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Volumn 8, Issue 9, 2013, Pages

The Ferredoxin ThnA3 Negatively Regulates Tetralin Biodegradation Gene Expression via ThnY, a Ferredoxin Reductase That Functions as a Regulator of the Catabolic Pathway

Author keywords

[No Author keywords available]

Indexed keywords

BENZENE; CYCLOHEXANE; DECALIN; OXIDOREDUCTASE; PROTEIN THNY; TETRALIN DERIVATIVE; UNCLASSIFIED DRUG;

EID: 84884188121     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0073910     Document Type: Article
Times cited : (7)

References (25)
  • 1
    • 4444236429 scopus 로고    scopus 로고
    • Regulation of tetralin biodegradation and identification of genes essential for expression of thn operons
    • doi:10.1128/JB.186.18.6101-6109.2004
    • Martinez-Perez O, Moreno-Ruiz E, Floriano B, Santero E, (2004) Regulation of tetralin biodegradation and identification of genes essential for expression of thn operons. J Bacteriol 186: 6101-6109. doi:10.1128/JB.186.18.6101-6109.2004.
    • (2004) J Bacteriol , vol.186 , pp. 6101-6109
    • Martinez-Perez, O.1    Moreno-Ruiz, E.2    Floriano, B.3    Santero, E.4
  • 2
    • 76149133658 scopus 로고    scopus 로고
    • Tetralin-induced and ThnR-regulated aldehyde dehydrogenase and beta-oxidation genes in Sphingomonas macrogolitabida strain TFA
    • doi:10.1128/AEM.01846-09
    • Lopez-Sanchez A, Floriano B, Andujar E, Hernaez MJ, Santero E, (2010) Tetralin-induced and ThnR-regulated aldehyde dehydrogenase and beta-oxidation genes in Sphingomonas macrogolitabida strain TFA. Appl Environ Microbiol 76: 110-118. doi:10.1128/AEM.01846-09. PubMed: 19897762.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 110-118
    • Lopez-Sanchez, A.1    Floriano, B.2    Andujar, E.3    Hernaez, M.J.4    Santero, E.5
  • 3
    • 34248336957 scopus 로고    scopus 로고
    • Integrated response to inducers by communication between a catabolic pathway and its regulatory system
    • doi:10.1128/JB.00057-07
    • Martinez-Perez O, Lopez-Sanchez A, Reyes-Ramirez F, Floriano B, Santero E, (2007) Integrated response to inducers by communication between a catabolic pathway and its regulatory system. J Bacteriol 189: 3768-3775. doi:10.1128/JB.00057-07.
    • (2007) J Bacteriol , vol.189 , pp. 3768-3775
    • Martinez-Perez, O.1    Lopez-Sanchez, A.2    Reyes-Ramirez, F.3    Floriano, B.4    Santero, E.5
  • 4
    • 78751516684 scopus 로고    scopus 로고
    • ThnY is a ferredoxin reductase-like iron-sulfur flavoprotein that has evolved to function as a regulator of tetralin biodegradation gene expression
    • doi:10.1074/jbc.M110.184648
    • Garcia LL, Rivas-Marin E, Floriano B, Bernhardt R, Ewen KM, et al. (2011) ThnY is a ferredoxin reductase-like iron-sulfur flavoprotein that has evolved to function as a regulator of tetralin biodegradation gene expression. J Biol Chem 286: 1709-1718. doi:10.1074/jbc.M110.184648.
    • (2011) J Biol Chem , vol.286 , pp. 1709-1718
    • Garcia, L.L.1    Rivas-Marin, E.2    Floriano, B.3    Bernhardt, R.4    Ewen, K.M.5
  • 5
    • 70350169199 scopus 로고    scopus 로고
    • Co-ordinated regulation of two divergent promoters through higher-order complex formation by the LysR-type regulator ThnR
    • doi:10.1111/j.1365-2958.2009.06834.x
    • Lopez-Sanchez A, Rivas-Marin E, Martinez-Perez O, Floriano B, Santero E, (2009) Co-ordinated regulation of two divergent promoters through higher-order complex formation by the LysR-type regulator ThnR. Mol Microbiol 73: 1086-1100. doi:10.1111/j.1365-2958.2009.06834.x.
    • (2009) Mol Microbiol , vol.73 , pp. 1086-1100
    • Lopez-Sanchez, A.1    Rivas-Marin, E.2    Martinez-Perez, O.3    Floriano, B.4    Santero, E.5
  • 6
    • 0019321174 scopus 로고
    • Purification and characterization of an oxygenase component in benzoate 1,2-dioxygenase system from Pseudomonas arvilla C-1
    • PubMed:7372624
