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Volumn 23, Issue 1, 2005, Pages 88-93

Substrate-induced gene-expression screening of environmental metagenome libraries for isolation of catabolic genes

Author keywords

[No Author keywords available]

Indexed keywords

CLONING; ENZYMES; SCREENING;

EID: 19144369096     PISSN: 10870156     EISSN: 15461696     Source Type: Journal    
DOI: 10.1038/nbt1048     Document Type: Article
Times cited : (327)

References (29)
  • 1
    • 2942576144 scopus 로고    scopus 로고
    • The soil metagenome - A rich resource for the discovery of novel natural products
    • Daniel, R. The soil metagenome-a rich resource for the discovery of novel natural products. Curr. Opin. Biotechnol. 15, 199-204 (2004).
    • (2004) Curr. Opin. Biotechnol. , vol.15 , pp. 199-204
    • Daniel, R.1
  • 2
    • 0032496652 scopus 로고    scopus 로고
    • PCR isolation of catechol 2,3-dioxygenase gene fragments from environmental samples and their assembly into functional genes
    • Okuta, A., Ohnishi, K. & Harayama, S. PCR isolation of catechol 2,3-dioxygenase gene fragments from environmental samples and their assembly into functional genes. Gene 212, 221-228 (1998).
    • (1998) Gene , vol.212 , pp. 221-228
    • Okuta, A.1    Ohnishi, K.2    Harayama, S.3
  • 3
    • 0032863699 scopus 로고    scopus 로고
    • Construction of environmental DNA libraries in Escherichia coli and screening for the presence of genes conferring utilization of 4-hydroxybutyrate
    • Henne, A., Daniel, R., Schmitz, R.A. & Gottschalk, G. Construction of environmental DNA libraries in Escherichia coli and screening for the presence of genes conferring utilization of 4-hydroxybutyrate. Appl. Environ. Microbiol. 65, 3901-3907 (1999).
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 3901-3907
    • Henne, A.1    Daniel, R.2    Schmitz, R.A.3    Gottschalk, G.4
  • 4
    • 0032695056 scopus 로고    scopus 로고
    • Characterization of a high-affinity phenol hydroxylase from Comamonas testosteroni R5 by gene cloning, and expression in Pseudomonas aeruginosa PAO1c
    • Teramoto, M., Futamata, H., Harayama, S. & Watanabe, K. Characterization of a high-affinity phenol hydroxylase from Comamonas testosteroni R5 by gene cloning, and expression in Pseudomonas aeruginosa PAO1c. Mol. Gen. Genet. 262, 552-558 (1999).
    • (1999) Mol. Gen. Genet. , vol.262 , pp. 552-558
    • Teramoto, M.1    Futamata, H.2    Harayama, S.3    Watanabe, K.4
  • 6
    • 0025358148 scopus 로고
    • Molecular characterization of the vir regulon of Agrobacterium tumefaciens: Complete nucleotide sequence and gene organization of the 2863-kbp regulon cloned as a single unit
    • Rogowsky, P.M. et al. Molecular characterization of the vir regulon of Agrobacterium tumefaciens: complete nucleotide sequence and gene organization of the 2863-kbp regulon cloned as a single unit. Plasmid 23, 85-106 (1990).
    • (1990) Plasmid , vol.23 , pp. 85-106
    • Rogowsky, P.M.1
  • 7
    • 0030866940 scopus 로고    scopus 로고
    • Fluorescence-based isolation of bacterial genes expressed within host cells
    • Valdivia, R.H. & Falkow, S. Fluorescence-based isolation of bacterial genes expressed within host cells. Science 277, 2007-2011 (1997).
    • (1997) Science , vol.277 , pp. 2007-2011
    • Valdivia, R.H.1    Falkow, S.2
  • 8
    • 0023691425 scopus 로고
    • Genetic applications of an inverse polymerase chain reaction
    • Ochman, H., Gerber, A.S. & Hartl, D.L. Genetic applications of an inverse polymerase chain reaction. Genetics 120, 621-623 (1988).
    • (1988) Genetics , vol.120 , pp. 621-623
    • Ochman, H.1    Gerber, A.S.2    Hartl, D.L.3
  • 9
    • 0031852106 scopus 로고    scopus 로고
    • Phenol hydroxylase cloned from Ralstonia eutropha strain E2 exhibits novel kinetic properties
    • Hino, S., Watanabe, K. & Takahashi, N. Phenol hydroxylase cloned from Ralstonia eutropha strain E2 exhibits novel kinetic properties. Microbiology 144, 1765-1772 (1998).
