Catechol ring-cleavage in Pseudomonas cepacia : the simultaneous induction of ortho and meta pathways

Hamzah, Riyad Y.; Al-Baharna, B. S.

doi:10.1007/s002530050139

Cited by 12 publications

(15 citation statements)

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“…The blank cuvette contained the same amount of enzyme in the same buffer without catechol added. The activities of catechol 1,2‐dioxygenase and 2,3‐dioxygenase were monitored at 255 and 375 nm, as described by Hamzah and colleagues (1994).…”

Section: Methodsmentioning

confidence: 99%

A pyrene‐degrading consortium from deep‐sea sediment of the West Pacific and its key member Cycloclasticus sp. P1

Wang

Lai

Cui

et al. 2008

Environmental Microbiology

183

135

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A pyrene-degrading bacterial consortium was obtained from deep-sea sediments of the Pacific Ocean. The consortium degraded many kinds of polycyclic aromatic hydrocarbons (PAHs), including naphthalene, phenanthrene, pyrene, acenaphthene, fluorene, anthracene, fluoranthene, 2-methylnaphthalene and 2,6-dimethylnaphthalene, but it did not grow with chrysene and benzo[alpha]pyrene. With methods of plate cultivation and polymerase chain reaction-denaturing gradient gel electrophoresis (PCR-DGGE), 72 bacteria belonging to 22 genera were detected from this consortium. Among the detected bacteria, the following genera frequently occurred: Flavobacterium, Cycloclasticus, Novosphingobium, Halomonas, Achromobacter, Roseovarius and Alcanivorax. The first two genera showed the strongest bands in denaturing gradient gel electrophoresis (DGGE) profiles and appeared in all PAH treatments. By now, only one isolate designated P1 was confirmed to be a pyrene degrader. It was identified to be Cycloclasticus spirillensus (100%). Although P1 can degrade pyrene independently, other bacteria, such as Novosphingobium sp. (Band 14), Halomonas sp. (Band 16) and an unidentified bacterium (Band 35), were involved in pyrene degradation in some way; they persist in the consortium in the test of dilution to extinction if only the consortium was motivated with pyrene. However, the secondary most important member Flavobacterium sp. evaded from the community at high dilutions. As a key member of the consortium, P1 distinguished itself by both cell morphology and carbon source range among the isolates of this genus. Based on intermediate analyses of pyrene degradation, P1 was supposed to take an upper pathway different from that previously reported. Together with the results of obtained genes from P1 homology with those responsible for naphthalene degradation, its degradation to pyrene is supposed to adopt another set of genes unique to presently detected. Summarily, an efficient pyrene-degrading consortium was obtained from the Pacific Ocean sediment, in which Cycloclasticus bacterium played a key role. This is the first report to exploit the diversity of pyrene-degrading bacteria in oceanic environments.

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Section: Methodsmentioning

confidence: 99%

A pyrene‐degrading consortium from deep‐sea sediment of the West Pacific and its key member Cycloclasticus sp. P1

Wang

Lai

Cui

et al. 2008

Environmental Microbiology

183

135

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“…Streptomycetes and their physiologically related actinomycetes are ubiquitous Gram‐positive soil bacteria and some of the most important industrial microorganisms for the biosynthesis of many valuable secondary metabolites, including antibiotics, anti‐cancer drugs, immunosuppressors, and enzyme inhibitors [1]. From an environmental and ecological perspective, they are also valuable due to their capabilities in degrading the diverse structures of various natural and unnatural organic compounds [2–6] like other well‐characterized Gram‐negative [7–11] and some Gram‐positive bacteria [12–16]. Interestingly, the overall characteristics of certain catabolic enzymes involved in aromatic compound metabolism such as catechol 1,2‐dioxygenase (C12O) found in Gram‐positive bacteria seem to be phylogenetically distant from those found in Gram‐negative bacteria, suggesting that the two metabolic systems might have originated from different evolutionary ancestors [12–16].…”