    • Yamaguchi M, Fujisawa H, (1980) Purification and characterization of an oxygenase component in benzoate 1,2-dioxygenase system from Pseudomonas arvilla C-1. J Biol Chem 255: 5058-5063. PubMed: 7372624.
    • (1980) J Biol Chem , vol.255 , pp. 5058-5063
    • Yamaguchi, M.1    Fujisawa, H.2
  • 7
    • 0025055440 scopus 로고
    • Purification and properties of NADH-ferredoxinNAP reductase, a component of naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816
    • PubMed:2294092
    • Haigler BE, Gibson DT, (1990) Purification and properties of NADH-ferredoxinNAP reductase, a component of naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816. J Bacteriol 172: 457-464. PubMed: 2294092.
    • (1990) J Bacteriol , vol.172 , pp. 457-464
    • Haigler, B.E.1    Gibson, D.T.2
  • 8
    • 0036947146 scopus 로고    scopus 로고
    • Purification and characterization of carbazole 1,9a-dioxygenase, a three-component dioxygenase system of Pseudomonas resinovorans strain CA10
    • doi:10.1128/AEM.68.12.5882-5890.2002
    • Nam JW, Nojiri H, Noguchi H, Uchimura H, Yoshida T, et al. (2002) Purification and characterization of carbazole 1,9a-dioxygenase, a three-component dioxygenase system of Pseudomonas resinovorans strain CA10. Appl Environ Microbiol 68: 5882-5890. doi:10.1128/AEM.68.12.5882-5890.2002.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 5882-5890
    • Nam, J.W.1    Nojiri, H.2    Noguchi, H.3    Uchimura, H.4    Yoshida, T.5
  • 10
    • 0037336362 scopus 로고    scopus 로고
    • Identification and functional characterization of Sphingomonas macrogolitabida strain TFA genes involved in the first two steps of the tetralin catabolic pathway
    • doi:10.1128/JB.185.6.2026-2030.2003
    • Moreno-Ruiz E, Hernaez MJ, Martinez-Perez O, Santero E, (2003) Identification and functional characterization of Sphingomonas macrogolitabida strain TFA genes involved in the first two steps of the tetralin catabolic pathway. J Bacteriol 185: 2026-2030. doi:10.1128/JB.185.6.2026-2030.2003.
    • (2003) J Bacteriol , vol.185 , pp. 2026-2030
    • Moreno-Ruiz, E.1    Hernaez, M.J.2    Martinez-Perez, O.3    Santero, E.4
  • 11
    • 0036301192 scopus 로고    scopus 로고
    • X-ray crystal structure of benzoate 1,2-dioxygenase reductase from Acinetobacter sp. strain ADP1
    • doi:10.1016/S0022-2836(02)00039-6
    • Karlsson A, Beharry ZM, Matthew Eby D, Coulter ED, Neidle EL, et al. (2002) X-ray crystal structure of benzoate 1,2-dioxygenase reductase from Acinetobacter sp. strain ADP1. J Mol Biol 318: 261-272. doi:10.1016/S0022-2836(02)00039-6.
    • (2002) J Mol Biol , vol.318 , pp. 261-272
    • Karlsson, A.1    Beharry, Z.M.2    Matthew Eby, D.3    Coulter, E.D.4    Neidle, E.L.5
  • 12
    • 0026023225 scopus 로고
    • Atomic structure of ferredoxin-NADP+ reductase: Prototype for a structurally novel flavoenzyme family
    • doi:10.1126/science.1986412
    • Karplus PA, Daniels MJ, Herriott JR, (1991) Atomic structure of ferredoxin-NADP+ reductase: prototype for a structurally novel flavoenzyme family. Science 251: 60-66. doi:10.1126/science.1986412. PubMed: 1986412.
    • (1991) Science , vol.251 , pp. 60-66
    • Karplus, P.A.1    Daniels, M.J.2    Herriott, J.R.3
  • 13
    • 0032989253 scopus 로고    scopus 로고
    • Aspartate 205 in the catalytic domain of naphthalene dioxygenase is essential for activity
    • Parales RE, Parales JV, Gibson DT, (1999) Aspartate 205 in the catalytic domain of naphthalene dioxygenase is essential for activity. J Bacteriol 181: 1831-1837.
    • (1999) J Bacteriol , vol.181 , pp. 1831-1837
    • Parales, R.E.1    Parales, J.V.2    Gibson, D.T.3
  • 14
    • 0034051818 scopus 로고    scopus 로고
    • Substrate specificity of naphthalene dioxygenase: Effect of specific amino acids at the active site of the enzyme
    • doi:10.1128/JB.182.6.1641-1649.2000
    • Parales RE, Lee K, Resnick SM, Jiang H, Lessner DJ, et al. (2000) Substrate specificity of naphthalene dioxygenase: effect of specific amino acids at the active site of the enzyme. J Bacteriol 182: 1641-1649. doi:10.1128/JB.182.6.1641-1649.2000. PubMed: 10692370.
