메뉴 건너뛰기




Volumn 71, Issue 11, 2005, Pages 6538-6544

Novel 4-chlorophenol degradation gene cluster and degradation route via hydroxyquinol in Arthrobacter chlorophenolicus A6

Author keywords

[No Author keywords available]

Indexed keywords

BIODEGRADATION; ENZYMES; GENE TRANSFER; GENES; PHENOLS;

EID: 32044453568     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.71.11.6538-6544.2005     Document Type: Article
Times cited : (107)

References (32)
  • 1
    • 0023445075 scopus 로고
    • Complete dechlorination of tetrachlorohydroquinone by cell extracts of pentachlorophenol-induced Rhodococcus chlorophenolicus
    • Apajalahti, J. H. A., and M. S. Salkinoja-Salonen. 1987. Complete dechlorination of tetrachlorohydroquinone by cell extracts of pentachlorophenol-induced Rhodococcus chlorophenolicus. J. Bacteriol. 169:5125-5130.
    • (1987) J. Bacteriol. , vol.169 , pp. 5125-5130
    • Apajalahti, J.H.A.1    Salkinoja-Salonen, M.S.2
  • 2
    • 0033040221 scopus 로고    scopus 로고
    • A functional 4-hydroxysalicylate/hydroxyquinol degradative pathway gene cluster is linked to the initial dibenzo-p-dioxin pathway genes in Sphingomonas sp. strain RW1
    • Armengaud, J., K. N. Timmis, and R.-M. Wittich. 1999. A functional 4-hydroxysalicylate/hydroxyquinol degradative pathway gene cluster is linked to the initial dibenzo-p-dioxin pathway genes in Sphingomonas sp. strain RW1. J. Bacteriol. 181:3452-3461.
    • (1999) J. Bacteriol. , vol.181 , pp. 3452-3461
    • Armengaud, J.1    Timmis, K.N.2    Wittich, R.-M.3
  • 3
    • 16644389032 scopus 로고    scopus 로고
    • Degradation of 4-chlorophenol at low temperature and during extreme temperature fluctuations by Arthrobacter chlorophenolicus A6
    • Backman, A., and J. K. Jansson. 2004. Degradation of 4-chlorophenol at low temperature and during extreme temperature fluctuations by Arthrobacter chlorophenolicus A6. Microb. Ecol. 48:246-253.
    • (2004) Microb. Ecol. , vol.48 , pp. 246-253
    • Backman, A.1    Jansson, J.K.2
  • 4
    • 2442704506 scopus 로고    scopus 로고
    • Impact of temperature on the physiological status of a potential bioremediation inoculant, Arthrobacter chlorophenolicus A6
    • Backman, A., N. Maraha, and J. K. Jansson. 2004. Impact of temperature on the physiological status of a potential bioremediation inoculant, Arthrobacter chlorophenolicus A6. Appl. Environ. Microbiol. 70:2952-2958.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 2952-2958
    • Backman, A.1    Maraha, N.2    Jansson, J.K.3
  • 5
    • 0030589194 scopus 로고    scopus 로고
    • Biodegradation of 4-chlorophenol via a hydroquinone pathway by Arthrobacter ureafaciens CPR706
    • Bae, H. S., J. M. Lee, and S.-T. Lee. 1996. Biodegradation of 4-chlorophenol via a hydroquinone pathway by Arthrobacter ureafaciens CPR706. FEMS Microbiol. Lett. 145:125-129.
    • (1996) FEMS Microbiol. Lett. , vol.145 , pp. 125-129
    • Bae, H.S.1    Lee, J.M.2    Lee, S.-T.3
  • 6
    • 0014386678 scopus 로고
    • The bacterial metabolism of 2,4-xylenol
    • Chapman, P. J., and D. J. Hopper. 1968. The bacterial metabolism of 2,4-xylenol. Biochem. J. 110:491-498.
    • (1968) Biochem. J. , vol.110 , pp. 491-498
    • Chapman, P.J.1    Hopper, D.J.2
  • 7
    • 0034696780 scopus 로고    scopus 로고
    • Plasmid-encoded degradation of p-nitrophenol and 4-nitrocatechol by Arthrobacter protophormiae
    • Chauhan, A., A. K. Chakraborti, and R. K. Jain. 2000. Plasmid-encoded degradation of p-nitrophenol and 4-nitrocatechol by Arthrobacter protophormiae. Biochem. Biophys. Res. Commun. 270:733-740.
    • (2000) Biochem. Biophys. Res. Commun. , vol.270 , pp. 733-740
    • Chauhan, A.1    Chakraborti, A.K.2    Jain, R.K.3
  • 8
    • 0032456306 scopus 로고    scopus 로고
