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Pseudomonas putida

About: Pseudomonas putida is a research topic. Over the lifetime, 6854 publications have been published within this topic receiving 230572 citations.


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TL;DR: Plasmid pAC27, encoding enzymes for 3-chlorobenzoate degradation, does not appear to carry genes for chemotaxis toward chlorinated compounds, and these compounds are chemoattractants for Pseudomonas putida PRS2000.
Abstract: The chlorinated aromatic acids 3-chlorobenzoate and 4-chlorobenzoate are chemoattractants for Pseudomonas putida PRS2000. These compounds are detected by a chromosomally encoded chemotactic response to benzoate which is inducible by beta-ketoadipate, an intermediate of benzoate catabolism. Plasmid pAC27, encoding enzymes for 3-chlorobenzoate degradation, does not appear to carry genes for chemotaxis toward chlorinated compounds.

77 citations

Journal ArticleDOI
TL;DR: The degradazione del bifenile da parte diPs. putida inizia con la formazione di un diolo cui si attribuisce la struttura di 2,3-diidro-2,3 -diossibifeniles, in quanto, per disidratazione a caldo con acido cloridrico, si trasforma in 2,ossibile and tracce di 3,4-diodroid as mentioned in this paper.
Abstract: La degradazione del bifenile da parte diPs. putida inizia con la formazione di un diolo cui si attribuisce la struttura di 2,3-diidro-2,3-diossibifenile, in quanto, per disidratazione a caldo con acido cloridrico, si trasforma in 2-ossibifenile e tracce di 3-ossibifenile. Il diolo viene ulteriormente degradato ad acido benzoico. Le cellule diPs. putida cresciute su bifenile sono simultaneamente indotte ad ossidare al Warburg il bifenile e l'acido benzoico, non il 3,4-diossibifenile e l'acido fenilpiruvico. Le stesse cellule contengono una metapirocatecasi costitutiva.

77 citations

Journal ArticleDOI
TL;DR: Several bacterial cultures were isolated that are able to degrade quinoline and to transform or to degrade methylquinolines and have multiple plasmids including a common 250-kilobase plasmid.
Abstract: Several bacterial cultures were isolated that are able to degrade quinoline and to transform or to degrade methylquinolines. The degradation of quinoline by strains of Pseudomonas aeruginosa QP and P. putida QP produced hydroxyquinolines, a transient pink compound, and other undetermined products. The quinoline-degrading strains of P. aeruginosa QP and P. putida QP hydroxylated a limited number of methylquinolines but could not degrade them, nor could they transform 2-methylquinoline, isoquinoline, or pyridine. Another pseudomonad, Pseudomonas sp. strain MQP, was isolated that could degrade 2-methylquinoline. P. aeruginosa QP was able to degrade or to transform quinoline and a few methylquinolines in a complex heterocyclic nitrogen-containing fraction of a shale oil. All of the quinoline- and methylquinoline-degrading strains have multiple plasmids including a common 250-kilobase plasmid. The 225-, 250-, and 320-kilobase plasmids of the P. aeruginosa QP strain all contained genes involved in quinoline metabolism. Images

77 citations

Journal ArticleDOI
TL;DR: In this article, a novel Gram-positive microorganism from sea water, capable of producing AHL, is reported, which is characterized as C3-oxo-octanoyl homoserine lactone (OOHL), and its production reaches a maximum of 15.6 μg L(-1), during the stationary growth phase of the organism.
Abstract: Acylated homoserine lactone (AHL)-based quorum sensing (QS) has been reported to be present only in Gram-negative microorganisms. Isolation of a novel Gram-positive microorganism from sea water, capable of producing AHL, is reported here. The isolate (GenBank: JF915892, designated as MPO) belonging to the Exiguobacterium genera is capable of inducing the AHL bioreporters, namely Chromobacterium violaceum CV026, Agrobacterium tumefaceins A136, and E. coli JM 109(psb1075). This inducer is characterized as C3-oxo-octanoyl homoserine lactone (OOHL), and its production reaches a maximum of 15.6 μg L(-1), during the stationary growth phase of the organism. MPO extract when exogenously added inhibits the formation of biofilm for the same organism and lowers the extracellular polymeric substances, indicating an AHL-associated phenotypic trait. The isolated sequence of a probable LuxR homolog from MPO (designated as ExgR) shows similar functional domains and contains conserved residues in LuxR from other known bacterial QS LuxR regulators. Also present immediately downstream to ExgR was found a sequence showing homology to known LuxI synthase of Pseudomonas putida. qPCR analysis suggests an increment in exgR mRNA on addition of AHL, further proving the role of ExgR as a QS regulator.

76 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023184
2022345
2021182
2020246
2019226
2018206