    • (2000) J Bacteriol , vol.182 , pp. 1641-1649
    • Parales, R.E.1    Lee, K.2    Resnick, S.M.3    Jiang, H.4    Lessner, D.J.5
  • 16
    • 0342948903 scopus 로고    scopus 로고
    • Identification of an extradiol dioxygenase involved in tetralin biodegradation: Gene sequence analysis and purification and characterization of the gene product
    • doi:10.1128/JB.182.3.789-795.2000
    • Andujar E, Hernaez MJ, Kaschabek SR, Reineke W, Santero E, (2000) Identification of an extradiol dioxygenase involved in tetralin biodegradation: gene sequence analysis and purification and characterization of the gene product. J Bacteriol 182: 789-795. doi:10.1128/JB.182.3.789-795.2000. PubMed: 10633115.
    • (2000) J Bacteriol , vol.182 , pp. 789-795
    • Andujar, E.1    Hernaez, M.J.2    Kaschabek, S.R.3    Reineke, W.4    Santero, E.5
  • 17
    • 0016156623 scopus 로고
    • Isolation and characterization of a 3-chlorobenzoate degrading pseudomonad
    • doi:10.1007/BF00696222
    • Dorn E, Hellwig M, Reineke W, Knackmuss HJ, (1974) Isolation and characterization of a 3-chlorobenzoate degrading pseudomonad. Arch Microbiol 99: 61-70. doi:10.1007/BF00696222.
    • (1974) Arch Microbiol , vol.99 , pp. 61-70
    • Dorn, E.1    Hellwig, M.2    Reineke, W.3    Knackmuss, H.J.4
  • 18
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • doi:10.1016/0378-1119(89)90358-2
    • Ho SN, Hunt HD, Horton RM, Pullen JK, Pease LR, (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77: 51-59. doi:10.1016/0378-1119(89)90358-2.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 19
    • 0003205668 scopus 로고    scopus 로고
    • Molecular Cloning
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory., Cold Spring Harbor, NY, Cold Spring Harbor Laboratory
    • Sambrook J, Russell DW, (2001) Molecular cloning. A laboratory Manual. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory.
    • (2001) A Laboratory Manual
    • Sambrook, J.1    Russell, D.W.2
  • 20
    • 0025675856 scopus 로고
    • High efficiency transformation of Escherichia coli with plasmids
    • doi:10.1016/0378-1119(90)90336-P
    • Inoue H, Nojima H, Okayama H, (1990) High efficiency transformation of Escherichia coli with plasmids. Gene 96: 23-28. doi:10.1016/0378-1119(90)90336-P.
    • (1990) Gene , vol.96 , pp. 23-28
    • Inoue, H.1    Nojima, H.2    Okayama, H.3
  • 21
    • 0034005123 scopus 로고    scopus 로고
    • Genetic analysis of functions involved in adhesion of Pseudomonas putida to seeds
    • doi:10.1128/JB.182.9.2363-2369.2000
    • Espinosa-Urgel M, Salido A, Ramos JL, (2000) Genetic analysis of functions involved in adhesion of Pseudomonas putida to seeds. J Bacteriol 182: 2363-2369. doi:10.1128/JB.182.9.2363-2369.2000. PubMed: 10762233.
    • (2000) J Bacteriol , vol.182 , pp. 2363-2369
    • Espinosa-Urgel, M.1    Salido, A.2    Ramos, J.L.3
  • 22
    • 0003785155 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory., Cold Spring Harbor, NY, Cold Spring Harbor Laboratory
    • Miller JH, (1972) Experiments in molecular genetics. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • doi:10.1038/227680a0
    • Laemmli UK, (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685. doi:10.1038/227680a0.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0032524127 scopus 로고    scopus 로고
    • Structure of an aromatic-ring-hydroxylating dioxygenase-naphthalene 1,2-dioxygenase
    • doi:10.1016/S0969-2126(98)00059-8
    • Kauppi B, Lee K, Carredano E, Parales RE, Gibson DT, et al. (1998) Structure of an aromatic-ring-hydroxylating dioxygenase-naphthalene 1,2-dioxygenase. Structure 6: 571-586. doi:10.1016/S0969-2126(98)00059-8.
    • (1998) Structure , vol.6 , pp. 571-586
    • Kauppi, B.1    Lee, K.2    Carredano, E.3    Parales, R.E.4    Gibson, D.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.