Analysis and Manipulation of Plasmid-Encoded Pathways for the Catabolism of Aromatic Compounds by Soil Bacteria

Timmis, Kenneth N.; Lehrbach, P. R.; Harayama, Shigeaki; Don, R. H.; Mermod, Nicolas; Bas, Sylvette; Leppik, R A; Weightman, Andrew J.; Reineke, Walter; Knackmuss, Hans‐Joachim

doi:10.1007/978-1-4613-2447-8_50

Cited by 32 publications

(16 citation statements)

References 28 publications

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“…Interestingly, a substantial number of aromatic catabolic pathways are plasmid encoded, and some of them have been elucidated in detail in terms of their biochemistry, organization, and regulation of the genes (15,23,33,40).…”

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Characterization of an Escherichia coli aromatic hydroxylase with a broad substrate range

1993

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“…The specificities of enzymes that catalyze hydroxylation are one of the factors which determine the type of compounds metabolized by the cell (12,18,40). When 4-HPA can be used as a growth substrate, two metabolic routes are available.…”

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Characterization of an Escherichia coli aromatic hydroxylase with a broad substrate range

1993

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“…Several genera of soil bacteria are known to degrade and utilize a variety of these compounds via the presence of partial or complete catabolic pathways encoded by large plasmids. The enzymes responsible for catalyzing the initial steps in the degradative pathways are of particular interest because of their potential use in the development of bacteria and plants capable of degrading and detoxifying xenobiotic compounds (10,17,20).The plasmid pJP4 of Alcaligenes eutrophus JMP134 encodes enzymes for the catabolism of 2,4-dichlorophenoxyacetic acid (2,4-D) and 3-chlorobenzoate (3-CBA) (5, 7). The first enzyme in the 2,4-D catabolic pathway cleaves the ether linkage of 2,4-D to produce glyoxylate and 2,4-dichlorophenol (2,4-DCP).…”

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Duplication of a 2,4-dichlorophenoxyacetic acid monooxygenase gene in Alcaligenes eutrophus JMP134(pJP4)

Perkins

Lurquin

1988

J Bacteriol

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The Alcaligenes eutrophus JMP134 plasmid pJP4 contains genes necessary for the complete degradation of 2,4-dichlorophenoxyacetic acid (2,4-D) and 3-chlorobenzoic acid. tfdA encodes 2,4-D monooxygenase, the initial enzyme in the 2,4-D catabolic pathway. The (fdA locus has recently been localized to a region on pJP4 13 kilobases away from a cluster of five genes, #'dB to ifdF, which encode the enzymes responsible for the further degradation of 2,4-D to chloromaleylacetic acid (W. R. Streber, K. N. Timmis, and M. H. Zenk, J. Bacteriol. 169:2950-2955. A second, dissimilar locus on pJP4, fdAII, has been observed which encodes 2,4-D monooxygenase activity. Gas chromatographic analysis of the 2,4-D metabolites of A. eutrophus harboring pJP4 or subclones thereof localized fd4AII to within a 9-kilobase SstI fragment of pJP4 which also carries the genes #fdBCDEF. This fragment was further characterized in Escherichia coli by deletion and subcloning analysis. A region of 2.5 kilobases, adjacent to afdC, enabled E. coli extracts to degrade 2,4-D to 2,4-dichlorophenol. Hybridization under low-stringency conditions was observed between tfdA and ifdAII, signifying that the 2,4-D monooxygenase gene was present as two related copies on pJP4.Halogenated aromatics have become increasingly prevalent in our environment as a result of industrial pollution and herbicide use in agriculture. Several genera of soil bacteria are known to degrade and utilize a variety of these compounds via the presence of partial or complete catabolic pathways encoded by large plasmids. The enzymes responsible for catalyzing the initial steps in the degradative pathways are of particular interest because of their potential use in the development of bacteria and plants capable of degrading and detoxifying xenobiotic compounds (10,17,20).The plasmid pJP4 of Alcaligenes eutrophus JMP134 encodes enzymes for the catabolism of 2,4-dichlorophenoxyacetic acid (2,4-D) and 3-chlorobenzoate (3-CBA) (5, 7). The first enzyme in the 2,4-D catabolic pathway cleaves the ether linkage of 2,4-D to produce glyoxylate and 2,4-dichlorophenol (2,4-DCP). Five genes, tfdB to tfdF, converting 2,4-DCP to chloromaleylacetic acid, are located on a 6.3-kilobase (kb) region of EcoRI fragment B (7) (Fig. 1). A gene encoding 2,4-D monooxygenase, tfdA, has been localized to a region 13 kb distant from the tfdBCDEF genes (19) (Fig. 1).When grown on 3-chlorobenzoate as a sole carbon source, pJP4 can undergo a wide variety of genetic rearrangements (10). This may reflect a capacity of the bacterium to adapt itself to grow more efficiently under different environmental conditions. Such rearrangements include deletions and duplications of specific regions of the plasmid. We have found a second locus which encodes an additional 2,4-D monooxygenase activity in pJP4. We have designated the enzyme 2,4-D monooxygenase II and the gene tfdAII. This locus was found adjacent to the gene encoding chlorocatechol 1,2-dioxygenase, tfdC. The tfdAII locus is clustered with genes tfdBCDEF on plasmid pJP4...

