Language：English   Publishing type：Research paper (scientific journal)  

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Language：English   Publishing type：Research paper (scientific journal)  

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Language：English   Publishing type：Research paper (scientific journal)  

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Language：English   Publishing type：Research paper (scientific journal)  

Rhodococcus erythropolis TA421, a polychlorinated biphenyl and biphenyl degrader isolated from a termite ecosystem, has seven bphC genes expressing 2,3-dihydroxybiphenyl dioxygenase activity. R. erythropolis TA421 harbored a large and probably linear plasmid on which three (bphC2, bphC3, and bphC4) of the seven bphC genes were located. A non-biphenyl-degrading mutant, designated strain TA422, was obtained spontaneously from R. erythropolis TA421. TA422 lacked the plasmid, suggesting that the three bphC genes were involved in the degrdn. of biphenyl. Southern blot analyses showed that R. erythropolis TA421 and Rhodococcus globerulus P6 have a similar set of bphC genes and that the genes for biphenyl catabolism are located on plasmids of different sizes. These results indicated that the genes encoding the biphenyl catabolic pathway in Rhodococcus strains are borne on plasmids.

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Language：English   Publishing type：Research paper (scientific journal)  

The solvent-tolerant biphenyl/polychlorinated biphenyl (PCB) degraders Pseudomonas putida strain CE2010, Alcaligenes xylosoxydans ssp. denitrificans strain YO129, and Alcaligenes xylosoxydans strain A41 were isolated and characterized in comparison with other biphenyl/PCB or toluene-degrading bacteria. Among the biphenyl/PCB or toluene-degrading bacteria, Pseudomonas putida CE2010 showed the highest solvent-tolerance.

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Language：English   Publishing type：Research paper (international conference proceedings)  

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Language：English   Publishing type：Research paper (scientific journal)  

Rhodococcus erythropolis TA421 was isolated from a termite ecosystem and is able to degrade a wide range of polychlorinated biphenyl (PCB) congeners. Genetic and biochem. analyses of the PCB catabolic pathway of this organism revealed that there are 4 different bphC genes (bphC1, bphC2, bphC3, and bphC4) which encode 2,3-dihydroxybiphenyl dioxygenases. As detd. by Southern hybridization, none of the bphC genes exhibits homol. to any other bphC gene. BphC1, bphC2, and bphC4 encode enzymes that have narrow substrate specificities and cleave the first arom. ring in the meta position. In contrast, bphC3 encodes a meta cleavage dioxygenase with broad substrate specificity. J. A. Asturias et al. (1994) have shown that the closely related organism Rhodococcus globerulus P6 contains 3 different bphC genes (bphC1, bphC2, and bphC3) which encode meta cleavage dioxygenases. The data suggest that there is a diverse family of bphC genes which encode PCB meta cleavage dioxygenases in members of the genus Rhodococcus.

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Language：English   Publishing type：Research paper (scientific journal)  

Gram-pos. bacteria, identified as Rhodococcus erythropolis, were isolated from the ecosystem of the wood-feeding termite Reticulitermes speratus and found to aerobically degrade polychlorinated biphenyl (PCB) compds. Rhodococcus erythropolis stain TA421 and strain TA431 were isolated by enrichment culture from termites obtained from different locations and each was found to be capable of degrading polychlorinated biphenyl (PCB) compds. to chlorobenzoates. These results suggest that the termite ecosystem is one possible habitat for biphenyl- and PCB-degrading Rhodococci. The spectrum of PCB-congeners degraded by strain TA421 is different from that of other, previously characterized PCB-degrading bacteria such as Rhodococcus globerulus strain P6 (formerly Corynebacterium sp. strain MB1) or Pseudomonas sp. strain LB400.

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Language：English   Publishing type：Research paper (scientific journal)  

The urease of thermophilic Bacillus sp. strain TB-90 is composed of 3 subunits with mol. masses of 61, 12, and 11 kDa. By using synthetic oligonucleotide probes based on N-terminal amino acid sequence of each subunit, a 3.2-kb EcoRI fragment of TB-90 genomic DNA was cloned. Moreover, 2 two other DNA fragments were cloned by gene walking starting from this fragment. Finally, a 6.2-kb DNA fragment which expressed catalytically active urease in Escherichia coli was reconstructed in vitro by combining these 3 DNA fragments. Nucleotide sequencing anal. revealed that the urease gene complex consists of 9 genes, which were designated ureA, ureB, ureC, ureE, ureF, ureG, ureD, ureH, and ureI in order of arrangement. The structural genes ureA, ureB, and ureC encode the 11-, 12-, and 61-kDa subunits, resp. The deduced amino acid sequences of UreD, UreE, UreF, and UreG, the gene products of the accessory genes, are homologous to those of the corresponding Ure proteins of Klebsiella aerogenes. UreD, UreF, and UreG were essential for expression of urease activity in E. coli and are suggested to play important roles in the maturation step of the urease in a co- and/or posttranslational manner. On the other hand, UreH and UreI exhibited no significant similarity to the known accessory proteins of other bacteria. However, UreH showed 23% amino acid identity to the Alcaligenes eutrophus HoxN protein, a high-affinity nickel transporter.

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Language：Japanese   Presentation type：Oral presentation (general)  

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Language：Japanese   Presentation type：Oral presentation (general)  

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Language：Japanese   Presentation type：Oral presentation (general)  

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Language：Japanese   Presentation type：Oral presentation (general)  

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Language：Japanese   Presentation type：Oral presentation (general)  

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Language：Japanese   Presentation type：Oral presentation (general)  

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Language：Japanese   Presentation type：Oral presentation (general)  

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Language：English   Presentation type：Oral presentation (general)  

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Language：Japanese   Presentation type：Oral presentation (general)  

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Language：Japanese   Presentation type：Oral presentation (general)  

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Language：Japanese   Presentation type：Oral presentation (general)  

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Language：Japanese   Presentation type：Oral presentation (general)  

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Language：Japanese   Presentation type：Oral presentation (general)  

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Language：Japanese   Presentation type：Oral presentation (general)  

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Language：Japanese   Presentation type：Oral presentation (general)  

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Language：Japanese   Presentation type：Oral presentation (general)  

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Language：Japanese   Presentation type：Oral presentation (general)  

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Language：Japanese   Presentation type：Oral presentation (general)  

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Language：Japanese   Presentation type：Oral presentation (general)  

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Language：Japanese   Presentation type：Oral presentation (general)  

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Language：Japanese   Presentation type：Oral presentation (general)  

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Language：Japanese   Presentation type：Oral presentation (general)  

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Language：Japanese   Presentation type：Oral presentation (general)  

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Language：Japanese   Presentation type：Oral presentation (general)  

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Language：Japanese   Presentation type：Oral presentation (general)  

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Language：Japanese   Presentation type：Oral presentation (general)  

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Language：Japanese   Presentation type：Oral presentation (general)  

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Language：Japanese   Presentation type：Oral presentation (general)  

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