Detoxification of Protoanemonin by Dienelactone Hydrolase

Brückmann, Markus; Blasco, Rafael; Timmis, Kenneth N.; Pieper, Dietmar H.

doi:10.1128/jb.180.2.400-402.1998

Cited by 29 publications

(7 citation statements)

References 23 publications

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“…It has been demonstrated recently that protoanemonin can be transformed, albeit inefficiently, by the dienelactone hydrolase of Pseudomonas sp. B13 to cis-acetylacrylate (Brü ckmann et al, 1998). We therefore tested whether cis-acetylacrylate can serve as a sole source of carbon and energy for MT1 grown in minimal medium.…”

Section: Resultsmentioning

confidence: 99%

Towards elucidation of microbial community metabolic pathways: unravelling the network of carbon sharing in a pollutant‐degrading bacterial consortium by immunocapture and isotopic ratio mass spectrometry

Pelz

Tesar

Wittich

et al. 1999

Environmental Microbiology

138

126

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Although much information on metabolic pathways within individual organisms is available, little is known about the pathways operating in natural communities in which extensive sharing of nutritional resources is the rule. In order to analyse such a consortium pathway, we have investigated the flow of 4-chlorosalicylate as carbon substrate within a simple chemostat microbial community using 13C-labelled metabolites and isotopic ratio mass spectrometric analysis of label enrichment in immunocaptured member populations of the community. A complex pathway network of carbon sharing was thereby revealed, involving two different metabolic routes, one of which is completely novel and involves the toxic metabolite protoanemonin. The high stability of the community results, at least in part, from interdependencies based on carbon sharing and the rapid removal of toxic metabolites.

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Section: Resultsmentioning

confidence: 99%

Towards elucidation of microbial community metabolic pathways: unravelling the network of carbon sharing in a pollutant‐degrading bacterial consortium by immunocapture and isotopic ratio mass spectrometry

Pelz

Tesar

Wittich

et al. 1999

Environmental Microbiology

138

126

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“…Moreover, the fact that the PQS precursors anthranilate and 4-chlorosalicylate follow very similar catabolic pathways via catechols, together with the role of PQS in iron homeostasis, points the attention to the potential role of protoanemonin in this particular regulatory circuit. A possible role could be related to the anthranilate degradation pathway, since protoanemonin is a product of muconate cycloisomerase CatB from the catechol degradation pathway (Brückmann et al, 1998), an intermediate possibly inducing PQS synthesis. As a consequence, the iron starvation response is induced as observed in protoanemonin-treated cultures of P. aeruginosa.…”

Section: Discussionmentioning

confidence: 99%

Protoanemonin: a natural quorum sensing inhibitor that selectively activates iron starvation response

Fazzini

Skindersoe

Bielecki

et al. 2012

Environmental Microbiology

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Many Gram-negative bacteria employ cell-to-cell communication mediated by N-acyl homoserine lactones (quorum sensing) to control expression of a wide range of genes including, but not limited to, genes encoding virulence factors. Outside the laboratory, the bacteria live in complex communities where signals may be perceived across species. We here present a newly found natural quorum sensing inhibitor, produced by the pseudomonads Pseudomonas sp. B13 and Pseudomonas reinekei MT1 as a blind end in the biodegradation of organochloride xenobiotics, which inhibits quorum sensing in P. aeruginosa in naturally occurring concentrations. This catabolite, 4-methylenebut-2-en-4-olide, also known as protoanemonin, has been reported to possess antibacterial properties, but seems to have dual functions. Using transcriptomics and proteomics, we found that protoanemonin significantly reduced expression of genes and secretion of proteins known to be under control of quorum sensing in P. aeruginosa. Moreover, we found activation of genes and gene products involved in iron starvation response. It is thus likely that inhibition of quorum sensing, as the production of antibiotics, is a phenomenon found in complex bacterial communities.

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“…The reactions are catalyzed by the following enzymes: benzoate dioxygenase and dihydrodiol dehydrogenase (reaction A), chlorocatechol 1,2-dioxygenase (B), chloromuconate cycloisomerase (C), dienelactone hydrolase (D) and maleylacetate reductase (E). Dashed arrows possible reactions catalyzed by muconolactone isomerase (F) (Prucha et al 1996a) and muconate cycloisomerase (G) (Bruckmann et al 1998;Vollmer et al 1998), which are expressed in the presence of benzoate…”

Section: Discussionmentioning

confidence: 99%

TfdD II , one of the two chloromuconate cycloisomerases of Ralstonia eutropha JMP134 (pJP4), cannot efficiently convert 2-chloro- cis , cis -muconate to trans -dienelactone to allow growth on 3-chlorobenzoate

Laemmli

Schönenberger

Suter

et al. 2002

Archives of Microbiology

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Ralstonia eutropha JMP134 (pJP4) harbors two functional gene clusters for the degradation of chlorocatechols, i.e. tfdCDEF (in short: tfd (I)) and tfdD (II) C (II) E (II) F (II) (in short: tfd (II)), which are both present on the catabolic plasmid pJP4. In this study, we compared the function of both gene clusters for degradation of chlorocatechols by constructing isolated and hybrid tfd (I)- tfd (II) clusters on plasmids in R. eutropha, by activity assays of Tfd enzymes, and by HPLC/MS of individual enzymatic catalytic steps in chlorocatechol conversion. R. eutropha containing the tfd (II) cluster alone or hybrid tfd-clusters with tfdD (II) as sole gene for chloromuconate cycloisomerase were impaired in growth on 3-chlorobenzoate, in contrast to R. eutrophaharboring the complete tfd (I) cluster. Enzyme activities for TfdD(II) and for TfdE(II) were very low in R. eutropha when induced with 3-chlorobenzoate. By contrast, a relatively high enzyme activity was found for TfdF(II). Spectral conversion assays with extracts from R. eutropha strains expressing tfdD (II) all showed accumulation of a compound with a similar UV spectrum as 2-chloro- cis,cis-muconate from 3-chlorocatechol. HPLC analysis of in vitro assays in which each individual step in 3-chlorocatechol conversion was reproduced by sequentially adding cell extracts of an Escherichia coli expressing one Tfd enzyme only demonstrated that TfdD(II) was unable to cause conversion of 2-chloro- cis,cis-muconate. No accumulation of intermediates was observed with 4-chlorocatechol. From these results, we conclude that at least TfdD(II) is a bottleneck in conversion of 3-chlorocatechol and, therefore, in efficient metabolism of 3-chlorobenzoate. This study showed the subtle functional and expression differences between similar enzymes of the tfd-encoded pathway and demonstrated that extreme care has to be taken when inferring functionality from sequence data alone.

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Detoxification of Protoanemonin by Dienelactone Hydrolase

Cited by 29 publications

References 23 publications

Towards elucidation of microbial community metabolic pathways: unravelling the network of carbon sharing in a pollutant‐degrading bacterial consortium by immunocapture and isotopic ratio mass spectrometry

Towards elucidation of microbial community metabolic pathways: unravelling the network of carbon sharing in a pollutant‐degrading bacterial consortium by immunocapture and isotopic ratio mass spectrometry

Protoanemonin: a natural quorum sensing inhibitor that selectively activates iron starvation response

TfdD II , one of the two chloromuconate cycloisomerases of Ralstonia eutropha JMP134 (pJP4), cannot efficiently convert 2-chloro- cis , cis -muconate to trans -dienelactone to allow growth on 3-chlorobenzoate

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