Cloning and sequence analysis of hydroxyquinol 1,2-dioxygenase gene in 2,4,6-trichlorophenol-degrading Ralstonia pickettii DTP0602 and characterization of its product

Hatta, Takashi; Nakano, Osamu; Imai, Nobuyuki; Takizawa, Noboru; Kiyohara, Hohzoh

doi:10.1016/s1389-1723(99)80030-9

Cited by 39 publications

(35 citation statements)

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“…1). Three published hydroxyquinol dioxygenase gene sequences, i.e., hadC of Burkholderia pickettii (9), tftH of Burkholderia cepacia AC1100 (5), and dxnF of Sphingomonas wittichi RW1 (2), were aligned, and a primer set was designed. With this primer set and the total DNA of strain SAO101 as a template, PCR was carried out.…”

Section: Resultsmentioning

confidence: 99%

“…This ORF showed the highest identity (76%) with ORF2 (hydroxyquinol 1,2-dioxygenase) of Arthrobacter sp. strain and also showed 43 to 52% identity with hydroxyquinol 1,2-dioxygenases from gram-negative bacteria, such as HadC of R. pickettii DTP0602 (9) and TcpC of R. eutropha JMP134 (16). Of the other ORFs found in the sequenced region, the products of ORF5 to -8 showed similarity with a putative secreted protein, a putative YjeB/Rrf2-type transcriptional regulator, a putative SoxR/MerR-type transcriptional regulator, and a putative drug transporter, respectively.…”

Section: Resultsmentioning

confidence: 99%

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A Novel p -Nitrophenol Degradation Gene Cluster from a Gram-Positive Bacterium, Rhodococcus opacus SAO101

2004

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p-Nitrophenol (4-NP) is recognized as an environmental contaminant; it is used primarily for manufacturing medicines and pesticides. To date, several 4-NP-degrading bacteria have been isolated; however, the genetic information remains very limited. In this study, a novel 4-NP degradation gene cluster from a gram-positive bacterium, Rhodococcus opacus SAO101, was identified and characterized. The deduced amino acid sequences of npcB, npcA, and npcC showed identity with phenol 2-hydroxylase component B (reductase, PheA2) of Geobacillus thermoglucosidasius A7 (32%), with 2,4,6-trichlorophenol monooxygenase (TcpA) of Ralstonia eutropha JMP134 (44%), and with hydroxyquinol 1,2-dioxygenase (ORF2) of Arthrobacter sp. strain BA-5-17 (76%), respectively. The npcB, npcA, and npcC genes were cloned into pET-17b to construct the respective expression vectors pETnpcB, pETnpcA, and pETnpcC. Conversion of 4-NP was observed when a mixture of crude cell extracts of Escherichia coli containing pETnpcB and pETnpcA was used in the experiment. The mixture converted 4-NP to hydroxyquinol and also converted 4-nitrocatechol (4-NCA) to hydroxyquinol. Furthermore, the crude cell extract of E. coli containing pETnpcC converted hydroxyquinol to maleylacetate. These results suggested that npcB and npcA encode the two-component 4-NP/4-NCA monooxygenase and that npcC encodes hydroxyquinol 1,2-dioxygenase. The npcA and npcC mutant strains, SDA1 and SDC1, completely lost the ability to grow on 4-NP as the sole carbon source. These results clearly indicated that the cloned npc genes play an essential role in 4-NP mineralization in R. opacus SAO101.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

A Novel p -Nitrophenol Degradation Gene Cluster from a Gram-Positive Bacterium, Rhodococcus opacus SAO101

2004

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“…They can persist for many years in the environment because of their resistance to microbiological degradation. In the last decade, various methods have been proposed to remove phenols, including catalytic oxidation [1,2], photo-oxidation [3], electrochemical oxidation [4], biological degradation [5], ultrafiltration [6] and adsorption [7][8][9][10][11][12][13][14][15]. Since the other methods need special process requirements or special catalysts, adsorption seems to be a good choice in terms of the cost and operation for the removal of phenolic compounds from wastewater.…”

Section: Introductionmentioning

confidence: 99%

Studies on adsorption of phenol and 4-nitrophenol on MgAl-mixed oxide derived from MgAl-layered double hydroxide

