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Volumn 71, Issue 2, 2005, Pages 1025-1034

Transcriptional organization of genes for protocatechuate and quinate degradation from Acinetobacter sp. strain ADP1

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC COMPOUNDS; CATALYST ACTIVITY; CHROMOSOMES; DATA REDUCTION; DEGRADATION; ENCODING (SYMBOLS); ENZYMES; STRAIN; SUBSTRATES;

EID: 13544251411     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.71.2.1025-1034.2005     Document Type: Article
Times cited : (24)

References (41)
  • 2
    • 0026579902 scopus 로고
    • Genetic analysis of supraoperonic clustering by use of natural transformation in Acinetobacter calcoaceticus
    • Averhoff, B., L. Gregg-Jolly, D. Elsemore, and L. N. Ornston. 1992. Genetic analysis of supraoperonic clustering by use of natural transformation in Acinetobacter calcoaceticus. J. Bacteriol. 174:200-204.
    • (1992) J. Bacteriol. , vol.174 , pp. 200-204
    • Averhoff, B.1    Gregg-Jolly, L.2    Elsemore, D.3    Ornston, L.N.4
  • 3
    • 1342325448 scopus 로고    scopus 로고
    • Transcriptional organization and regulation of the L-idonic acid pathway (GntII system) in Escherichia coli
    • Bausch, C., M. Ramsey, and T. Conway. 2004. Transcriptional organization and regulation of the L-idonic acid pathway (GntII system) in Escherichia coli. J. Bacteriol. 186:1388-1397.
    • (2004) J. Bacteriol. , vol.186 , pp. 1388-1397
    • Bausch, C.1    Ramsey, M.2    Conway, T.3
  • 4
    • 0029125099 scopus 로고
    • New gentamicin-resistance and lacZ promoter-probe cassettes suitable for insertion mutagenesis and generation of transcriptional fusions
    • Becker, A., M. Schmidt, W. Jäger, and A. Pühler. 1995. New gentamicin-resistance and lacZ promoter-probe cassettes suitable for insertion mutagenesis and generation of transcriptional fusions. Gene 162:37-39.
    • (1995) Gene , vol.162 , pp. 37-39
    • Becker, A.1    Schmidt, M.2    Jäger, W.3    Pühler, A.4
  • 5
    • 0014241496 scopus 로고
    • Regulation of the enzymes of the β-ketoadipate pathway in Moraxella calcoacetica. 3. Effects of 3-hydroxy-4-methylbenzoate on the synthesis of enzymes of the protocatechuate branch
    • Cánovas, J. L., B. F. Johnson, and M. L. Wheelis. 1968. Regulation of the enzymes of the β-ketoadipate pathway in Moraxella calcoacetica. 3. Effects of 3-hydroxy-4-methylbenzoate on the synthesis of enzymes of the protocatechuate branch. Eur. J. Biochem. 3:305-311.
    • (1968) Eur. J. Biochem. , vol.3 , pp. 305-311
    • Cánovas, J.L.1    Johnson, B.F.2    Wheelis, M.L.3
  • 6
    • 0014242368 scopus 로고
    • Regulation of the enzymes of the β-ketoadipate pathway in Moraxella calcoacetica. 2. The role of protocatechuate as inducer
    • Canovas, J. L., M. L. Wheelis, and R. Y. Stanier. 1968. Regulation of the enzymes of the β-ketoadipate pathway in Moraxella calcoacetica. 2. The role of protocatechuate as inducer. Eur. J. Biochem. 3:293-304.
    • (1968) Eur. J. Biochem. , vol.3 , pp. 293-304
    • Canovas, J.L.1    Wheelis, M.L.2    Stanier, R.Y.3
  • 7
    • 0035988320 scopus 로고    scopus 로고
    • Multiple operons connected with catabolism of aromatic compounds in Acinetobacter sp. strain ADP1 are under carbon catabolite repression
    • Dal, S., I. Steiner, and U. Gerischer. 2002. Multiple operons connected with catabolism of aromatic compounds in Acinetobacter sp. strain ADP1 are under carbon catabolite repression. J. Mol. Microbiol. Biotechnol. 4:389-404.