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“…Members of the genus Pseudomonas are attractive biocatalysts for the production of chemicals because of their ability to oxidize a wide variety of organic compounds (11,(14)(15)(16)(17). The metabolic diversity of many pseudomonads is attributable to plasmid-encoded metabolic sequences (10, 17).…”

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Recruitment of naphthalene dissimilatory enzymes for the oxidation of 1,4-dichloronaphthalene to 3,6-dichlorosalicylate, a precursor for the herbicide dicamba

Durham¹,

Stewart²

1987

J Bacteriol

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Pseudomonas putida expresses plasmid-encoded enzymes and regulatory proteins for the dissimilation of naphthalene through salicylate and the a-keto acid pathway. A strain of P. putida (NAH:TnS/G67) defective in salicylate hydroxylase (nahG) was assessed for its ability to oxidize 1,4-dichloronaphthalene. Washed cell suspensions were shown to accumulate 3,6-dichlorosalicylate, which, after further chemical treatment, yields the herbicide dicamba (3,6-dichloro-2-methoxybenzoate). However, the rate of dichiorosalicylate formation from dichloronaphthalene was less than 1% of the rate of salicylate formation from unsubstituted naphthalene.Recent advances in biotechnology have resulted in the development of microorganisms for the production of chemicals and the detoxification of chemical wastes. Members of the genus Pseudomonas are attractive biocatalysts for the production of chemicals because of their ability to oxidize a wide variety of organic compounds (11,(14)(15)(16)(17). The metabolic diversity of many pseudomonads is attributable to plasmid-encoded metabolic sequences (10, 17). In general, plasmid-borne dissimilatory enzymes exhibit relaxed substrate specificity (8, 12) and thus can be used for the oxidation of substrate analogs. The most thoroughly characterized degradative plasmids are the NAH7 plasmid, which specifies naphthalene dissimilation (2, 22), and the TOL plasmid (pWWO), which provides genetic information for the degradation of toluenes, xylenes, and related compounds (7,20,21). Genetic manipulations of these plasmids have resulted in the construction of strains with extended metabolic capabilities (8,12,17,23) and the production of chemical products such as indigo (5, 9), catechol (23), cis-dihydrodiols (1, 13, 23), salicylate (4, 22), and cresols (19).Naphthalene is degraded by P. putida through catechol and the a-keto acid or meta cleavage pathway (2, 24). The NAH7 degradative plasmid is composed of two gene clusters with an intervening regulatory region (22). The first cluster encodes for the oxidation of naphthalene to salicylate (Fig.

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Analysis and Manipulation of Plasmid-Encoded Pathways for the Catabolism of Aromatic Compounds by Soil Bacteria

Cited by 32 publications

References 28 publications

Characterization of an Escherichia coli aromatic hydroxylase with a broad substrate range

Characterization of an Escherichia coli aromatic hydroxylase with a broad substrate range

Duplication of a 2,4-dichlorophenoxyacetic acid monooxygenase gene in Alcaligenes eutrophus JMP134(pJP4)

Recruitment of naphthalene dissimilatory enzymes for the oxidation of 1,4-dichloronaphthalene to 3,6-dichlorosalicylate, a precursor for the herbicide dicamba

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