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Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
Published on: November 15, 2017
Photobacterium profundum under pressure: a MS-based label-free quantitative proteomics study
Thierry Le Bihan1, Joe Rayner, Marcia M Roy
1SynthSys, The University of Edinburgh, Edinburgh, United Kingdom. thierry.lebihan@ed.ac.uk
Plos One
|June 7, 2013
Summary
This study reveals how the deep-sea bacterium Photobacterium profundum adapts to high pressure by altering protein expression in key metabolic pathways like glycolysis and oxidative phosphorylation.
Area of Science:
- Microbiology
- Biochemistry
- Proteomics
Background:
- Photobacterium profundum SS9 is a piezophilic bacterium, thriving under high hydrostatic pressure.
- Its ability to grow at atmospheric pressure makes it a valuable model for studying piezophily.
- Understanding pressure adaptation is crucial for deep-sea microbiology.
Purpose of the Study:
- To investigate proteomic changes in P. profundum under different hydrostatic pressures.
- To identify proteins involved in high-pressure adaptation and metabolic shifts.
- To explore the direct impact of pressure on protein expression and nutrient assimilation.
Main Methods:
- Shotgun proteomic analysis using label-free quantitation.
- Mass spectrometry to identify and quantify proteins.
- Comparison of P. profundum proteomes at atmospheric vs. high pressure.
Main Results:
- Identified differentially expressed proteins related to high-pressure adaptation.
- Observed upregulation of glycolysis/gluconeogenesis proteins at high pressure.
- Noted upregulation of oxidative phosphorylation proteins at atmospheric pressure.
- Suggested direct pressure regulation of some nutrient transport and assimilation proteins.
Conclusions:
- Hydrostatic pressure significantly impacts P. profundum's proteome and metabolic pathways.
- Specific proteins are likely directly regulated by pressure, influencing adaptation.
- This research provides insights into the molecular mechanisms of piezophily.
