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Volumn 182, Issue 1, 2000, Pages 100-106

HbaR, a 4-hydroxybenzoate sensor and FNR-CRP superfamily member, regulates anaerobic 4-hydroxybenzoate degradation by Rhodopseudomonas palustris

Author keywords

[No Author keywords available]

Indexed keywords

4 HYDROXYBENZOIC ACID; AMINO ACID; AMPICILLIN; BETA GALACTOSIDASE; CHLORAMPHENICOL; COENZYME A; GENTAMICIN; KANAMYCIN; NITRATE; OXYGEN; REGULATOR PROTEIN; SPECTINOMYCIN; SUCCINIC ACID;

EID: 0033987161     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.182.1.100-106.2000     Document Type: Article
Times cited : (38)

References (40)
  • 1
    • 0029146375 scopus 로고
    • Expression of the nir and nor genes for denitrification of Pseudomonas aeruginosa requires a novel CRP/FNR-related transcriptional regulator, DNR, in addition to ANR
    • Arai, H., Y. Igarashi, and T. Kodama. 1995. Expression of the nir and nor genes for denitrification of Pseudomonas aeruginosa requires a novel CRP/FNR-related transcriptional regulator, DNR, in addition to ANR. FEBS Lett. 371:73-76.
    • (1995) FEBS Lett. , vol.371 , pp. 73-76
    • Arai, H.1    Igarashi, Y.2    Kodama, T.3
  • 2
    • 0030885697 scopus 로고    scopus 로고
    • Cascade regulation of the two CRP/FNR-related transcriptional regulators (ANR and DNR) and the denitritication enzymes in Pseudomonas aeruginosa
    • Arai, H., T. Kodama, and Y. Igarashi. 1997. Cascade regulation of the two CRP/FNR-related transcriptional regulators (ANR and DNR) and the denitritication enzymes in Pseudomonas aeruginosa. Mol. Microbiol. 25:1141-1148.
    • (1997) Mol. Microbiol. , vol.25 , pp. 1141-1148
    • Arai, H.1    Kodama, T.2    Igarashi, Y.3
  • 4
    • 0027477049 scopus 로고
    • Enzymes of anaerobic metabolism of phenolic compounds: 4-hydroxybenzoate-CoA ligase from a denitrifying pseudomonas species
    • Biegert, T., U. Altenschmidt, C. Eckerskorn, and G. Fuchs. 1993, Enzymes of anaerobic metabolism of phenolic compounds: 4-hydroxybenzoate-CoA ligase from a denitrifying Pseudomonas species. Eur. J. Biochem. 213:555-561.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 555-561
    • Biegert, T.1    Altenschmidt, U.2    Eckerskorn, C.3    Fuchs, G.4
  • 5
    • 0032006814 scopus 로고    scopus 로고
    • 4-Hydroxybenzoyl-CoA reductase (dehydroxylating) from the denitrifying bacterium Thauera aromatica. Prosthetic groups, electron donor, and genes of a member of the molybdenum-flavin-iron-sulfur proteins
    • Breese, K., and G. Fuchs. 1998. 4-Hydroxybenzoyl-CoA reductase (dehydroxylating) from the denitrifying bacterium Thauera aromatica. Prosthetic groups, electron donor, and genes of a member of the molybdenum-flavin-iron-sulfur proteins. Eur. J. Biochem. 251:916-923.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 916-923
    • Breese, K.1    Fuchs, G.2
  • 6
    • 0026056114 scopus 로고
    • Anaerobically expressed Escherichia coli genes identified by operon fusion techniques
    • Choe, M., and W. S. Reznikoff. 1991. Anaerobically expressed Escherichia coli genes identified by operon fusion techniques. J. Bacteriol. 173:6139-6146.
