Isolation of the Pseudomonas aeruginosa Gene Affecting Uptake of Dibenzothiophene in n-Tetradecane

スポンサーリンク

概要

• 論文の詳細を見る

• The dsz desulfurization gene cluster from Rhodococcus erythropolis KA2-5-1 was transferred into the chromosomes of Pseudomonas aeruginosa strain NC1MB9571 using a transposon vector. All of the recombinant strains completely desulfurized 1 mM dibenzothiophene (DBT) in n-tetradecane (n-TD) except one, named strain PARM1. Strain PARM1 was unable to desulfurize DBT in n-TD, but was able to desulfurize it in water. The n-alkane utilization ability, the biosurfactant production and the fatty acid composition of cells in strain PARM1 were the same level as those of the other recombinants. The transposon insertion area of strain PARM1 was analyzed by transposon tagging. We cloned three possible open reading frames (ORFs), designated hcuA, hcuB and hcuC, from the genomic DNA of P. aeruginosa NCIMB9571 using the transposon insertion area of strain PARM1 as a DNA probe. Examination of the sequence revealed the transposon was inserted into hcuA. The full length of the hcuABC genes transformed into strain PARM1 achieved 87% recovery of the desulfurization activity of DBT in n-TD, but partial hcuABC genes achieved only 0-12%. These results indicate that DBT desulfurization in the oil phase by recombinant P. aeruginosa strain NCIMB9571 requires the full length of the hcuABC gene cluster. The hcuABC gene cluster relates to DBT uptake from the oil phase to inside of the cell, and the uptake ability is independent of the n-alkane utilization ability, the biosurfactant production and the fatty acid composition of cells.

• 社団法人日本生物工学会の論文
• 2003-05-25

著者

• MARUHASHI KENJI

  Bio-Refining Process Laboratory, Japan Cooperation Center, Petroleum

• Watanabe Katsuyuki

  Pharmacological Research Laboratories Fujisawa Pharmaceutical Co. Ltd.

• Watanabe K

  Division Of Applied Bioscience Graduate School Of Agriculture Hokkaido University

• Noda K

  Bio-refining Process Laboratory Technical Cooperation Department Japan Cooperation Center

• Maruhashi Kenji

  Bio-refining Process Laboratory Technical Cooperation Department Japan Cooperation Center

• NODA KEN-ICHI

  Bio-Refining Process Laboratory Technical Cooperation Department, Japan Cooperation Center

• WATANABE KIMIKO

  Bio-Refining Process Laboratory Technical Cooperation Department, Japan Cooperation Center

• Noda Kenichi

  Bio-Refining Process Laboratory Technical Cooperation Department, Japan Cooperation Center

関連論文

• An Approach to High-Level Production of Cephalosporin Acylase from Pseudomonas strain N176 in Escherichia coli
• Isolation and Characterization of Slime-Producing Bacteria Capable of Utilizing Petroleum Hydrocarbons as a Sole Carbon Source
• Responses of Activated Sludge to an Increase in Phenol Loading
• Effects of Exogenous Phenol-Degrading Bacteria on Performance and Ecosystem of Activated Sludge
• Diversity in Kinetics of Bacterial Phenol-Oxygenating Activity
• Enhancement and Stabilization of Desulfurization Activity of Rhodococcus erythropolis KA2-5-1 by Feeding Ethanol and Sulfur Components(BIOCHEMICAL ENGINEERING)
• Analysis of Dibenzothiophene Metabolic Pathway in Mycobacterium Strain G3
• Analyses of Substrate Specificity of the Desulfurizing Bacterium Mycobacterium sp. G3
• Cloning and Heterologous Expression of a β-Fructofuranosidase Gene from Arthrobacter globiformis IFO 3062, and Site-Directed Mutagenesis of the Essential Aspartic Acid and Glutamic Acid of the Active Site (ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHN
• Cloning and Heterologous Expression of a Glucodextranase Gene from Arthrobacter globiformis I42, and Experimental Evidence for the Catalytic Diad of the Recombinant Enzyme(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
• Cloning of a Gene Cluster Responsible for the Biosynthesis of Diterpene Aphidicolin, a Specific Inhibitor of DNA Polymerase α
• Potent Inhibition of Macrophomate Synthase by Reaction Intermediate Analogs
• Macrophomate Synthase: Characterization, Sequence, and Expression in Escherichia coli of the Novel Enzyme Catalyzing Unusual Multistep Transformation of 2-Pyrones to Benzoates^1
• Kinetic Analysis of Microbial Desulfurization of Model and Light Gas Oils Containing Multiple Alkyl Dibenzothiophenes
• Improvement of Desulfurization Activity in Rhodococcus erythropolis KA2-5-1 by Genetic Engineering
• An Approach to High-Level Production of Mecasermin (Somatomedin C) Fused Protein in Escherichia coli HB101
• Characterization of Starch Synthase I and II Expressed in Early Developing Seeds of Kidney Bean (Phaseolus vulgaris L.)
• Isolation of the Pseudomonas aeruginosa Gene Affecting Uptake of Dibenzothiophene in n-Tetradecane
• Isolation of a Recombinant Desulfurizing 4,6-Dipropyl Dibenzothiophene in n-Tetradecane
• Linking Genetics, Physiology and Ecology : an Interdisciplinary Approach for Advancing Bioremediation(ENVIRONMENTAL BIOTECHNOLOGY)
• Substrate Diversity of Macrophomate Synthase Catalyzing an Unusual Multistep Transformation from 2-Pyrones to Benzoates
• Purification and Characterization of Dibenzothiophene Sulfone Monooxygenase and FMN-Dependent NADH Oxidoreductase from the Thermophilic Bacterium Paenibacillus sp.Strain A11-2
• Cloning and Expression of the Gene Encoding the Thermophilic NAD(P)H-FMN Oxidoreductase Coupling with the Desulfurization Enzymes from Paenibacillus sp.A11-2
• Selective Cleavage of the Two C-S Bonds in Asymmetrically Alkylated Dibenzothiophenes by Rhodococcus erythropolis KA2-5-1
• Desulfurization Characteristics of Thermophilic Paenibacillus sp.Strain A11-2 against Asymmetrically Alkylated Dibenzothiophenes
• A Highly Active Producer of Coproporphyrin III and Uroporphyrin III
• Identification of Porphyrins Produced from Isopropanol by Arthrobacter hyalinus

もっと見る 閉じる

スポンサーリンク