    • (1998) Microbiology , vol.144 , pp. 1765-1772
    • Hino, S.1    Watanabe, K.2    Takahashi, N.3
  • 11
    • 0001493114 scopus 로고    scopus 로고
    • Growth phase-dependent transcription of the sigma(54)-dependent Po promoter controlling the Pseudomonas-derned (methyl)phenol dmp operon of pVI150
    • Sze, C.C., Moore, T. & Shingler, V. Growth phase-dependent transcription of the sigma(54)-dependent Po promoter controlling the Pseudomonas-derned (methyl)phenol dmp operon of pVI150. J. Bacteriol. 178, 3727-3735 (1996).
    • (1996) J. Bacteriol. , vol.178 , pp. 3727-3735
    • Sze, C.C.1    Moore, T.2    Shingler, V.3
  • 12
    • 0031691310 scopus 로고    scopus 로고
    • Carbon-source-dependent expression of the PalkB promoter from the Pseudomonas oleovorans alkane degradation pathway
    • Yuste, L., Canosa, I. & Rojo, F. Carbon-source-dependent expression of the PalkB promoter from the Pseudomonas oleovorans alkane degradation pathway. J. Bacteriol. 180, 5218-5226 (1998).
    • (1998) J. Bacteriol. , vol.180 , pp. 5218-5226
    • Yuste, L.1    Canosa, I.2    Rojo, F.3
  • 13
    • 0033759661 scopus 로고    scopus 로고
    • Molecular characterization of bacterial populations in petroleum-contaminated groundwater discharged from underground crude-oil-storage cavities
    • Watanabe, K. et al. Molecular characterization of bacterial populations in petroleum-contaminated groundwater discharged from underground crude-oil-storage cavities. Appl. Environ. Microbiol. 66, 4803-4809 (2000).
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 4803-4809
    • Watanabe, K.1
  • 14
    • 0027282545 scopus 로고
    • Transcriptional control of the Pseudomonas putida TOL plasmid catabolic pathways
    • Marques, S. & Ramos, J.L. Transcriptional control of the Pseudomonas putida TOL plasmid catabolic pathways. Mol. Microbiol. 9, 923-929 (1993).
    • (1993) Mol. Microbiol. , vol.9 , pp. 923-929
    • Marques, S.1    Ramos, J.L.2
  • 15
    • 0026495342 scopus 로고
    • Roles of CatR and cis,cis-muconate in activation of the catBC operon, which is involved in benzoate degradation in Pseudomonas putida
    • Parsek, M.R., Shinabarger, D.L., Rothmel, R.K. & Chakrabarty, A.M. Roles of CatR and cis,cis-muconate in activation of the catBC operon, which is involved in benzoate degradation in Pseudomonas putida. J. Bacteriol. 174, 7798-7806 (1992).
    • (1992) J. Bacteriol. , vol.174 , pp. 7798-7806
    • Parsek, M.R.1    Shinabarger, D.L.2    Rothmel, R.K.3    Chakrabarty, A.M.4
  • 16
    • 0029025536 scopus 로고
    • Characterization of MarR, the repressor of the multiple antibiotic resistance (mar) operon in Eschericia coli
    • Seoane, A.S. & Levy, S.B. Characterization of MarR, the repressor of the multiple antibiotic resistance (mar) operon in Eschericia coli. J. Bacteriol. 177, 3414-3419 (1995).
    • (1995) J. Bacteriol. , vol.177 , pp. 3414-3419
    • Seoane, A.S.1    Levy, S.B.2
  • 17
    • 0033623422 scopus 로고    scopus 로고
    • BenR, a XylS homolog, regulates three different pathways of aromatic acid degradation in Pseudomonas putida
    • Cowles, C.E., Nichols, N.N. & Harwood, C.S. BenR, a XylS homolog, regulates three different pathways of aromatic acid degradation in Pseudomonas putida. J. Bacteriol. 182, 6339-6346 (2000).
    • (2000) J. Bacteriol. , vol.182 , pp. 6339-6346
    • Cowles, C.E.1    Nichols, N.N.2    Harwood, C.S.3
  • 18
    • 0025139202 scopus 로고
    • Nucleotide sequencing and characterization of Pseudomonas putida catR: A positive regulator of the catBC operon is a member of the LysR family
    • Rothmel, R.K. et al. Nucleotide sequencing and characterization of Pseudomonas putida catR: a positive regulator of the catBC operon is a member of the LysR family. J. Bacteriol. 172, 922-931 (1990).
    • (1990) J. Bacteriol. , vol.172 , pp. 922-931
    • Rothmel, R.K.1
  • 19
    • 0032738032 scopus 로고    scopus 로고
