Bacterial consortium proteomics under 4-chlorosalicylate carbon-limiting conditions
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DOI
In this study, the stable consortium composed by Pseudomonas reinekei strain MT1 and Achromobacter xylosoxidans strain MT3 (cell numbers in proportion 9:1) was under investigation to reveal bacterial interactions that take place under severe nutrient-limiting conditions. The analysis of steady states in continuous cultures was carried out at the proteome, metabolic profile, and population dynamic levels. Carbon-limiting studies showed a higher metabolic versatility in the community through upregulation of parallel catabolic enzymes (salicylate 5-hydroxylase and 17-fold on 2-keto-4-pentenoate hydratase) indicating a possible alternative carbon routing in the upper degradation pathway highlighting the effect of minor proportions of strain MT3 over the major consortia component strain MT1 with a significant change in the expression levels of the enzymes of the mainly induced biodegradation pathway such as salicylate 1-hydroxylase and catechol 1,2-dioxygenase together with important changes in the outer membrane composition of P. reinekei MT1 under different culture conditions. The study has demonstrated the importance of the outer membrane as a sensing/response protective barrier caused by interspecies interactions highlighting the role of the major outer membrane proteins OprF and porin D in P. reinekei sp. MT1 under the culture conditions tested.
Keywords
- Achromobacter denitrificans/chemistry, Bacterial Outer Membrane Proteins/biosynthesis, Bacterial Proteins/biosynthesis, Catechol 1,2-Dioxygenase/biosynthesis, Hydrolases/biosynthesis, Ketol-Acid Reductoisomerase/biosynthesis, Metabolic Networks and Pathways, Metabolome, Mixed Function Oxygenases/biosynthesis, Oxidative Stress, Peptide Elongation Factors/biosynthesis, Proteome/biosynthesis, Pseudomonas/chemistry, Salicylates/metabolism, Species Specificity, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Original language | English |
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Pages (from-to) | 2273-85 |
Number of pages | 13 |
Journal | Proteomics |
Volume | 9 |
Issue number | 8 |
DOIs | |
Publication status | Published - Apr 2009 |