    • (2002) J. Mol. Microbiol. Biotechnol. , vol.4 , pp. 389-404
    • Dal, S.1    Steiner, I.2    Gerischer, U.3
  • 8
    • 0033000387 scopus 로고    scopus 로고
    • The physiological contribution of Acinetobacter PcaK, a transport system that acts upon protocatechuate, can be masked by the overlapping specificity of VanK
    • D'Argenio, D. A., A. Segura, W. M. Coco, P. V. Bünz, and L. N. Ornston. 1999. The physiological contribution of Acinetobacter PcaK, a transport system that acts upon protocatechuate, can be masked by the overlapping specificity of VanK. J. Bacteriol. 181:3505-3515.
    • (1999) J. Bacteriol. , vol.181 , pp. 3505-3515
    • D'Argenio, D.A.1    Segura, A.2    Coco, W.M.3    Bünz, P.V.4    Ornston, L.N.5
  • 9
    • 0024288393 scopus 로고
    • Cytochrome b-562 from Acinetobacter calcoaceticus L.M.D. 79.41. Its characteristics and role as electron acceptor for quinoprotein glucose dehydrogenase
    • Dokter, P., J. E. van Wielink, M. A. van Kleef, and J. A. Duine. 1988. Cytochrome b-562 from Acinetobacter calcoaceticus L.M.D. 79.41. Its characteristics and role as electron acceptor for quinoprotein glucose dehydrogenase. Biochem. J. 254:131-138.
    • (1988) Biochem. J. , vol.254 , pp. 131-138
    • Dokter, P.1    Van Wielink, J.E.2    Van Kleef, M.A.3    Duine, J.A.4
  • 10
    • 0028125023 scopus 로고
    • The pca-pob supraoperonic cluster of Acinetobacter calcoaceticus contains quiA, the structural gene for quinateshikimate dehydrogenase
    • Elsemore, D. A., and L. N. Ornston. 1994. The pca-pob supraoperonic cluster of Acinetobacter calcoaceticus contains quiA, the structural gene for quinateshikimate dehydrogenase. J. Bacteriol. 176:7659-7666.
    • (1994) J. Bacteriol. , vol.176 , pp. 7659-7666
    • Elsemore, D.A.1    Ornston, L.N.2
  • 11
    • 0028820070 scopus 로고
    • Unusual ancestry of dehydratases associated with quinate catabolism in Acinetobacter calcoaceticus
    • Elsemore, D. A., and L. N. Ornston. 1995. Unusual ancestry of dehydratases associated with quinate catabolism in Acinetobacter calcoaceticus. J. Bacteriol. 177:5971-5978.
    • (1995) J. Bacteriol. , vol.177 , pp. 5971-5978
    • Elsemore, D.A.1    Ornston, L.N.2
  • 12
    • 0036190750 scopus 로고    scopus 로고
    • Specific and global regulation of genes associated with the degradation of aromatic compounds in bacteria
    • Gerischer, U. 2002. Specific and global regulation of genes associated with the degradation of aromatic compounds in bacteria. J. Mol. Microbiol. Biotechnol. 4:111-121.
    • (2002) J. Mol. Microbiol. Biotechnol. , vol.4 , pp. 111-121
    • Gerischer, U.1
  • 13
    • 0026531061 scopus 로고
    • mRNA analysis of the adc gene region of Clostridium acetobutylicum during the shift to solventogenesis
    • Gerischer, U., and P. Dürre. 1992. mRNA analysis of the adc gene region of Clostridium acetobutylicum during the shift to solventogenesis. J. Bacteriol. 174:426-433.
    • (1992) J. Bacteriol. , vol.174 , pp. 426-433
    • Gerischer, U.1    Dürre, P.2
  • 14
    • 0028915920 scopus 로고
    • Spontaneous mutations in pcaH and -G, structural genes for protocatechuate 3,4-dioxygenase in Acinetobacter calcoaceticus
    • Gerischer, U., and L. N. Ornston. 1995. Spontaneous mutations in pcaH and -G, structural genes for protocatechuate 3,4-dioxygenase in Acinetobacter calcoaceticus. J. Bacteriol. 177:1336-1347.