    • (1991) J. Bacteriol. , vol.173 , pp. 6139-6146
    • Choe, M.1    Reznikoff, W.S.2
  • 8
    • 0027385020 scopus 로고
    • Early and late responses of TOL promoters to pathway inducers: Identification of postexponential promoters in Pseudomonas putida with lacZ-tet bicistronic reporters
    • De Lorenzo, V., I. Cases, M. Herrero, and K. N. Timmis. 1993. Early and late responses of TOL promoters to pathway inducers: identification of postexponential promoters in Pseudomonas putida with lacZ-tet bicistronic reporters. J. Bacteriol. 175:6902-6907.
    • (1993) J. Bacteriol. , vol.175 , pp. 6902-6907
    • De Lorenzo, V.1    Cases, I.2    Herrero, M.3    Timmis, K.N.4
  • 9
    • 0026664931 scopus 로고
    • Anaerobic growth of Rhodopseudomonas palustris on 4-hydroxybenzoate is dependent on AadR, a member of the cyclic AMP receptor protein family of transcriptional regulators
    • Dispensa, M., C. T. Thomas, M.-K. Kim, J. A. Perrotta, J. Gibson, and C. S. Harwood. 1992. Anaerobic growth of Rhodopseudomonas palustris on 4-hydroxybenzoate is dependent on AadR, a member of the cyclic AMP receptor protein family of transcriptional regulators. J. Bacteriol. 174:5803-5813.
    • (1992) J. Bacteriol. , vol.174 , pp. 5803-5813
    • Dispensa, M.1    Thomas, C.T.2    Kim, M.-K.3    Perrotta, J.A.4    Gibson, J.5    Harwood, C.S.6
  • 10
    • 0028787585 scopus 로고
    • Benzoate-coenzyme A ligase, encoded by badA, is one of three ligases able to catalyze benzoyl-coenzyme A formation during anaerobic growth of Rhodopseudomonas palustris on benzoate
    • Egland, P. G., J. Gibson, and C. S. Harwood. 1995. Benzoate-coenzyme A ligase, encoded by badA, is one of three ligases able to catalyze benzoyl-coenzyme A formation during anaerobic growth of Rhodopseudomonas palustris on benzoate. J. Bacteriol. 177:6545-6551.
    • (1995) J. Bacteriol. , vol.177 , pp. 6545-6551
    • Egland, P.G.1    Gibson, J.2    Harwood, C.S.3
  • 11
    • 0344457383 scopus 로고    scopus 로고
    • BadR, a new MarR family member, regulates anaerobic benzoate degradation by Rhodopseudomonas palustris in concert with AadR, an Fnr family member
    • Egland, P. G., and C. S. Harwood. 1999. BadR, a new MarR family member, regulates anaerobic benzoate degradation by Rhodopseudomonas palustris in concert with AadR, an Fnr family member. J. Bacteriol. 181:2102-2109.
    • (1999) J. Bacteriol. , vol.181 , pp. 2102-2109
    • Egland, P.G.1    Harwood, C.S.2
  • 13
    • 0028108941 scopus 로고
    • Genetic regulation of nitrogen fixation in rhizobia
    • Fischer, H.-M. 1994. Genetic regulation of nitrogen fixation in rhizobia. Microbiol. Rev. 58:352-386.
    • (1994) Microbiol. Rev. , vol.58 , pp. 352-386
    • Fischer, H.-M.1
  • 14
    • 0028352589 scopus 로고
    • A luxR-luxI type regulatory system activates Agrobacterium Ti plasmid conjugal transfer in the presence of a plant tumor metabolite
    • Fuqua, C. W., and S. C. Winans. 1994. A luxR-luxI type regulatory system activates Agrobacterium Ti plasmid conjugal transfer in the presence of a plant tumor metabolite. J. Bacteriol. 176:2796-2806.
    • (1994) J. Bacteriol. , vol.176 , pp. 2796-2806
    • Fuqua, C.W.1    Winans, S.C.2
  • 15
    • 0010371726 scopus 로고
    • Gel retardation analysis of nucleic acis-protein interactions
    • D. Rickwood and B. D. Hames (ed.), IRL Press, New York, N.Y.