Section: Introductionmentioning

confidence: 99%

An inducibleStreptomycesgene cluster involved in aromatic compound metabolism

Park

Kim

2003

FEMS Microbiology Letters

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Streptomyces setonii (ATCC 39116) is a thermophilic soil actinomycete capable of degrading single aromatic compounds including phenol and benzoate via the ortho-cleavage pathway. Previously, a 6.3-kb S. setonii DNA fragment containing a thermophilic catechol 1,2-dioxygenase (C12O) gene was isolated and functionally overexpressed in Escherichia coli (An et al., FEMS Microbiol. Lett. 195 (2001) 17-22). Here the 6.3-kb S. setonii DNA fragment was shown to be organized into two putative divergently transcribed gene clusters with six complete and one incomplete open reading frames (ORFs). The first cluster with three ORFs showed homologies to previously known benA, benB, and benC, implying it is a part of the benzoate catabolic operon. The second cluster revealed an ortho-cleavage catechol catabolic operon with three translationally coupled ORFs (in order): catR, a putative LysR-type regulatory gene; catB, a muconate cycloisomerase gene; catA, a C12O gene. Each of these individually cloned ORFs was expressed in E. coli and identified as a distinct protein. The expression of the cloned S. setonii catechol operon was induced in Streptomyces lividans by specific single aromatic compounds including catechol, phenol, and 4-chlorophenol. A similar induction pattern was also observed using a luciferase gene-fused reporter system.

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“…Due to the environmental concerns related to these hazardous aromatic compounds, various ways to eliminate or reduce their environmental presence have been pursued including bioremediation using soil microorganisms [7,8]. It has been well documented that certain Gram‐negative soil bacteria, including Pseudomonas or Acinetobacter species, are capable of completely degrading relatively simple aromatic compounds including phenol and benzoate [8,9]. Furthermore, the enzymes and the genes involved in aromatic compound biodegradation have also been intensively elucidated at both biochemical and molecular genetic levels [10,11].…”

Section: Introductionmentioning

confidence: 99%

“…In general, most aromatic compounds are aerobically degraded through a common intermediate, catechol or protocatechuate depending on the chemical structure of the starting compound [10]. The catechol is further degraded either by cleavage between two hydroxyl groups by catechol 1,2‐dioxygenase (C12O) via an ortho ‐pathway or by cleavage adjacent to the hydroxyl groups by catechol 2,3‐dioxygenase via a meta ‐pathway [9,10], respectively. Recently, some Gram‐positive soil bacteria including the Arthrobacter and Rhodococcus species were also isolated from various environments and characterized as containing a similar C12O‐dependent catechol‐degrading ortho ‐pathway like the one found in the Gram‐negative bacteria [12–16].…”

Section: Introductionmentioning

confidence: 99%

Cloning and expression of thermophilic catechol 1,2-dioxygenase gene (catA) fromStreptomyces setonii

Park

Kim

2001

FEMS Microbiology Letters

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Streptomyces setonii (ATCC 39116) degrades various single aromatic compounds such as phenol or benzoate via an ortho-cleavage pathway using catechol 1,2-dioxygenase (C12O). A PCR using degenerate primers based on the conserved regions of known C12O-encoding genes amplified a 0.45-kbp DNA fragment from S. setonii total DNA. A Southern hybridization analysis and size-selected DNA library screening using the 0.45-kbp PCR product as a probe led to the isolation of a 6.4-kbp S. setonii DNA fragment, from which the C12O-encoding genetic locus was found to be located within a 1.4-kbp DNA fragment. A complete nucleotide sequencing analysis of the 1.4-kbp DNA fragment revealed a 0.84-kbp open reading frame, which showed a strong overall amino acid similarity to the known high-G+C Gram-positive (but significantly less to the Gram-negative) bacterial mesophilic C12Os. The heterologous expression of the cloned 1.4-kbp DNA fragment in Escherichia coli demonstrated that this C12O possessed a thermophilic activity within a broad temperature range (up to 65 degrees C) and showed a higher activity against 3-methylcatechol than catechol or 4-methylcatechol, but no activity against protocatechuate.

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Catechol ring-cleavage in Pseudomonas cepacia : the simultaneous induction of ortho and meta pathways

Cited by 12 publications

References 0 publications

A pyrene‐degrading consortium from deep‐sea sediment of the West Pacific and its key member Cycloclasticus sp. P1

A pyrene‐degrading consortium from deep‐sea sediment of the West Pacific and its key member Cycloclasticus sp. P1

An inducibleStreptomycesgene cluster involved in aromatic compound metabolism

Cloning and expression of thermophilic catechol 1,2-dioxygenase gene (catA) fromStreptomyces setonii

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