Kyrpidia spormannii strain:EA-1
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA419228 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| GCA_002804065.1_sequence_report.txt | Txt |
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Project description:The biotechnological usage of carbon dioxide has become a relevant aim for future processes. Microbial electrosynthesis is a rather new technique to energize biological CO2 fixation with the advantage to establish a continuous process based on a cathodic biofilm that is supplied with renewable electrical energy as electron and energy source. In this study, the recently characterized cathodic biofilm forming microorganism Kyrpidia spormannii strain EA-1 was used in an adaptive laboratory evolution experiment to enhance its cathodic biofilm growth capabilities. At the end of the experiment, the adapted cathodic population exhibited an up to fourfold higher biofilm accumulation rate, as well as faster substratum coverage and a more uniform biofilm morphology compared to the progenitor strain. Genomic variant analysis revealed a genomically heterogeneous population with genetic variations occurring to various extends throughout the community. Via the conducted analysis we identified possible targets for future genetic engineering with the aim to further optimize cathodic growth. Moreover, the results assist in elucidating the underlying processes that enable cathodic biofilm formation.
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Project description:Ruminiclostridium thermocellum DSM 1313 strain adhE*(EA) expression was studied along with ∆hydG and ∆hydG∆ech mutants strains deposited under GSE54082. All strains have been described in a study entitled Elimination of hydrogenase post-translational modification blocks H2 production and increases ethanol yield in Clostridium thermocellum. Biswas, et .al. Biotechnology for Biofuels 2015 8:20 Ruminiclostridium (Clostridium) thermocellum is a leading candidate organism for implementing a consolidated bioprocessing (CBP) strategy for biofuel production due to its native ability to rapidly consume cellulose and its existing ethanol production pathway. C. thermocellum converts cellulose and cellobiose to lactate, formate, acetate, H2, ethanol, amino acids, and other products. Elimination of the pathways leading to products such as H2 could redirect carbon flux towards ethanol production. Rather than delete each hydrogenase individually, we targeted a hydrogenase maturase gene (hydG), which is involved in converting the three [FeFe] hydrogenase apoenzymes into holoenzymes by assembling the active site. This functionally inactivated all three Fe-Fe hydrogenases simultaneously, as they were unable to make active enzymes. In the ∆hydG mutant, the [NiFe] hydrogenase-encoding ech was also deleted to obtain a mutant that functionally lacks all hydrogenase. The ethanol yield increased nearly 2-fold in ∆hydG∆ech compared to wild type, and H2 production was below the detection limit. Interestingly, ∆hydG and ∆hydG∆ech exhibited improved growth in the presence of acetate in the medium. Transcriptomic and proteomic analysis reveal that genes related to sulfate transport and metabolism were up-regulated in the presence of added acetate in ∆hydG, resulting in altered sulfur metabolism. Further genomic analysis of this strain revealed a mutation in the bi-functional alcohol/aldehyde dehydrogenase adhE gene, resulting in a strain with both NADH- and NADPH-dependent alcohol dehydrogenase activities, whereas the wild type strain can only utilize NADH. This is the exact same adhE mutation found in ethanol-tolerant C. thermocellum strain E50C, but ∆hydG∆ech is not more ethanol tolerant than the wild type. Targeting protein post-translational modification is a promising new approach to target multiple enzymes simultaneously for metabolic engineering. This GEO study pertains to expression profiles generated for C. thermocellum DSM 1313 strain adhE*(EA)
2017-02-01 | GSE77273 | GEO