Metallosphaera cuprina
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ABSTRACT:
PROVIDER: PRJNA65525 | ENA |
REPOSITORIES: ENA
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Project description:Conserved clusters of genes encoding DsrE and TusA homologs occur in many archaeal and bacterial sulfur oxidizers. TusA has a well documented function as a sulfurtransferase in tRNA modification and molybdenum cofactor biosynthesis in Escherichia coli, and DsrE is an active site subunit of the DsrEFH complex that is essential for sulfur trafficking in the phototrophic sulfur-oxidizing Allochromatium vinosum. In the acidothermophilic sulfur (S(0))- and tetrathionate (S4O6(2-))-oxidizing Metallosphaera cuprina Ar-4, a dsrE3A-dsrE2B-tusA arrangement is situated immediately between genes encoding dihydrolipoamide dehydrogenase and a heterodisulfide reductase-like complex. In this study, the biochemical features and sulfur transferring abilities of the DsrE2B, DsrE3A, and TusA proteins were investigated. DsrE3A and TusA proved to react with tetrathionate but not with NaSH, glutathione persulfide, polysulfide, thiosulfate, or sulfite. The products were identified as protein-Cys-S-thiosulfonates. DsrE3A was also able to cleave the thiosulfate group from TusA-Cys(18)-S-thiosulfonate. DsrE2B did not react with any of the sulfur compounds tested. DsrE3A and TusA interacted physically with each other and formed a heterocomplex. The cysteine residue (Cys(18)) of TusA is crucial for this interaction. The single cysteine mutants DsrE3A-C(93)S and DsrE3A-C(101)S retained the ability to transfer the thiosulfonate group to TusA. TusA-C(18)S neither reacted with tetrathionate nor was it loaded with thiosulfate with DsrE3A-Cys-S-thiosulfonate as the donor. The transfer of thiosulfate, mediated by a DsrE-like protein and TusA, is unprecedented not only in M. cuprina but also in other sulfur-oxidizing prokaryotes. The results of this study provide new knowledge on oxidative microbial sulfur metabolism.
| S-EPMC4175335 | biostudies-literature
Project description:The genome of the metal sulfide-oxidizing, thermoacidophilic strain Metallosphaera cuprina Ar-4 has been completely sequenced and annotated. Originally isolated from a sulfuric hot spring, strain Ar-4 grows optimally at 65°C and a pH of 3.5. The M. cuprina genome has a 1,840,348-bp circular chromosome (2,029 open reading frames [ORFs]) and is 16% smaller than the previously sequenced Metallosphaera sedula genome. Compared to the M. sedula genome, there are no counterpart genes in the M. cuprina genome for about 480 ORFs in the M. sedula genome, of which 243 ORFs are annotated as hypothetical protein genes. Still, there are 233 ORFs uniquely occurring in M. cuprina. Genome annotation supports that M. cuprina lives a facultative life on CO(2) and organics and obtains energy from oxidation of sulfidic ores and reduced inorganic sulfuric compounds.
| S-EPMC3133273 | biostudies-literature
Project description:By using heterotrophic proteome as reference, 169 proteins were found to change their abundance during autotrophic growth. The up-regulated proteins indicated that M. cuprina fixed CO2 through the previously identified 3-HB-CoA/4-HB-CoA cycle and obtained energy by oxidation of elemental sulfur as energy source under autotrophic growth. Enzymes/proteins involved in semi- and non-phosphorylating Entner-Doudoroff (ED) pathway were down-regulated. We also found that some transporter proteins changed their abundances, suggest that they were likely playing pivotal roles for growth under the respective conditions.
2022-02-22 | PXD000676 | Pride
Project description:Metallosphaera cuprina Ar-4 genome sequencing
| PRJNA65497 | ENA
Project description:This experiment aims on the identification of serine hydrolases from a complex thermophile community that live in a hot vent in Kamchatka Peninsula based on in vivo labelling with FP-alkyne directly in the hot spring and subsequent analysis using metagenomics/metaproteomics. To this end, sediment samples were collected and treated using the following three conditions. DMSO- treated control FP-alkyne labelled Samples for each condition were prepared in triplicate, resulting a total number of 6 samples per spring. Labelling was performed using 4 µM of the probe FP-alkyne and incubation for 2 h in the hot spring.
2024-06-03 | PXD025833 | Pride
Project description:Hydrogen served as a competitive inorganic energy source, impacting the CuFeS2 bioleaching efficiency of the extremely thermoacidophilic archaeon Metallosphaera sedula. Open reading frames encoding key terminal oxidase and electron transport chain components were triggered by CuFeS2. Evidence of heterotrophic metabolism was noted after extended periods of bioleaching, presumably related to cell lysis.
2010-03-15 | GSE20554 | GEO
Project description:Increased Acid Resistance of the Archaeon, Metallosphaera sedula by Adaptive Laboratory Evolution
| PRJNA321497 | ENA
Project description:Molecular Hydrogen Impact on Chalcopyrite Bioleaching by the Extremely Thermoacidophilic Archaeon Metallosphaera sedula
| PRJNA125197 | ENA
Project description:In our previous work, we had found that Saccharomyces cerevisiae needs of the Hog1 and Slt2 proteins to growth in a low pH environment caused by sulfuric acid, one of the stress factors during the process of ethanol production. Then was performed the gene-wide expression analysis in the hog1∆ and slt2∆ mutants in order to reveal the function of the Hog1p and Slt2p MAP Kinases in the regulation of S. cerevisiae global gene expression upon stress by sulfuric acid.
2013-10-18 | GSE51353 | GEO