메뉴 건너뛰기




Volumn 78, Issue 4, 2012, Pages 941-950

Identification and characterization of the LysR-type transcriptional regulator HsdR for steroid-inducible expression of the 3α-Hydroxysteroid dehydrogenase/carbonyl reductase gene in Comamonas testosteroni

Author keywords

[No Author keywords available]

Indexed keywords

COMAMONAS TESTOSTERONI; DE-REPRESSION; HYDROXYSTEROID DEHYDROGENASE; IN-VITRO; KEY ENZYMES; KNOCKOUT MUTANT; LOW LEVEL; MOBILITY SHIFT ASSAYS; POLYCLONAL ANTIBODY; POSITIVE TRANSCRIPTION; PROMOTER REGION; REDUCTASE GENES; RNA POLYMERASE; SOIL AND WATER; TESTOSTERONI; TRANSCRIPTIONAL FACTORS; TRANSCRIPTIONAL REGULATOR; TRANSFORMATION SYSTEMS; WILD TYPES;

EID: 84857066686     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.06872-11     Document Type: Article
Times cited : (15)

References (41)
  • 1
    • 0026215438 scopus 로고
    • Construction of novel expression vectors effective in Pseudomonas cells
    • Arai H, Igarashi Y, Kodama T. 1991. Construction of novel expression vectors effective in Pseudomonas cells. Agric. Biol. Chem. 55:2431-2432.
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 2431-2432
    • Arai, H.1    Igarashi, Y.2    Kodama, T.3
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0027389217 scopus 로고
    • Nucleotide sequence and initial functional characterization of the clcR gene encoding a LysR family activator of the clcABD chlorocatechol operon in Pseudomonas putida
    • Coco WM, Rothmel RK, Henikoff S, Chakrabarty AM. 1993. Nucleotide sequence and initial functional characterization of the clcR gene encoding a LysR family activator of the clcABD chlorocatechol operon in Pseudomonas putida. J. Bacteriol. 175:417-427.
    • (1993) J. Bacteriol. , vol.175 , pp. 417-427
    • Coco, W.M.1    Rothmel, R.K.2    Henikoff, S.3    Chakrabarty, A.M.4
  • 5
    • 0031958208 scopus 로고    scopus 로고
    • Regulation of benzoate degradation in Acinetobacter sp. strain ADP1 by BenM, a LysR-type transcriptional activator
    • Collier LS, Gaines GL, Neidle EL. 1998. Regulation of benzoate degradation in Acinetobacter sp. strain ADP1 by BenM, a LysR-type transcriptional activator. J. Bacteriol. 180:2493-2501.
    • (1998) J. Bacteriol. , vol.180 , pp. 2493-2501
    • Collier, L.S.1    Gaines, G.L.2    Neidle, E.L.3
  • 6
    • 47749106430 scopus 로고    scopus 로고
    • Testosterone-inducible regulator is a kinase that drives steroid sensing and metabolism in Comamonas testosteoni
    • Göhler A, Xiong G, Paulsen S, Trentmann G, Maser E. 2008. Testosterone-inducible regulator is a kinase that drives steroid sensing and metabolism in Comamonas testosteoni. J. Biol. Chem. 283:17380-17390.
    • (2008) J. Biol. Chem. , vol.283 , pp. 17380-17390
    • Göhler, A.1    Xiong, G.2    Paulsen, S.3    Trentmann, G.4    Maser, E.5
  • 7
    • 84857789802 scopus 로고    scopus 로고
    • Cloning, expression and characterization of a novel short-chain dehydrogenase/reductase (SDRx) in Comamonas testosteroni
    • doi:10.1016/ j.jsbmb.2010.11.008
    • Gong W, Xiong G, and Maser E. 2010. Cloning, expression and characterization of a novel short-chain dehydrogenase/reductase (SDRx) in Comamonas testosteroni. J. Steroid Biochem. Mol. Biol. doi:10.1016/ j.jsbmb.2010.11.008.
    • (2010) J. Steroid Biochem. Mol. Biol
