gz |
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Project description:Chlorobaculum tepidum is an anaerobic green sulfur bacterium which oxidizes sulfide, elemental sulfur, and thiosulfate for photosynthetic growth. It can also oxidize sulfide to produce extracellular S0 globules, which can be further oxidized to sulfate and used as an electron donor. Here we performed label free quantitative proteomics on total cell lysates prepared from different metabolic states, including a sulfur production state (10 hours post incubation, PI), the beginning of sulfur consumption (20 hours PI) and the end of sulfur consumption (40 hours PI), respectively. We observed an increased abundance of the sulfide:quinone oxidoreductase Sqr proteins in 20PI indicated a sulfur production state. The periplasmic thiosulfate-oxidizing Sox enzymes and the dissimilatory sulfite reductase Dsr subunits showed an increased abundance in 20PI, corresponding to the sulfur-consuming state. In addition, we found that the abundance of the heterodisulfide-reductase and the sulfhydrogenase operons was influenced of electron donor availability and may be associated with sulfur metabolism. Further, we isolated and analyzed the extracellular sulfur globules in the different metabolic states in order to study their morphology and the sulfur cluster composition, yielding 58 previously uncharacterized proteins in purified globules. Our results show that Cba tepidum regulates the cellular levels of enzymes involved in sulfur metabolism in response to the availability of reduced sulfur compounds.
2023-02-13 | PXD038039 | Pride
Project description:The green sulfur bacterium Chlorobaculum tepidum is proposed to oxidize sulfide and elemental sulfur via sulfite as an obligate intermediate. The sulfite pool is predicted to be contained in the cytoplasm and be oxidized by the concerted action of ApsBA, which directly oxidizes sulfite, and QmoABC, which transfers electrons from ApsBA to the quinone pool. Like other green sulfur bacteria, C. tepidum was unable to use exogenously provided sulfite as the sole electron donor. However, exogenous sulfite significantly stimulated the growth yield of sulfide limited batch cultures. The growth of C. tepidum mutant strains, CT0867/qmoB::TnOGm and CT0868/qmoC::TnOGm, was not increased by sulfite. Furthermore, these strains accumulated sulfite and displayed a growth yield decrease when grown on sulfide as the sole electron donor. These results support an obligate, cytoplasmic sulfite intermediate as part of the canonical sulfur oxidation pathway in C. tepidum that requires the Qmo complex for oxidation.
| S-EPMC3119408 | biostudies-literature
Project description:Background: Ependymomas encompass multiple, clinically relevant tumor types based on localization and molecular profiles. Although tumors of the methylation class “spinal ependymoma” (SP-EPN) represent the most common intramedullary neoplasms in children and adults, their developmental origin is ill-defined, molecular data are scarce, and the potential heterogeneity within SP-EPN remains unexplored. The only known recurrent genetic events in SP-EPN are loss of chromosome 22q and NF2 mutations, but neither types and frequency of these alterations nor their clinical meaning have been described in a large, epigenetically defined series. Methods: We mapped SP-EPN transcriptomes (n=76) to developmental atlases of the developing and adult spinal cord to uncover potential developmental origins of these tumors. In addition, transcriptomic, epigenetic (n=234), genetic (n=140), and clinical analyses (n=115) were integrated for a detailed overview on this entity. Results: Integration of transcriptomic ependymoma data with single-cell atlases of the spinal cord identified mature adult ependymal cells to display highest similarities to SP-EPN. Unsupervised hierarchical clustering of tumor data together with integrated analysis of methylation profiles identified two molecular SP-EPN subtypes. Subtype 1 predominantly contained NF2 wild type sequences with regular NF2 expression but revealed more extensive copy number alterations. Subtype 2 harbored previously known germline or sporadic NF2 mutations and was NF2-deficient in most cases, more often showed multilocular disease, and demonstrated a significantly reduced progression-free survival. Conclusion: Based on integrated molecular profiling of a large tumor series we identify two distinct SP-EPN subtypes with important implications for genetic counseling, patient surveillance, and drug development priorities.
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