title: Bacterial consortium proteomics under 4-chlorosalicylate carbon-limiting conditions.
abstract: 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.
authors.affiliation: Environmental Microbiology Lab, HZI-Helmholtz-Zentrum für Infektionsforschung, Braunschweig, Germany. rbobadi@utem.cl
authors.forename: Roberto A
authors.initials: RA
authors.lastname: Bobadilla Fazzini
authors.forename: Agata
authors.initials: A
authors.lastname: Bielecka
authors.forename: Ana K Poucas
authors.initials: AK
authors.lastname: Quintas
authors.forename: Peter N
authors.initials: PN
authors.lastname: Golyshin
authors.forename: Maria J
authors.initials: MJ
authors.lastname: Preto
authors.forename: Kenneth N
authors.initials: KN
authors.lastname: Timmis
authors.forename: Vitor A P Martins
authors.initials: VA
authors.lastname: dos Santos
mesh_terms: D042441:Achromobacter denitrificans / Q000737:chemistry / Q000378:metabolism*; D001425:Bacterial Outer Membrane Proteins / Q000096:biosynthesis; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000737:chemistry; D050548:Catechol 1,2-Dioxygenase / Q000096:biosynthesis; D006867:Hydrolases / Q000096:biosynthesis; D050540:Ketol-Acid Reductoisomerase / Q000096:biosynthesis; D053858:Metabolic Networks and Pathways; D055442:Metabolome; D006899:Mixed Function Oxygenases / Q000096:biosynthesis; D018384:Oxidative Stress; D010445:Peptide Elongation Factors / Q000096:biosynthesis; D020543:Proteome / Q000096:biosynthesis* / Q000737:chemistry; D011549:Pseudomonas / Q000737:chemistry / Q000378:metabolism*; D012459:Salicylates / Q000378:metabolism*; D013045:Species Specificity; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D010445:Peptide Elongation Factors; D020543:Proteome; D012459:Salicylates; C023512:elongation factor Ts; C479918:4-chlorosalicylic acid; D006899:Mixed Function Oxygenases; D050540:Ketol-Acid Reductoisomerase; D050548:Catechol 1,2-Dioxygenase; C022619:salicylate 1-monooxygenase; D006867:Hydrolases; C019723:arginine deiminase