    • Garner, M. M., and A. Revzin. 1990. Gel retardation analysis of nucleic acis-protein interactions, p. 201-223. In D. Rickwood and B. D. Hames (ed.), Gel electrophoresis of nucleic acids. A practical approach, 2nd ed, IRL Press, New York, N.Y.
    • (1990) Gel Electrophoresis of Nucleic Acids. A Practical Approach, 2nd Ed , pp. 201-223
    • Garner, M.M.1    Revzin, A.2
  • 16
    • 0027955354 scopus 로고
    • 4-Hydroxybenzoate-coenzyme A ligase from Rhodopseudomonas palustris: Purification, gene sequence, and role in anaerobic degradation
    • Gibson, J., M. Dispensa, G. C. Fogg, D. T. Evans, and C. S. Harwood. 1994. 4-Hydroxybenzoate-coenzyme A ligase from Rhodopseudomonas palustris: purification, gene sequence, and role in anaerobic degradation. J. Bacteriol. 176:634-641.
    • (1994) J. Bacteriol. , vol.176 , pp. 634-641
    • Gibson, J.1    Dispensa, M.2    Fogg, G.C.3    Evans, D.T.4    Harwood, C.S.5
  • 17
    • 0031033229 scopus 로고    scopus 로고
    • 4-hydroxybenzoyl coenzyme A reductase (dehydroxylating) is required for anaerobic degradation of 4-hydroxybenzoate by Rhodopseudomonas palustris and shares features with molybdenum-containing hydroxylases
    • Gibson, J., M. Dispensa, and C. S. Harwood. 1997, 4-Hydroxybenzoyl coenzyme A reductase (dehydroxylating) is required for anaerobic degradation of 4-hydroxybenzoate by Rhodopseudomonas palustris and shares features with molybdenum-containing hydroxylases. J. Bacteriol. 179:634-642.
    • (1997) J. Bacteriol. , vol.179 , pp. 634-642
    • Gibson, J.1    Dispensa, M.2    Harwood, C.S.3
  • 18
    • 0032466209 scopus 로고    scopus 로고
    • Anaerobic metabolism of aromatic compounds via the henzoyl-CoA pathway
    • Harwood, C. S., G. Burchhardt, H. Herrmann, and G. Fuchs. 1999. Anaerobic metabolism of aromatic compounds via the henzoyl-CoA pathway. FEMS Microbiol. Rev. 22:439-458.
    • (1999) FEMS Microbiol. Rev. , vol.22 , pp. 439-458
    • Harwood, C.S.1    Burchhardt, G.2    Herrmann, H.3    Fuchs, G.4
  • 19
    • 0023971827 scopus 로고
    • Anaerobic and aerobic metabolism of diverse aromatic compounds by the photosynthetic bacterium Rhodopseudomonas palustris
    • Harwood, C. S., and J. Gibson. 1988. Anaerobic and aerobic metabolism of diverse aromatic compounds by the photosynthetic bacterium Rhodopseudomonas palustris. Appl. Environ. Microbiol. 54:712-717.
    • (1988) Appl. Environ. Microbiol. , vol.54 , pp. 712-717
    • Harwood, C.S.1    Gibson, J.2
  • 20
    • 0014162610 scopus 로고
    • The metabolism of p-hydroxybenzoate by Rhodopseudomonas palustris and its regulation
    • Hegeman, G. D. 1967. The metabolism of p-hydroxybenzoate by Rhodopseudomonas palustris and its regulation. Arch. Microbiol. 59:143-148.
    • (1967) Arch. Microbiol. , vol.59 , pp. 143-148
    • Hegeman, G.D.1
  • 21
    • 0025812763 scopus 로고
    • Regulation of benzoate-CoA ligase in Rhodopseudomonas palustris
    • Kim, M.-K., and C. S. Harwood. 1991. Regulation of benzoate-CoA ligase in Rhodopseudomonas palustris. FEMS Microbiol. Lett. 83:199-204.