Chen

Zhang³

et al. 2009

Separation and Purification Technology

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a b s t r a c tIn this research, the removal of two phenols (4-nitrophenol and phenol) from aqueous solution was investigated using MgAl-mixed oxide. This oxide was prepared by calcining crystalline MgAl-CO 3 -layered double hydroxide (LDH) at 500 • C for 4 h. We found that it takes 10-12 h for adsorption of 4-nitrophenol to reach the equilibrium at room temperature while the equilibrium time is 20-25 h for phenol adsorption. The kinetic process of 4-nitrophenol adsorption seemingly follows the first-order reaction but phenol is adsorbed in a pseudo-second-order model. We also noted that the maximum adsorption amount of 4-nitrophenol by fitted three-parameter Langmuir-Freundlich isotherm is 367.8 mg/g, much higher than that of phenol (46.9 mg/g). The differences in the adsorption kinetics and dynamics have been related to the adsorption mechanism and adsorbate-adsorbent interactions. The reconstruction of MgAl-mixed oxide in aqueous solution incorporates 4-nitrophenolate into the interlayer. However, it is difficult to intercalate phenolate due to its weaker affinity for LDH in comparison with OH − . In addition, adsorption of MgAl-mixed oxide for 4-nitrophenol and phenol is slightly affected by the initial pH, but considerably facilitated by increasing the adsorption temperature.

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“…1b). The 2,4,6-TCP 4-monooxygenase gene (hadA), probable electron transfer protein gene (hadB), hydroxyquinol 1,2-dioxygenase gene (hadC) and maleylacetate reductase gene (hadD) were characterized previously (Hatta et al, 1999;Takizawa et al, 1995). The hadX gene might be the 2,4,6-TCP monooxygenase component of a probable electron transfer gene.…”

Section: Introductionmentioning

confidence: 99%

“…Determination of the HadR mt oligomerization state by gel filtration chromatography was performed as described by Hatta et al (1999). The molecular masses of the subunits and protein concentration were determined by 12.5 % SDS-PAGE and Bradford assay, respectively (Bradford, 1976).…”

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confidence: 99%

The regulatory mechanism of 2,4,6-trichlorophenol catabolic operon expression by HadR in Ralstonia pickettii DTP0602

et al. 2013

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Ralstonia pickettii DTP0602 utilizes 2,4,6-trichlorophenol (2,4,6-TCP) as its sole source of carbon. The expression of catabolic pathway genes (hadA, hadB and hadC) for 2,4,6-TCP has been reported to be regulated by the LysR-type transcriptional regulator (LTTR) HadR. Generally, coinducers are recognized as being important for the function of LTTRs, and alteration of the LTTR-protection sequence and the degree of DNA bending are characteristic of LTTRs with or without a recognized coinducer. In this study, we describe the mechanism by which HadR regulates the expression of 2,4,6-TCP catabolic genes. The 2,4,6-TCP catabolic pathway genes in DTP0602 consist of two transcriptional units: hadX-hadA-hadB-hadC and monocistronic hadR. Purified HadR binds to the hadX promoter and HadR-DNA complex formation was induced in the presence of 16 types of substituted phenols, including chloro-and nitro-phenols and tribromo-phenol. In contrast with observations of other well-characterized LTTRs, the tested phenols showed no diversity of the bending angle of the HadR binding fragment. The expression of 2,4,6-TCP catabolic pathway genes, which are regulated by HadR, was not influenced by the DNA bending angle of HadR. Moreover, the transcription of hadX, hadA and hadB was induced in the presence of seven types of substituted phenols, whereas the other substituted phenols, which induced formation of the HadR-DNA complex, did not induce the transcription of hadX, hadA or hadB in vivo.

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Cloning and sequence analysis of hydroxyquinol 1,2-dioxygenase gene in 2,4,6-trichlorophenol-degrading Ralstonia pickettii DTP0602 and characterization of its product

Cited by 39 publications

References 40 publications

A Novel p -Nitrophenol Degradation Gene Cluster from a Gram-Positive Bacterium, Rhodococcus opacus SAO101

A Novel p -Nitrophenol Degradation Gene Cluster from a Gram-Positive Bacterium, Rhodococcus opacus SAO101

Studies on adsorption of phenol and 4-nitrophenol on MgAl-mixed oxide derived from MgAl-layered double hydroxide

The regulatory mechanism of 2,4,6-trichlorophenol catabolic operon expression by HadR in Ralstonia pickettii DTP0602

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