Mapping of ben genes of Pseudomonas aeruginosa

Zhang, C

doi:10.1016/0378-1097(93)90609-6

Cited by 4 publications

(5 citation statements)

References 6 publications

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“…6), is separated from the antABC genes by approximately one-third of the ADP1 chromosome (16). In contrast, the Pseudomonas aeruginosa ant loci map to a region between the ben and cat genes (50,51). Although the P. aeruginosa ant loci are involved in the catabolism of anthranilate, individual gene functions have not been assigned, nor have these genes been characterized (38).…”

Section: Discussionmentioning

confidence: 99%

“…6) (16). The clustering of many Acinetobacter and Pseudomonas catabolic genes raises questions not only about the evolutionary origin of these regions but also about their relationships with catabolic plasmids (19,50,51). Future studies are needed to determine whether additional genes involved in aromatic compound degradation are in the vicinity of the antABC genes of ADP1.…”

Section: Discussionmentioning

confidence: 99%

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Similarities between the antABC -Encoded Anthranilate Dioxygenase and the benABC -Encoded Benzoate Dioxygenase of Acinetobacter sp. Strain ADP1

1998

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Acinetobacter sp. strain ADP1 can use benzoate or anthranilate as a sole carbon source. These structurally similar compounds are independently converted to catechol, allowing further degradation to proceed via the β-ketoadipate pathway. In this study, the first step in anthranilate catabolism was characterized. A mutant unable to grow on anthranilate, ACN26, was selected. The sequence of a wild-type DNA fragment that restored growth revealed theantABC genes, encoding 54-, 19-, and 39-kDa proteins, respectively. The deduced AntABC sequences were homologous to those of class IB multicomponent aromatic ring-dihydroxylating enzymes, including the dioxygenase that initiates benzoate catabolism. Expression of antABC in Escherichia coli, a bacterium that normally does not degrade anthranilate, enabled the conversion of anthranilate to catechol. Unlike benzoate dioxygenase (BenABC), anthranilate dioxygenase (AntABC) catalyzed catechol formation without requiring a dehydrogenase. In Acinetobacter mutants,benC substituted for antC during growth on anthranilate, suggesting relatively broad substrate specificity of the BenC reductase, which transfers electrons from NADH to the terminal oxygenase. In contrast, the benAB genes did not substitute for antAB. An antA point mutation in ACN26 prevented anthranilate degradation, and this mutation was independent of a mucK mutation in the same strain that prevented exogenous muconate degradation. Anthranilate induced expression of antA, although no associated transcriptional regulators were identified. Disruption of three open reading frames in the immediate vicinity ofantABC did not prevent the use of anthranilate as a sole carbon source. TheantABC genes were mapped on the ADP1 chromosome and were not linked to the two known supraoperonic gene clusters involved in aromatic compound degradation.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Similarities between the antABC -Encoded Anthranilate Dioxygenase and the benABC -Encoded Benzoate Dioxygenase of Acinetobacter sp. Strain ADP1

1998

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“…Sequence comparisons were used to address the evolutionary relationships among various ARHDOs. Previous studies of catabolic mutants and the relative positions of genetic loci (46,47) allowed us to identify the putative AntDO and BenDO sequences of P. aeruginosa. In pairwise comparisons of the deduced sequences of AntDO from Acinetobacter sp.…”

Section: Resultsmentioning

confidence: 99%

“…The ADP1 BenDO and AntDO sequences were compared to six-phase translations of the complete genome sequence of P. aeruginosa PAO1 (http://www.pseudomonas.com) using the BLAST program of the National Center for Biotechnology Information (http://www.ncbi.nlm.nih .gov). Putative antABC and benABC sequences at approximate positions 2829398 and 2835988 were identified on the basis of similarity to ADP1 sequences (52 to 70% identity between homologous deduced protein sequences), restriction site analyses of EcoRI and KpnI recognition sequences from previous studies, and the relative position of cat, ant, and ben genes determined by previous investigations of mutants and mapping studies of mutant loci (46,47).…”