    • Gong, W.1    Xiong, G.2    Maser, E.3
  • 8
    • 0030905387 scopus 로고    scopus 로고
    • Anaerobic mineralization of cholesterol by a novel type of denitrifying bacterium
    • Harder J, Probian C. 1997. Anaerobic mineralization of cholesterol by a novel type of denitrifying bacterium. Arch. Microbiol. 167:269-274.
    • (1997) Arch. Microbiol. , vol.167 , pp. 269-274
    • Harder, J.1    Probian, C.2
  • 10
    • 39749126195 scopus 로고    scopus 로고
    • The LysR-type transcriptional regulator LeuO controls expression of several genes in Salmonella enterica serovar Typhi
    • Hernández-Lucas I, et al. 2008. The LysR-type transcriptional regulator LeuO controls expression of several genes in Salmonella enterica serovar Typhi. J. Bacteriol. 190:1658-1670.
    • (2008) J. Bacteriol. , vol.190 , pp. 1658-1670
    • Hernández-Lucas, I.1
  • 11
    • 33750695273 scopus 로고    scopus 로고
    • RovM, a novel LysR-type regulator of the virulence activator gene rovA, controls cell invasion, virulence and motility of Yersinia pseudotuberculosis
    • Heroven AK, Dersch P. 2006. RovM, a novel LysR-type regulator of the virulence activator gene rovA, controls cell invasion, virulence and motility of Yersinia pseudotuberculosis. Mol. Microbiol. 62:1469-1483.
    • (2006) Mol. Microbiol. , vol.62 , pp. 1469-1483
    • Heroven, A.K.1    Dersch, P.2
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0023316582 scopus 로고
    • Pseudomonas mutant strains that accumulate androstane and seco-androstane intermediates from bile acids
    • Leppik RA, Sinden DJ. 1987. Pseudomonas mutant strains that accumulate androstane and seco-androstane intermediates from bile acids. Biochem. J. 243:15-21.
    • (1987) Biochem. J. , vol.243 , pp. 15-21
    • Leppik, R.A.1    Sinden, D.J.2
  • 14
    • 0024401346 scopus 로고
    • Binding of the Citrobacter freundii AmpR regulator to a single DNA site provides both autoregulation and activation of the inducible ampC beta-lactamase gene
    • Lindquist S, Lindberg F, Normark S. 1989. Binding of the Citrobacter freundii AmpR regulator to a single DNA site provides both autoregulation and activation of the inducible ampC beta-lactamase gene. J. Bacteriol. 171:3746-3753.
    • (1989) J. Bacteriol. , vol.171 , pp. 3746-3753
    • Lindquist, S.1    Lindberg, F.2    Normark, S.3
  • 15
    • 58949097886 scopus 로고    scopus 로고
    • Structure and function of the LysRtype transcriptional regulator (LTTR) family proteins
    • Maddocks SE, Oyston PCF. 2008. Structure and function of the LysRtype transcriptional regulator (LTTR) family proteins. Microbiology 154: 3609-3623.
    • (2008) Microbiology , vol.154 , pp. 3609-3623
    • Maddocks, S.E.1    Oyston, P.C.F.2
  • 16
    • 0030896478 scopus 로고    scopus 로고
    • Advances in microbial steroid biotransformation
    • Mahato SB, Garai S. 1997. Advances in microbial steroid biotransformation. Steroids 62:332-345.
    • (1997) Steroids , vol.62 , pp. 332-345
    • Mahato, S.B.1    Garai, S.2
  • 17
    • 0027690139 scopus 로고
    • Current trends in microbial steroid biotransformation
    • Mahato SB, Majumdar I. 1993. Current trends in microbial steroid biotransformation. Phytochemistry 34:883-898.
    • (1993) Phytochemistry , vol.34 , pp. 883-898