    • Cloning and sequence analysis of two Pseudomonas flavoprotein xenobiotic reductases
    • Blehert, D.S., Fox, B.C. & Chambliss, G.H. Cloning and sequence analysis of two Pseudomonas flavoprotein xenobiotic reductases. J. Bacteriol. 181, 6254-6263 (1999).
    • (1999) J. Bacteriol. , vol.181 , pp. 6254-6263
    • Blehert, D.S.1    Fox, B.C.2    Chambliss, G.H.3
  • 20
    • 0014939377 scopus 로고
    • Tyrosine phenol lyase I. Purification, crystallization, and properties
    • Kumagai, H., Yamada, H., Matsui, H., Ohkishi, H. & Ogata, K. Tyrosine phenol lyase I. Purification, crystallization, and properties. J. Biol. Chem. 245, 1767-1772 (1970).
    • (1970) J. Biol. Chem. , vol.245 , pp. 1767-1772
    • Kumagai, H.1    Yamada, H.2    Matsui, H.3    Ohkishi, H.4    Ogata, K.5
  • 21
    • 0033820931 scopus 로고    scopus 로고
    • Identification of Escherichia coli ubiB, a gene required for the first monooxygenase step in ubiquinone biosynthesis
    • Poon, W.W. et al. Identification of Escherichia coli ubiB, a gene required for the first monooxygenase step in ubiquinone biosynthesis. J. Bacteriol. 182, 5139-5146 (2000).
    • (2000) J. Bacteriol. , vol.182 , pp. 5139-5146
    • Poon, W.W.1
  • 22
    • 0242500968 scopus 로고    scopus 로고
    • Informatics for unveiling hidden genome signatures
    • Abe, T. et al. Informatics for unveiling hidden genome signatures. Genome Res. 13, 693-702 (2003).
    • (2003) Genome Res. , vol.13 , pp. 693-702
    • Abe, T.1
  • 23
    • 0348103717 scopus 로고    scopus 로고
    • Complete genome sequence of the metabolically versatile photo-synthetic bacterium Rhodopseudomonas palustris
    • Larimer, F.W. et al. Complete genome sequence of the metabolically versatile photo-synthetic bacterium Rhodopseudomonas palustris. Nat. Biotechnol. 22, 55-61 (2004).
    • (2004) Nat. Biotechnol. , vol.22 , pp. 55-61
    • Larimer, F.W.1
  • 24
    • 0026611048 scopus 로고
    • Cytochrome P-450terp. Isolation and purification of the protein and cloning and sequencing of its operon
    • Peterson, J. et al. Cytochrome P-450terp. Isolation and purification of the protein and cloning and sequencing of its operon. J. Biol. Chem. 267, 14193-14203 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 14193-14203
    • Peterson, J.1
  • 25
    • 2142664219 scopus 로고
    • (eds. Falk, J.E., Lemberg, R., & Morton, R.K.) (Pergamon Press Ltd, Oxford)
    • George, P., Bettlestene, J. & Griffith, J.S. in Haematin Enzymes, vol. 1 (eds. Falk, J.E., Lemberg, R., & Morton, R.K.) 105-141 (Pergamon Press Ltd, Oxford 1961).
    • (1961) Haematin Enzymes , vol.1 , pp. 105-141
    • George, P.1    Bettlestene, J.2    Griffith, J.S.3
  • 26
    • 0025257597 scopus 로고
    • Putidaredoxin reductase and putidaredoxin
    • Peterson, J.A., Lorence, M.C. & Amarneh, B. Putidaredoxin reductase and putidaredoxin. J. Biol. Chem. 265, 6066-6073 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 6066-6073
    • Peterson, J.A.1    Lorence, M.C.2    Amarneh, B.3
  • 28
    • 0033597834 scopus 로고    scopus 로고
    • On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES
    • Sakikawa, C., Taguchi, H., Makino, Y. & Yoshida, M. On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES. J. Biol. Chem. 274, 21251-21256 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 21251-21256
    • Sakikawa, C.1    Taguchi, H.2    Makino, Y.3    Yoshida, M.4
  • 29
    • 0037337346 scopus 로고    scopus 로고
    • Isolation and characterization of thermophilic Bacilli degrading cinnamic, 4-coumaric, and ferulic acids
    • Peng, X., Misawa, N. & Harayama, S. Isolation and characterization of thermophilic Bacilli degrading cinnamic, 4-coumaric, and ferulic acids. Appl. Environ. Microbiol. 69, 1417-1427 (2003).
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 1417-1427
    • Peng, X.1    Misawa, N.2    Harayama, S.3


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