Pseudothermotoga lettingae TMO
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ABSTRACT:
PROVIDER: PRJNA15644 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:Thermophilic, methanol-degrading organism
| PRJNA35743 | ENA
Project description:Pseudothermotoga elfii strain DSM9442 and P. elfii subsp. lettingae strain TMOT are hyperthermophilic bacteria. P. elfii is a moderate piezophile, isolated from an oil-producing well in Africa at a depth of more than 1600 m. P. lettingae is piezotolerant, isolated from a thermophilic bioreactor fed with methanol as the sole carbon and energy source. In this study, we analysed these bacteria at the genomic and transcriptomic levels. According to the hydrostatic pressure growth conditions the transcriptomic analyses revealed differentially expressed genes emphasizing amino acid and sugars metabolism and transport as the major hydrostatic pressure responding processes. Notably, this work highlights the central role of the amino acid aspartate as key intermediate of the pressure adaptation mechanisms of the deep strain P. elfii DSM 9442. In addition, several differentially expressed genes involved in the membrane and cell wall biosynthesis pathways may be linked to the chain formation morphotype previously described at high pressure for strain P. elfii DSM9442.
2023-03-30 | GSE226101 | GEO
Project description:Methylamine-degrading organism
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Project description:Thermophilic cellulose degrading bacterium
| PRJNA28259 | ENA
Project description:Thermophilic organism found in decaying organic matter.
| PRJNA94 | ENA
Project description:Thermophilic cellulose-degrading bacterium Metagenome
| PRJNA238853 | ENA
Project description:The aim of this study was to unravel the methanol metabolism of Desulfotomaculum kuznetsovii. Anaerobic methylotrophs, such as methanogens and acetogens, use a pathway initiated by a cobalamine-containing methanol methyltransferase, whereas aerobic methylotrophs generally oxidize methanol to formaldehyde through a pathway initiated by a methanol dehydrogenase. Sulfate-respiring cells grown with methanol in the presence and absence of cobalt and vitamin B12 were analyzed and compared with cells grown with lactate or ethanol. Proteome analysis showed the presence of two methanol degrading pathways in D. kuznetsovii: a cobalt-dependent methanol methyltransferase and a cobalt-independent alcohol dehydrogenase. This is the first time that two methanol pathways have been shown to be present in a single microorganism, and we hypothesize this can give D. kuznetsovii a competitive advantage.
2018-01-22 | PXD006899 | Pride
Project description:Methanol is considered as an interesting carbon source in biobased microbial production processes. As Corynebacterium glutamicum is an important host in industrial biotechnology, in particular for amino acid production, we performed studies on the response of this organism to methanol. C. glutamicum wild type was able to convert 13C-labeled methanol to 13CO2. Analysis of global gene expression in the presence of methanol revealed several genes of ethanol catabolism to be up-regulated, indicating that some of the corresponding enzymes are involved in methanol oxidation. Indeed, a mutant lacking the alcohol dehydrogenase gene adhA showed a 62% reduced methanol consumption rate, indicating that AdhA is mainly responsible for methanol oxidation to formaldehyde. Further studies revealed that oxidation of formaldehyde to formate is catalyzed predominantly by two enzymes, the acetaldehyde dehydrogenase Ald and the mycothiol-dependent formaldehyde dehydrogenase AdhE. The deletion mutants aldadhE and aldmshC were severely impaired in their ability to oxidize formaldehyde, but residual methanol oxidation to CO2 was still possible. The oxidation of formate to CO2 is catalyzed by the formate dehydrogenase FdhF recently identified by us. Similar to ethanol, methanol catabolism is subject to carbon catabolite repression in the presence of glucose and is dependent on the transcriptional regulator RamA, which was previously shown to be essential for expression of adhA and ald. In conclusion, we were able to show that C. glutamicum possesses an endogeneous pathway for methanol oxidation to CO2 and to identify the enzymes and a transcriptional regulator involved in this pathway.
2013-09-27 | GSE49936 | GEO