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CitationNamesAbstract
Metatranscriptomics Supports the Mechanism for Biocathode Electroautotrophy by “CandidatusTenderia electrophaga” Eddie et al. (2017). mSystems 2 (2) Tenderia electrophaga Ts
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Proteome Remodeling in Response to Sulfur Limitation in “ Candidatus Pelagibacter ubique” Smith et al. (2016). mSystems 1 (4) Pelagibacter ubiqueversans Ts
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Metatranscriptomics Supports the Mechanism for Biocathode Electroautotrophy by “CandidatusTenderia electrophaga”
Bacteria that directly use electrodes as metabolic electron donors (biocathodes) have been proposed for applications ranging from microbial electrosynthesis to advanced bioelectronics for cellular communication with machines. However, just as we understand very little about oxidation of analogous natural insoluble electron donors, such as iron oxide, the organisms and extracellular electron transfer (EET) pathways underlying the electrode-cell direct electron transfer processes are almost completely unknown. Biocathodes are a stable biofilm cultivation platform to interrogate both the rate and mechanism of EET using electrochemistry and to study the electroautotrophic organisms that catalyze these reactions. Here we provide new evidence supporting the hypothesis that the uncultured bacterium “CandidatusTenderia electrophaga” directly couples extracellular electron transfer to CO2fixation. Our results provide insight into developing biocathode technology, such as microbial electrosynthesis, as well as advancing our understanding of chemolithoautotrophy.
Proteome Remodeling in Response to Sulfur Limitation in “ Candidatus Pelagibacter ubique”
“ Ca . Pelagibacter ubique” is a key driver of marine biogeochemistry cycles and a model for understanding how minimal genomes evolved in free-living anucleate organisms. This study explores the unusual sulfur acquisition strategy that has evolved in these cells, which lack assimilatory sulfate reduction and instead rely on reduced sulfur compounds found in oxic marine environments to meet their cellular quotas. Our findings demonstrate that the sulfur acquisition systems are constitutively expressed but the enzymatic steps leading to the essential sulfur-containing amino acid methionine are regulated by a unique array of riboswitches and genes, many of which are encoded in a rapidly evolving genome region. These findings support mounting evidence that streamlined cells have evolved regulatory mechanisms that minimize transcriptional switching and, unexpectedly, localize essential sulfur acquisition genes in a genome region normally associated with adaption to environmental variation.
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