    • (1995) J. Bacteriol. , vol.177 , pp. 1336-1347
    • Gerischer, U.1    Ornston, L.N.2
  • 15
    • 0031938056 scopus 로고    scopus 로고
    • PcaU, a transcriptional activator of genes for protocatechuate utilization in Acinetobacter
    • Gerischer, U., A. Segura, and L. N. Ornston. 1998. PcaU, a transcriptional activator of genes for protocatechuate utilization in Acinetobacter. J. Bacteriol. 180:1512-1524.
    • (1998) J. Bacteriol. , vol.180 , pp. 1512-1524
    • Gerischer, U.1    Segura, A.2    Ornston, L.N.3
  • 16
    • 0028245132 scopus 로고
    • Properties of Acinetobacter calcoaceticus recA and its contribution to intracellular gene conversion
    • Gregg-Jolly, L. A., and L. N. Ornston. 1994. Properties of Acinetobacter calcoaceticus recA and its contribution to intracellular gene conversion. Mol. Microbiol. 12:985-992.
    • (1994) Mol. Microbiol. , vol.12 , pp. 985-992
    • Gregg-Jolly, L.A.1    Ornston, L.N.2
  • 17
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. 1983. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166:557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 18
    • 0025056536 scopus 로고
    • DNA sequences of genes encoding Acinetobacter calcoaceticus protocatechuate 3,4-dioxygenase: Evidence indicating shuffling of genes and of DNA sequences within genes during their evolutionary divergence
    • Hartnett, C., E. L. Neidle, K.-L. Ngai, and L. N. Ornston. 1990. DNA sequences of genes encoding Acinetobacter calcoaceticus protocatechuate 3,4-dioxygenase: evidence indicating shuffling of genes and of DNA sequences within genes during their evolutionary divergence. J. Bacteriol. 172:956-966.
    • (1990) J. Bacteriol. , vol.172 , pp. 956-966
    • Hartnett, C.1    Neidle, E.L.2    Ngai, K.-L.3    Ornston, L.N.4
  • 19
    • 13544274862 scopus 로고
    • Ph.D. thesis. Yale University, New Haven, Conn.
    • Hartnett, G. B. 1993. Ph.D. thesis. Yale University, New Haven, Conn.
    • (1993)
    • Hartnett, G.B.1
  • 20
    • 0029795374 scopus 로고    scopus 로고
    • The β-ketoadipate pathway and the biology of self-identity
    • Harwood, C. S., and R. E. Parales. 1996. The β-ketoadipate pathway and the biology of self-identity. Annu. Rev. Microbiol. 50:553-590.
    • (1996) Annu. Rev. Microbiol. , vol.50 , pp. 553-590
    • Harwood, C.S.1    Parales, R.E.2
  • 21
    • 0027787581 scopus 로고
    • The pre-chorismate (shikimate) and quinate pathways in filamentous fungi: Theoretical and practical aspects
    • Hawkins, A. R., H. K. Lamb, J. D. Moore, I. G. Charles, and C. F. Roberts. 1993. The pre-chorismate (shikimate) and quinate pathways in filamentous fungi: theoretical and practical aspects. J. Gen. Microbiol. 139:2891-2899.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 2891-2899
    • Hawkins, A.R.1    Lamb, H.K.2    Moore, J.D.3    Charles, I.G.4    Roberts, C.F.5
  • 22
    • 0014503154 scopus 로고
    • Transformation of Acinetobacter calco-aceticus (Bacterium anitratum)
    • Juni, E., and A. Janik. 1969. Transformation of Acinetobacter calco-aceticus (Bacterium anitratum). J. Bacteriol. 98:281-288.
    • (1969) J. Bacteriol. , vol.98 , pp. 281-288
    • Juni, E.1    Janik, A.2
  • 23
    • 0023715368 scopus 로고
    • Improved broad-host-range plasmids for DNA cloning in gram-negative bacteria
    • Keen, N. T., S. Tamaki, D. Kobayashi, and D. Trollinger. 1988. Improved broad-host-range plasmids for DNA cloning in gram-negative bacteria. Gene 70:191-197.