    • Simultaneous degradation of p-nitrophenol and phenol by a newly isolated Nocardioides sp
    • Cho, Y.-G., J.-H. Yoon, Y.-H. Park, and S.-T. Lee. 1998. Simultaneous degradation of p-nitrophenol and phenol by a newly isolated Nocardioides sp. J. Gen. Appl. Microbiol. 44:303-309.
    • (1998) J. Gen. Appl. Microbiol. , vol.44 , pp. 303-309
    • Cho, Y.-G.1    Yoon, J.-H.2    Park, Y.-H.3    Lee, S.-T.4
  • 9
    • 0035202047 scopus 로고    scopus 로고
    • Use of green fluorescent protein and luciferase biomarkers to monitor survival and activity of Arthrobacter chlorophenolicus A6 cells during degradation of 4-chlorophenol in soil
    • Elväng, A. M., K. Westerberg, C. Jernberg, and J. K. Jansson. 2001. Use of green fluorescent protein and luciferase biomarkers to monitor survival and activity of Arthrobacter chlorophenolicus A6 cells during degradation of 4-chlorophenol in soil. Environ. Microbiol. 3:32-42.
    • (2001) Environ. Microbiol. , vol.3 , pp. 32-42
    • Elväng, A.M.1    Westerberg, K.2    Jernberg, C.3    Jansson, J.K.4
  • 10
    • 0034964969 scopus 로고    scopus 로고
    • Isolation and characterization of IS1409, an insertion element of 4-chlorobenzoate-degrading Arthrobacter sp. strain TM1, and development of a system for transposon mutagenesis
    • Gartemann, K.-H., and R. Eichenlaub. 2001. Isolation and characterization of IS1409, an insertion element of 4-chlorobenzoate-degrading Arthrobacter sp. strain TM1, and development of a system for transposon mutagenesis. J. Bacteriol. 183:3729-3736.
    • (2001) J. Bacteriol. , vol.183 , pp. 3729-3736
    • Gartemann, K.-H.1    Eichenlaub, R.2
  • 11
    • 0026805891 scopus 로고
    • Functional and evolutionary relationships among diverse oxygenases
    • Harayama, S., and M. Kok. 1992. Functional and evolutionary relationships among diverse oxygenases. Annu. Rev. Microbiol. 46:565-601.
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 565-601
    • Harayama, S.1    Kok, M.2
  • 12
    • 0036890005 scopus 로고    scopus 로고
    • Impact of 4-chlorophenol contamination and/or inoculation with the 4-chlorophenol-degrading strain, Arthrobacter chlorophenolicus A6L, on soil bacterial community structure
    • Jernberg, C., and J. K. Jansson. 2002. Impact of 4-chlorophenol contamination and/or inoculation with the 4-chlorophenol-degrading strain, Arthrobacter chlorophenolicus A6L, on soil bacterial community structure. FEMS Microbiol. Ecol. 42:387-397.
    • (2002) FEMS Microbiol. Ecol. , vol.42 , pp. 387-397
    • Jernberg, C.1    Jansson, J.K.2
  • 13
    • 0000894177 scopus 로고
    • AL
    • P. H. A. Sneath, N. S. Mair, M. E. Sharpe, and J. G. Holt (ed.), Williams & Wilkins, Baltimore, Md
    • AL, p. 1228-1301. In P. H. A. Sneath, N. S. Mair, M. E. Sharpe, and J. G. Holt (ed.), Bergey's manual of systematic bacteriology, vol. 2. Williams & Wilkins, Baltimore, Md.
    • (1986) Bergey's Manual of Systematic Bacteriology , vol.2 , pp. 1228-1301
    • Keddie, R.M.1    Collins, M.D.2    Jones, D.3
  • 14
    • 3242807396 scopus 로고    scopus 로고
    • A novel p-nitrophenol degradation gene cluster from a gram-positive bacterium, Rhodococcus opacus SAO101
    • Kitagawa, W., N. Kimura, and Y. Kamagata. 2004. A novel p-nitrophenol degradation gene cluster from a gram-positive bacterium, Rhodococcus opacus SAO101. J. Bacteriol. 186:4894-4902.
    • (2004) J. Bacteriol. , vol.186 , pp. 4894-4902
    • Kitagawa, W.1    Kimura, N.2    Kamagata, Y.3
  • 15
    • 0028924379 scopus 로고
    • Nucleotide sequence and expression of kerA, the gene encoding a keratinolytic protease of Bacillus licheniformis PWD-1