    • Mahato, S.B.1    Majumdar, I.2
  • 18
    • 0000068909 scopus 로고
    • Induction and purification of α- and β-hydroxysteroid dehydrogenases
    • Marcus PI, Talalay P. 1956. Induction and purification of α- and β-hydroxysteroid dehydrogenases. J. Biol. Chem. 218:661-674.
    • (1956) J. Biol. Chem. , vol.218 , pp. 661-674
    • Marcus, P.I.1    Talalay, P.2
  • 19
    • 0343090874 scopus 로고    scopus 로고
    • Functional expression, purification, and characterization of 3α-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni
    • Maser E, Möbus E, Xiong G. 2000. Functional expression, purification, and characterization of 3α-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni. Biochem. Biophys. Res. Commun. 272:622-628.
    • (2000) Biochem. Biophys. Res. Commun. , vol.272 , pp. 622-628
    • Maser, E.1    Möbus, E.2    Xiong, G.3
  • 20
    • 0030955228 scopus 로고    scopus 로고
    • Testosteroneregulated expression of enzymes involved in steroid and aromatic hydrocarbon catabolism in Comamonas testosteroni
    • Möbus E, Jahn M, Schmid R, Jahn D, Maser E. 1997. Testosteroneregulated expression of enzymes involved in steroid and aromatic hydrocarbon catabolism in Comamonas testosteroni. J. Bacteriol. 179:5951-5955.
    • (1997) J. Bacteriol. , vol.179 , pp. 5951-5955
    • Möbus, E.1    Jahn, M.2    Schmid, R.3    Jahn, D.4    Maser, E.5
  • 21
    • 0032729245 scopus 로고    scopus 로고
    • Transcriptional activation of the chlorocatechol degradative genes of Ralstonia eutropha NH9
    • Ogawa N, McFall SM, Klem TJ, Miyashita K, Chakrabarty AM. 1999. Transcriptional activation of the chlorocatechol degradative genes of Ralstonia eutropha NH9. J. Bacteriol. 181:6697-6705.
    • (1999) J. Bacteriol. , vol.181 , pp. 6697-6705
    • Ogawa, N.1    McFall, S.M.2    Klem, T.J.3    Miyashita, K.4    Chakrabarty, A.M.5
  • 22
    • 0030152146 scopus 로고    scopus 로고
    • Antibiotic resistance and enhanced insecticide catabolism as consequences of steroid induction in the Gram-negative bacterium Comamonas testosteroni
    • Oppermann UCT, Belai I, Maser E. 1996. Antibiotic resistance and enhanced insecticide catabolism as consequences of steroid induction in the Gram-negative bacterium Comamonas testosteroni. J. Steroid Biochem. Mol. Biol. 58:217-223.
    • (1996) J. Steroid Biochem. Mol. Biol. , vol.58 , pp. 217-223
    • Oppermann, U.C.T.1    Belai, I.2    Maser, E.3
  • 23
    • 0027532680 scopus 로고
    • Carbonyl reduction by 3α-HSD from Comamonas testosteroni-new properties and its relationship to the SCAD family
    • Oppermann UCT, Netter KJ, Maser E. 1993. Carbonyl reduction by 3α-HSD from Comamonas testosteroni-new properties and its relationship to the SCAD family. Adv. Exp. Med. Biol. 328:379-390.
    • (1993) Adv. Exp. Med. Biol. , vol.328 , pp. 379-390
    • Oppermann, U.C.T.1    Netter, K.J.2    Maser, E.3
  • 24
    • 0029973223 scopus 로고    scopus 로고
    • Characterization of a 3α-hydroxysteroid dehydrogenase/carbonyl reductase from the gramnegative bacterium Comamonas testosteroni
    • Oppermann UCT, Maser E. 1996. Characterization of a 3α-hydroxysteroid dehydrogenase/carbonyl reductase from the gramnegative bacterium Comamonas testosteroni. Eur. J. Biochem. 241:744-749.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 744-749