    • (1991) FEMS Microbiol. Lett. , vol.83 , pp. 199-204
    • Kim, M.-K.1    Harwood, C.S.2
  • 22
    • 0028793123 scopus 로고
    • Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes
    • Kovach, M. E., P. H. Elzer, D. S. Hill, G. T. Robertson, M. A. Farris, R. M. Roop II, and K. M. Peterson. 1995. Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes. Gene 166:175-176.
    • (1995) Gene , vol.166 , pp. 175-176
    • Kovach, M.E.1    Elzer, P.H.2    Hill, D.S.3    Robertson, G.T.4    Farris, M.A.5    Roop R.M. II6    Peterson, K.M.7
  • 23
    • 0025175101 scopus 로고
    • Mutations in fnr that alter anaerobic regulation of electron transport-associated genes in Escherichia coli
    • Melville, S. B., and R. P. Gunsalus. 1990. Mutations in fnr that alter anaerobic regulation of electron transport-associated genes in Escherichia coli. J. Biol. Chem. 265:18733-18736.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18733-18736
    • Melville, S.B.1    Gunsalus, R.P.2
  • 24
  • 25
    • 0014027888 scopus 로고
    • The conversion of catechol and protocatechuate to β-ketoadipate by Pseudomonas putida. I. Biochemistry
    • Ornston, L. N., and R. Y. Stanier. 1966. The conversion of catechol and protocatechuate to β-ketoadipate by Pseudomonas putida. I. Biochemistry. J. Biol. Chem. 241:3776-3786.
    • (1966) J. Biol. Chem. , vol.241 , pp. 3776-3786
    • Ornston, L.N.1    Stanier, R.Y.2
  • 26
    • 0027381431 scopus 로고
    • Construction and use of a new broad-host-range lacZ transcriptional fusion vector, pHRP309, for Gram bacteria
    • Parales, R. E., and C. S. Harwood. 1993. Construction and use of a new broad-host-range lacZ transcriptional fusion vector, pHRP309, for Gram bacteria. Gene 133:23-30.
    • (1993) Gene , vol.133 , pp. 23-30
    • Parales, R.E.1    Harwood, C.S.2
  • 27
    • 0000059204 scopus 로고
    • Gel-shift assay and DNase 1 footprinting in analysis of transcriptional regulation of biodegradation genes
    • K. W. Adolph (ed.). Academic Press, New York, N. Y.
    • Parsek, M. R., W. M. Coco, and A. M. Chakrabarty. 1994. Gel-shift assay and DNase 1 footprinting in analysis of transcriptional regulation of biodegradation genes, p. 273-290. In K. W. Adolph (ed.), Molecular biological techniques, part A, vol. 3. Academic Press, New York, N. Y.
    • (1994) Molecular Biological Techniques, Part A , vol.3 , pp. 273-290
    • Parsek, M.R.1    Coco, W.M.2    Chakrabarty, A.M.3
  • 28
    • 0027158657 scopus 로고
    • Versatile suicide vectors which allow direct selection for gene replacement in gram-negative bacteria
    • Quandt, J., and M. F. Hynes. 1993. Versatile suicide vectors which allow direct selection for gene replacement in gram-negative bacteria. Gene 127: 15-21.
    • (1993) Gene , vol.127 , pp. 15-21
    • Quandt, J.1    Hynes, M.F.2
  • 29
    • 50549178319 scopus 로고
    • Preparation of transforming deoxyribonucleic acid by phenol treatment
    • Saito, H., and K. I. Miura. 1963. Preparation of transforming deoxyribonucleic acid by phenol treatment. Biochim. Biophys. Acta 72:619-629.
    • (1963) Biochim. Biophys. Acta , vol.72 , pp. 619-629
    • Saito, H.1    Miura, K.I.2
  • 31
    • 0027134384 scopus 로고
    • Small broad-host-range gentamycin resistance gene cassettes for site-specific insertion and deletion mutagenesis
    • Schweizer, H. P. 1993. Small broad-host-range gentamycin resistance gene cassettes for site-specific insertion and deletion mutagenesis. BioTechniques 15:831-834.