    • Lin, X., D. W. Kelemen, E. S. Miller, and J. C. H. Shih. 1995. Nucleotide sequence and expression of kerA, the gene encoding a keratinolytic protease of Bacillus licheniformis PWD-1. Appl. Environ. Microbiol. 61:1469-1474.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1469-1474
    • Lin, X.1    Kelemen, D.W.2    Miller, E.S.3    Shih, J.C.H.4
  • 16
    • 0036279656 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of a 2,4,6-trichlorophenol degradation pathway in Ralstonia eutropha JMP134
    • Louie, T. M., C. M. Webster, and L. Xun. 2002. Genetic and biochemical characterization of a 2,4,6-trichlorophenol degradation pathway in Ralstonia eutropha JMP134. J. Bacteriol. 184:3492-3500.
    • (2002) J. Bacteriol. , vol.184 , pp. 3492-3500
    • Louie, T.M.1    Webster, C.M.2    Xun, L.3
  • 17
    • 0035751609 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of the gene encoding 4-hydroxy-4-methyl-2-oxoglutarate aldolase from Pseudomonas ochraceae NGJ1
    • Maruvama, K., M. Miwa, N. Tsujii, T. Nagai, N. Tomita, T. Harada, H. Sobajima, and H. Sugisaki. 2001. Cloning, sequencing, and expression of the gene encoding 4-hydroxy-4-methyl-2-oxoglutarate aldolase from Pseudomonas ochraceae NGJ1. Biosci. Biotechnol. Biochem. 65:2701-2709.
    • (2001) Biosci. Biotechnol. Biochem. , vol.65 , pp. 2701-2709
    • Maruvama, K.1    Miwa, M.2    Tsujii, N.3    Nagai, T.4    Tomita, N.5    Harada, T.6    Sobajima, H.7    Sugisaki, H.8
  • 18
    • 0031609962 scopus 로고    scopus 로고
    • Detection of firefly luciferase-tagged bacteria in environmental samples
    • Möller, A., and J. K. Jansson. 1998. Detection of firefly luciferase-tagged bacteria in environmental samples. Methods Mol. Biol. 102:269-283.
    • (1998) Methods Mol. Biol. , vol.102 , pp. 269-283
    • Möller, A.1    Jansson, J.K.2
  • 19
    • 0033590643 scopus 로고    scopus 로고
    • Cloning and sequence analysis of two catechol-degrading gene clusters from the aniline-assimilating bacterium Frateuria species ANA-18
    • Murakami, S., A. Takashima, J. Takemoto, S. Takenaka, R. Shinke, and K. Aoki. 1999. Cloning and sequence analysis of two catechol-degrading gene clusters from the aniline-assimilating bacterium Frateuria species ANA-18. Gene 226:189-198.
    • (1999) Gene , vol.226 , pp. 189-198
    • Murakami, S.1    Takashima, A.2    Takemoto, J.3    Takenaka, S.4    Shinke, R.5    Aoki, K.6
  • 20
    • 0033127751 scopus 로고    scopus 로고
    • Cloning of a gene encoding hydroxyquinol 1,2-dioxygenase that catalyzes both intradiol and extradiol ring cleavage of catechol
    • Murakami, S., T. Okuno, E. Matsumura, S. Takenaka, R. Shinke, and K. Aoki. 1999. Cloning of a gene encoding hydroxyquinol 1,2-dioxygenase that catalyzes both intradiol and extradiol ring cleavage of catechol. Biosci. Biotechnol. Biochem. 63:859-865.
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 859-865
    • Murakami, S.1    Okuno, T.2    Matsumura, E.3    Takenaka, S.4    Shinke, R.5    Aoki, K.6
  • 21
    • 0025815712 scopus 로고
    • Sequence of the gene (pheA) encoding phenol monooxygenase from Pseudomonas sp. EST1001: Expression in Escherichia coli and Pseudomonas putida
    • Nurk, A., L. Kasak, and M. Kivisaar. 1991. Sequence of the gene (pheA) encoding phenol monooxygenase from Pseudomonas sp. EST1001: expression in Escherichia coli and Pseudomonas putida. Gene 102:13-18.
    • (1991) Gene , vol.102 , pp. 13-18
    • Nurk, A.1    Kasak, L.2    Kivisaar, M.3
  • 22
    • 0034682335 scopus 로고    scopus 로고
    • Lateral gene transfer and the nature of bacterial innovation
    • Ochman, H., J. G. Lawrence, and E. A. Groisman. 2000. Lateral gene transfer and the nature of bacterial innovation. Nature 405:299-304.
    • (2000) Nature , vol.405 , pp. 299-304
    • Ochman, H.1    Lawrence, J.G.2    Groisman, E.A.3