    • (1988) Gene , vol.70 , pp. 191-197
    • Keen, N.T.1    Tamaki, S.2    Kobayashi, D.3    Trollinger, D.4
  • 24
    • 0024787144 scopus 로고
    • Construction of a lacZ-kanamycin-resistance cassette, useful for site-directed mutagenesis and as a promoter probe
    • Kokotek, W., and W. Lotz. 1989. Construction of a lacZ-kanamycin- resistance cassette, useful for site-directed mutagenesis and as a promoter probe. Gene 84:467-471.
    • (1989) Gene , vol.84 , pp. 467-471
    • Kokotek, W.1    Lotz, W.2
  • 25
    • 0028040511 scopus 로고
    • Contrasting patterns of evolutionary divergence within the Acinetobacter calcoaceticus pca operon
    • Kowalchuk, G. A., G. B. Hartnett, A. Benson, J. E. Houghton, K.-L. Ngai, and L. N. Ornston. 1994. Contrasting patterns of evolutionary divergence within the Acinetobacter calcoaceticus pca operon. Gene 146:23-30.
    • (1994) Gene , vol.146 , pp. 23-30
    • Kowalchuk, G.A.1    Hartnett, G.B.2    Benson, A.3    Houghton, J.E.4    Ngai, K.-L.5    Ornston, L.N.6
  • 26
    • 0026507940 scopus 로고
    • Differential flux through the quinate and shikimate pathways. Implications for the channelling hypothesis
    • Lamb, H. K., J. P. van den Hombergh, G. H. Newton, J. D. Moore, C. F. Roberts, and A. R. Hawkins. 1992. Differential flux through the quinate and shikimate pathways. Implications for the channelling hypothesis. Biochem. J. 284:181-187.
    • (1992) Biochem. J. , vol.284 , pp. 181-187
    • Lamb, H.K.1    Van Den Hombergh, J.P.2    Newton, G.H.3    Moore, J.D.4    Roberts, C.F.5    Hawkins, A.R.6
  • 27
    • 0003842951 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Miller, J. H. 1992. A short course in bacterial genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1992) A Short Course in Bacterial Genetics
    • Miller, J.H.1
  • 28
    • 0030818839 scopus 로고    scopus 로고
    • PcaK, a high-affinity permease for the aromatic compounds 4-hydroxybenzoate and protocatechuate from Pseudomonas putida
    • Nichols, N. N., and C. S. Harwood. 1997. PcaK, a high-affinity permease for the aromatic compounds 4-hydroxybenzoate and protocatechuate from Pseudomonas putida. J. Bacteriol. 179:5056-5061.
    • (1997) J. Bacteriol. , vol.179 , pp. 5056-5061
    • Nichols, N.N.1    Harwood, C.S.2
  • 29
    • 0024284571 scopus 로고
    • Defining the consensus sequences of E. coli promoter elements by random selection
    • Oliphant, A. R., and K. Struhl. 1988. Defining the consensus sequences of E. coli promoter elements by random selection. Nucleic Acids Res. 16:7673-7683.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 7673-7683
    • Oliphant, A.R.1    Struhl, K.2
  • 30
    • 0141482111 scopus 로고    scopus 로고
    • Hydroxycinnamate (hca) catabolic genes from Acinetobacter sp. strain ADP1 are repressed by HcaR and are induced by hydroxycinnamoyl-coenzyme A thioesters
    • Parke, D., and L. N. Ornston. 2003. Hydroxycinnamate (hca) catabolic genes from Acinetobacter sp. strain ADP1 are repressed by HcaR and are induced by hydroxycinnamoyl-coenzyme A thioesters. Appl. Environ. Microbiol. 69:5398-5409.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 5398-5409
    • Parke, D.1    Ornston, L.N.2
  • 31
    • 0036203062 scopus 로고    scopus 로고
    • Differential DNA binding of transcriptional regulator PcaU from Acinetobacter sp. strain ADP1
    • Popp, R., T. Kohl, P. Patz, G. Trautwein, and U. Gerischer. 2002. Differential DNA binding of transcriptional regulator PcaU from Acinetobacter sp. strain ADP1. J. Bacteriol. 184:1988-1997.
    • (2002) J. Bacteriol. , vol.184 , pp. 1988-1997
    • Popp, R.1    Kohl, T.2    Patz, P.3    Trautwein, G.4    Gerischer, U.5
  • 32
    • 0032939521 scopus 로고    scopus 로고
    • mRNA degradation in bacteria
    • Rauhut, R., and G. Klug. 1999. mRNA degradation in bacteria. FEMS Microbiol. Rev. 23:353-370.