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confidence: 99%

Characterization and Evolution of Anthranilate 1,2-Dioxygenase from Acinetobacter sp. Strain ADP1

Dm¹,

Beharry

et al. 2001

J Bacteriol

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The two-component anthranilate 1,2-dioxygenase of the bacterium Acinetobacter sp. strain ADP1 was expressed in Escherichia coli and purified to homogeneity. This enzyme converts anthranilate Activities of the combined components were measured as rates and quantities of NADH oxidation, substrate disappearance, product appearance, and O 2 consumption. Anthranilate conversion to catechol was stoichiometrically coupled to NADH oxidation and O 2 consumption. The substrate analog benzoate was converted to a nonaromatic benzoate 1,2-diol with similarly tight coupling. This latter activity is identical to that of the related benzoate 1,2-dioxygenase. A variant anthranilate 1,2-dioxygenase, previously found to convey temperature sensitivity in vivo because of a methionine-to-lysine change in the large oxygenase subunit, was purified and characterized. The purified M43K variant, however, did not hydroxylate anthranilate or benzoate at either the permissive (23°C) or nonpermissive (39°C) growth temperatures. The wild-type anthranilate 1,2-dioxygenase did not efficiently hydroxylate methylated or halogenated benzoates, despite its sequence similarity to broad-substrate specific dioxygenases that do. Phylogenetic trees of the ␣ and ␤ subunits of these terminal dioxygenases that act on natural and xenobiotic substrates indicated that the subunits of each terminal oxygenase evolved from a common ancestral two-subunit component.

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“…The enzymes encoded by these chromosome-encoded operons convert benzoate into substrates of the Krebs cycle through catechol-cis,cis-muconate and 3-ketoadipate intermediates (6,23,28). Unlike plain, unsubstituted benzoate, methylbenzoates are neither substrates nor inducers of this ortho cleavage pathway, and therefore, they cannot be metabolized through this route.…”

mentioning

confidence: 99%

Cross talk between catabolic pathways in Pseudomonas putida: XylS-dependent and -independent activation of the TOL meta operon requires the same cis-acting sequences within the Pm promoter

Kessler¹,

Marqués²,

Köhler³

et al. 1994

J Bacteriol

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The Pm promoter of the meta cleavage operon in the TOL (toluene degradation) plasmid pWW0 of Pseudomonas putida becomes activated by the plasmid-encoded XylS regulator in the presence of benzoate and certain substituted analogs such as 3-methylbenzoate. In the absence of XylS, Pm was still responsive to unsubstituted benzoate but with induction kinetics and a range of transcriptional activity which differed substantially from those for the XylS-mediated activation. XylS-independent induction by benzoate did not occur in a rpoN genetic background. Pm was also silent while cells were actively growing in rich medium. However, XylS-dependent transcription and XylS-independent transcription were initiated at the same nucleotide, as determined with primer extension mapping. Furthermore, a series of deletions and mutations at the Pm promoter sequence showed the same overall pattern of responsiveness to benzoate with and without XylS, thus providing genetic evidence that the same promoter structure is recognized and activated by at least two different regulators. One of them is XylS, while the other, provided by the host bacterium, could be related to the chromosome-encoded benzoate degradation pathway.

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Mapping of ben genes of Pseudomonas aeruginosa

Cited by 4 publications

References 6 publications

Similarities between the antABC -Encoded Anthranilate Dioxygenase and the benABC -Encoded Benzoate Dioxygenase of Acinetobacter sp. Strain ADP1

Similarities between the antABC -Encoded Anthranilate Dioxygenase and the benABC -Encoded Benzoate Dioxygenase of Acinetobacter sp. Strain ADP1

Characterization and Evolution of Anthranilate 1,2-Dioxygenase from Acinetobacter sp. Strain ADP1

Cross talk between catabolic pathways in Pseudomonas putida: XylS-dependent and -independent activation of the TOL meta operon requires the same cis-acting sequences within the Pm promoter

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