  • 23
    • 0024296029 scopus 로고
    • Structure and assembly of protocatechuate 3,4-dioxygenase
    • Ohlendorf, D. H., J. D. Lipscomb, and P. C. Weber. 1988. Structure and assembly of protocatechuate 3,4-dioxygenase. Nature 336:403-405.
    • (1988) Nature , vol.336 , pp. 403-405
    • Ohlendorf, D.H.1    Lipscomb, J.D.2    Weber, P.C.3
  • 24
    • 0033843773 scopus 로고    scopus 로고
    • Degradation of 2,4,6-trichlorophenol via chlorohydroxyquinol in Ralstonia eutropha JMP134 and JMP222
    • Padilla, L., V. Malus, P. Zenteno, and B. González. 2000. Degradation of 2,4,6-trichlorophenol via chlorohydroxyquinol in Ralstonia eutropha JMP134 and JMP222. J. Basic Microbiol. 4:243-249.
    • (2000) J. Basic Microbiol. , vol.4 , pp. 243-249
    • Padilla, L.1    Malus, V.2    Zenteno, P.3    González, B.4
  • 25
    • 0030590090 scopus 로고    scopus 로고
    • Plasmid-encoded degradation of p-nitrophenol by Pseudomonas cepacia
    • Prakash, D., A. Chauhan, and R. K. Jain. 1996. Plasmid-encoded degradation of p-nitrophenol by Pseudomonas cepacia. Biochem. Biophys. Res. Commun. 224:375-381.
    • (1996) Biochem. Biophys. Res. Commun. , vol.224 , pp. 375-381
    • Prakash, D.1    Chauhan, A.2    Jain, R.K.3
  • 26
    • 0141593614 scopus 로고    scopus 로고
    • The metabolic pathway of 4-aminophenol in Burkholderia sp. strain AK-5 differs from that of aniline and aniline with C-4 substituents
    • Takenaka, S., S. Okugawa, M. Kadowaki, S. Murakami, and K. Aoki. 2003. The metabolic pathway of 4-aminophenol in Burkholderia sp. strain AK-5 differs from that of aniline and aniline with C-4 substituents. Appl. Environ. Microbiol. 69:5410-5413.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 5410-5413
    • Takenaka, S.1    Okugawa, S.2    Kadowaki, M.3    Murakami, S.4    Aoki, K.5
  • 27
    • 0028793586 scopus 로고
    • A locus of Pseudomonas pickettii DTP0602, had, that encodes 2,4,6-trichlorophenol-4-dechlorinase with hydroxylase activity, and hydroxylation of various chlorophenols by the enzyme
    • Takizawa, N., H. Yokovama, K. Yanagihara, T. Hatta, and H. Kiyohara. 1995. A locus of Pseudomonas pickettii DTP0602, had, that encodes 2,4,6-trichlorophenol-4-dechlorinase with hydroxylase activity, and hydroxylation of various chlorophenols by the enzyme. J. Ferment. Bioeng. 80:318-326.
    • (1995) J. Ferment. Bioeng. , vol.80 , pp. 318-326
    • Takizawa, N.1    Yokovama, H.2    Yanagihara, K.3    Hatta, T.4    Kiyohara, H.5
  • 28
    • 0034519183 scopus 로고    scopus 로고
    • Arthrobacter chlorophenolicus sp. nov., a new species capable of degrading high concentrations of 4-chlorophenol
    • Westerberg, K., A. M. Elväng, E. Stackebrandt, and J. K. Jansson. 2000. Arthrobacter chlorophenolicus sp. nov., a new species capable of degrading high concentrations of 4-chlorophenol. Int. J. Syst. Appl. Microbiol. 50:2083-2092.
    • (2000) Int. J. Syst. Appl. Microbiol. , vol.50 , pp. 2083-2092
    • Westerberg, K.1    Elväng, A.M.2    Stackebrandt, E.3    Jansson, J.K.4
  • 30
    • 0025318864 scopus 로고
    • The 'effective number of codons' used in a gene
    • Wright, F. 1990. The 'effective number of codons' used in a gene. Gene 87:23-29.
    • (1990) Gene , vol.87 , pp. 23-29
    • Wright, F.1
  • 31
    • 1342304117 scopus 로고    scopus 로고
    • A monooxygenase catalyzes sequential dechlorinations of 2,4,6-trichlorophenol by oxidative and hydrolytic reactions
    • Xun, L., and C. M. Webster. 2004. A monooxygenase catalyzes sequential dechlorinations of 2,4,6-trichlorophenol by oxidative and hydrolytic reactions. J. Biol. Chem. 279:6696-6700.
    • (2004) J. Biol. Chem. , vol.279 , pp. 6696-6700
    • Xun, L.1    Webster, C.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.