    • (1999) FEMS Microbiol. Rev. , vol.23 , pp. 353-370
    • Rauhut, R.1    Klug, G.2
  • 33
    • 0022559895 scopus 로고
    • Plasmid vectors for the genetic analysis and manipulation of Rhizobia and other gram-negative bacteria
    • Simon, R., M. O'Connell, M. Labes, and A. Pühler. 1986. Plasmid vectors for the genetic analysis and manipulation of Rhizobia and other gram-negative bacteria. Methods Enzymol. 118:640-659.
    • (1986) Methods Enzymol. , vol.118 , pp. 640-659
    • Simon, R.1    O'Connell, M.2    Labes, M.3    Pühler, A.4
  • 34
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in gram negative bacteria
    • Simon, R., M. O'Connell, M. Labes, and A. Pühler. 1983. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in gram negative bacteria. Bio/Technology 1983:784-791.
    • (1983) Bio/Technology , vol.1983 , pp. 784-791
    • Simon, R.1    O'Connell, M.2    Labes, M.3    Pühler, A.4
  • 35
    • 0037229359 scopus 로고    scopus 로고
    • Genes for chlorogenate and hydroxycinnamate catabolism (hca) are linked to functionally related genes in the dca-pca-qui-pob-hca chromosomal cluster of Acinetobacter sp. strain ADP1
    • Smith, M. A., V. B. Weaver, D. M. Young, and L. N. Ornston. 2003. Genes for chlorogenate and hydroxycinnamate catabolism (hca) are linked to functionally related genes in the dca-pca-qui-pob-hca chromosomal cluster of Acinetobacter sp. strain ADP1. Appl. Environ. Microbiol. 69:524-532.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 524-532
    • Smith, M.A.1    Weaver, V.B.2    Young, D.M.3    Ornston, L.N.4
  • 37
    • 0035153271 scopus 로고    scopus 로고
    • Effects exerted by transcriptional regulator PcaU from Acinetobacter sp. strain ADP1
    • Trautwein, G., and U. Gerischer. 2001. Effects exerted by transcriptional regulator PcaU from Acinetobacter sp. strain ADP1. J. Bacteriol. 183:873-881.
    • (2001) J. Bacteriol. , vol.183 , pp. 873-881
    • Trautwein, G.1    Gerischer, U.2
  • 39
    • 0014813719 scopus 로고
    • Regulation of the enzymes of the β-ketoadipate pathway in Moraxella. Control of quinate oxidation by protocatechuate
    • Tresguerres, M. E. F., G. De Torrontegui, W. M. Ingledew, and J. L. Cánovas. 1970. Regulation of the enzymes of the β-ketoadipate pathway in Moraxella. Control of quinate oxidation by protocatechuate. Eur. J. Biochem. 14:445-450.
    • (1970) Eur. J. Biochem. , vol.14 , pp. 445-450
    • Tresguerres, M.E.F.1    De Torrontegui, G.2    Ingledew, W.M.3    Cánovas, J.L.4
  • 40
    • 0006485946 scopus 로고
    • Potential competition for 5-dehydroshikimate between the aromatic biosynthetic route and the catabolic hydroaromatic pathway
    • Tresguerres, M. E. F., W. M. Ingledew, and J. L. Cánovas. 1972. Potential competition for 5-dehydroshikimate between the aromatic biosynthetic route and the catabolic hydroaromatic pathway. Arch. Mikrobiol. 82:111-119.
    • (1972) Arch. Mikrobiol. , vol.82 , pp. 111-119
    • Tresguerres, M.E.F.1    Ingledew, W.M.2    Cánovas, J.L.3
  • 41
    • 0024005577 scopus 로고
    • Bacterial NAD(P)-independent quinate dehydrogenase is a quinoprotein
    • van Kleef, M. A., and J. A. Duine. 1988. Bacterial NAD(P)-independent quinate dehydrogenase is a quinoprotein. Arch. Microbiol. 150:32-36.
    • (1988) Arch. Microbiol. , vol.150 , pp. 32-36
    • Van Kleef, M.A.1    Duine, J.A.2


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