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Proteomics data for characterizing Microbacterium oleivorans A9, an uranium-tolerant actinobacterium isolated near the Chernobyl nuclear power plant.


ABSTRACT: Microbacterium oleivorans A9 cells were exposed or not to 10?µM uranyl nitrate as resting cells in sodium chloride solution. Bacteria exposed to U(VI) and controls were harvested after 0.5, 4, and 24?h of toxicant exposure. Bacteria were subjected to high-throughput proteomics analysis using a Q-Exactive HF high resolution tandem mass spectrometer incorporating an ultra-high-field orbitrap analyzer. MS/MS spectra were assigned with a protein sequence database derived from a draft genome obtained by Illumina sequencing and systematic six-reading frame translation of all the contigs. Proteins identified in bacteria exposed to U(VI) and controls at the three time points allow defining the proteome dynamics upon uranium stress. The data reported here are related to a published study regarding the proteome dynamics of M. oleivorans A9 upon uranium stress by Gallois et al. (in press) entitled "Proteogenomic insights into uranium tolerance of a Chernobyl?s Microbacterium bacterial isolate". The data accompanying the manuscript describing the database searches and comparative analysis have been deposited to the ProteomeXchange with identifier PXD005794.

SUBMITTER: Gallois N 

PROVIDER: S-EPMC6231083 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature

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Proteomics data for characterizing <i>Microbacterium oleivorans A9</i>, an uranium-tolerant actinobacterium isolated near the Chernobyl nuclear power plant.

Gallois Nicolas N   Piette Laurie L   Ortet Philippe P   Barakat Mohamed M   Long Justine J   Berthomieu Catherine C   Armengaud Jean J   Chapon Virginie V   Alpha-Bazin Béatrice B  

Data in brief 20181030


<i>Microbacterium oleivorans</i> A9 cells were exposed or not to 10 µM uranyl nitrate as resting cells in sodium chloride solution. Bacteria exposed to U(VI) and controls were harvested after 0.5, 4, and 24 h of toxicant exposure. Bacteria were subjected to high-throughput proteomics analysis using a Q-Exactive HF high resolution tandem mass spectrometer incorporating an ultra-high-field orbitrap analyzer. MS/MS spectra were assigned with a protein sequence database derived from a draft genome o  ...[more]

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