    • (1993) BioTechniques , vol.15 , pp. 831-834
    • Schweizer, H.P.1
  • 32
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in gram-negative bacteria
    • Simon, R., U. Priefer, and A. Pühler. 1983. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in gram-negative bacteria. Bio/Technology 1:784-791.
    • (1983) Bio/Technology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 33
    • 0025173637 scopus 로고
    • Interconversion of the DNA-binding specificities of two related transcriptional regulators, CRP and FNR
    • Spiro, S., K. L. Gaston, A. I. Bell, R. E. Roberts, S. J. W. Busby, and J. R. Guest. 1990. Interconversion of the DNA-binding specificities of two related transcriptional regulators, CRP and FNR. Mol. Microbiol. 4:1831-1838.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1831-1838
    • Spiro, S.1    Gaston, K.L.2    Bell, A.I.3    Roberts, R.E.4    Busby, S.J.W.5    Guest, J.R.6
  • 34
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier, F. W., and B. A. Moffatt. 1986. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189:113-130.
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 35
    • 0021919826 scopus 로고
    • A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes
    • Tabor, S., and C. C. Richardson. 1985. A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes. Proc. Natl. Acad. Sci. USA 82:1074-1078.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 1074-1078
    • Tabor, S.1    Richardson, C.C.2
  • 36
    • 0028959433 scopus 로고
    • Nitrite and nitric oxide reduction in Paracoccus denitrificans is under the control of NNR, a regulatory protein that belongs to the FNR family of transcriptional activators
    • Van Spanning, R. J. M., A. P. N. De Boer, W. N. M. Reijnders, S. Spiro, H. V. Westerhoff, A. H. Stouthamer, and J. Van Der Oost. 1995. Nitrite and nitric oxide reduction in Paracoccus denitrificans is under the control of NNR, a regulatory protein that belongs to the FNR family of transcriptional activators. FEBS Lett. 360:151-154.
    • (1995) FEBS Lett. , vol.360 , pp. 151-154
    • Van Spanning, R.J.M.1    De Boer, A.P.N.2    Reijnders, W.N.M.3    Spiro, S.4    Westerhoff, H.V.5    Stouthamer, A.H.6    Van Der Oost, J.7
  • 37
    • 0031037665 scopus 로고    scopus 로고
    • FnrP and NNR of Paracoccus denitrificans are both members of the FNR family of transcriptional activators but have distinct roles in respiratory adaptation in response to oxygen limitation
    • Van Spanning, R. J. M., A. P. N. De Boer, W. N. M. Reijnders, H. V. Westerhoff, A. H. Stouthamer, and J. Van Der Oost. 1997. FnrP and NNR of Paracoccus denitrificans are both members of the FNR family of transcriptional activators but have distinct roles in respiratory adaptation in response to oxygen limitation. Mol. Microbiol. 25:893-907.
    • (1997) Mol. Microbiol. , vol.25 , pp. 893-907
    • Van Spanning, R.J.M.1    De Boer, A.P.N.2    Reijnders, W.N.M.3    Westerhoff, H.V.4    Stouthamer, A.H.5    Van Der Oost, J.6
  • 39
    • 0033060309 scopus 로고    scopus 로고
    • Multiple transcription factors of the FNR family in denitrifying Pseudomonas stutzeri: Characterization of four fnr-like genes, regulatory responses and cognate metabolic processes
    • Vollack, K.-U., E. Härtig, H. Körner, and W. G. Zumft. 1999. Multiple transcription factors of the FNR family in denitrifying Pseudomonas stutzeri: characterization of four fnr-like genes, regulatory responses and cognate metabolic processes. Mol. Microbiol. 31:1681-1694.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1681-1694
    • Vollack, K.-U.1    Härtig, E.2    Körner, H.3    Zumft, W.G.4
  • 40
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3


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