Over het archief
Het OWA, het open archief van het Waterbouwkundig Laboratorium heeft tot doel alle vrij toegankelijke onderzoeksresultaten van dit instituut in digitale vorm aan te bieden. Op die manier wil het de zichtbaarheid, verspreiding en gebruik van deze onderzoeksresultaten, alsook de wetenschappelijke communicatie maximaal bevorderen.
Dit archief wordt uitgebouwd en beheerd volgens de principes van de Open Access Movement, en het daaruit ontstane Open Archives Initiative.
Basisinformatie over ‘Open Access to scholarly information'.
Proteogenomic analysis of Epibacterium Mobile BBCC367, a relevant marine bacterium isolated from the South Pacific Ocean
Matallana-Surget, S.; Werner, J.; Wattiez, R.; Lebaron, K.; Intertaglia, L.; Regan, C.; Morris, J.; Teeling, H.; Ferrer, M.; Golyshin, P.N.; Gerogiorgis, D.; Reilly, S.I.; Lebaron, P. (2018). Proteogenomic analysis of Epibacterium Mobile BBCC367, a relevant marine bacterium isolated from the South Pacific Ocean. Front. Microbiol. 9: 3125. https://dx.doi.org/10.3389/fmicb.2018.03125
In: Frontiers in Microbiology. Frontiers Media: Lausanne. ISSN 1664-302X; e-ISSN 1664-302X, meer
| |
Trefwoorden |
Epibacterium mobile Marien/Kust |
Author keywords |
Epibacterium mobile; proteogenomic; roseobacter; stress response andadaptation; quantitative proteomics |
Auteurs | | Top |
- Matallana-Surget, S.
- Werner, J.
- Wattiez, R., meer
- Lebaron, K.
- Intertaglia, L.
|
- Regan, C.
- Morris, J.
- Teeling, H.
- Ferrer, M.
|
- Golyshin, P.N., meer
- Gerogiorgis, D.
- Reilly, S.I.
- Lebaron, P., meer
|
Abstract |
Epibacterium mobile BBCC367 is a marine bacterium that is common in coastal areas. It belongs to the Roseobacter clade, a widespread group in pelagic marine ecosystems. Species of the Roseobacter clade are regularly used as models to understand the evolution and physiological adaptability of generalist bacteria. E. mobile BBCC367 comprises two chromosomes and two plasmids. We used gel-free shotgun proteomics to assess its protein expression under 16 different conditions, including stress factors such as elevated temperature, nutrient limitation, high metal concentration, and UVB exposure. Comparison of the different conditions allowed us not only to retrieve almost 70% of the predicted proteins, but also to define three main protein assemblages: 584 essential core proteins, 2,144 facultative accessory proteins and 355 specific unique proteins. While the core proteome mainly exhibited proteins involved in essential functions to sustain life such as DNA, amino acids, carbohydrates, cofactors, vitamins and lipids metabolisms, the accessory and unique proteomes revealed a more specific adaptation with the expression of stress-related proteins, such as DNA repair proteins (accessory proteome), transcription regulators and a significant predominance of transporters (unique proteome). Our study provides insights into how E. mobile BBCC367 adapts to environmental changes and copes with diverse stresses. |
IMIS is ontwikkeld en wordt gehost door het VLIZ.