    • Oppermann, U.C.T.1    Maser, E.2
  • 25
    • 0028565028 scopus 로고
    • Interaction of two LysR-type regulatory proteins CatR and ClcR with heterologous promoters: functional and evolutionary implications
    • Parsek MR, McFall SM, Shinabarger DL, Chakrabarty AM. 1994. Interaction of two LysR-type regulatory proteins CatR and ClcR with heterologous promoters: functional and evolutionary implications. Proc. Natl. Acad. Sci. U. S. A. 91:12393-12397.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 12393-12397
    • Parsek, M.R.1    McFall, S.M.2    Shinabarger, D.L.3    Chakrabarty, A.M.4
  • 26
    • 33244467651 scopus 로고    scopus 로고
    • Bile salt biotransformations by human intestinal bacteria
    • Ridlon JM, Kang DJ, Hylemon PB. 2006. Bile salt biotransformations by human intestinal bacteria. J. Lipid Res. 47:241-259.
    • (2006) J. Lipid Res. , vol.47 , pp. 241-259
    • Ridlon, J.M.1    Kang, D.J.2    Hylemon, P.B.3
  • 27
    • 0028865450 scopus 로고
    • catM encodes a LysR-type transcriptional activator regulating catechol degradation in Acinetobacter calcoaceticus
    • Romero-Arroyo CE, Schell MA, Gaines GL, Neidle EL. 1995. catM encodes a LysR-type transcriptional activator regulating catechol degradation in Acinetobacter calcoaceticus. J. Bacteriol. 177:5891-5898.
    • (1995) J. Bacteriol. , vol.177 , pp. 5891-5898
    • Romero-Arroyo, C.E.1    Schell, M.A.2    Gaines, G.L.3    Neidle, E.L.4
  • 28
    • 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 RK, et al. 1990. 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) J. Bacteriol. , vol.172 , pp. 922-931
    • Rothmel, R.K.1
  • 29
    • 69049085674 scopus 로고    scopus 로고
    • The structure of CrgA from Neisseria meningitidis reveals a new octameric assembly state for LysR transcriptional regulators
    • Sainsbury S, et al. 2009. The structure of CrgA from Neisseria meningitidis reveals a new octameric assembly state for LysR transcriptional regulators. Nucleic Acids Res. 37:4545-4558.
    • (2009) Nucleic Acids Res , vol.37 , pp. 4545-4558
    • Sainsbury, S.1
  • 31
    • 79957580470 scopus 로고    scopus 로고
    • Steroid degradation and two steroidinducible enzymes in the marine bacterium H5
    • Sang Y, Xiong G, Maser E. 2011. Steroid degradation and two steroidinducible enzymes in the marine bacterium H5. Chem. Biol. Interact. 191:89-94.
    • (2011) Chem. Biol. Interact. , vol.191 , pp. 89-94
    • Sang, Y.1    Xiong, G.2    Maser, E.3
  • 32
    • 0027446708 scopus 로고
    • Schell MA. 1993. Molecular biology of the LysR family of transcriptional regulators. Annu. Rev. Microbiol. 47:597-626.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 597-626
    • Schell, M.A.1
  • 33
    • 0001078277 scopus 로고
    • Oxidative degradation of testosterone by adaptive enzymes
    • Talalay P, Dobson MM, Tapley DF. 1952. Oxidative degradation of testosterone by adaptive enzymes. Nature 170:620-621.
    • (1952) Nature , vol.170 , pp. 620-621
    • Talalay, P.1    Dobson, M.M.2    Tapley, D.F.3
  • 34
    • 0023119345 scopus 로고
    • Reclassification of Pseudomonas acidovorans den Dooren de Jong 1926 and Pseudomonas testosteroni Marcus and Talahay 1956 as Comamonas acidovorans comb. nov. and Comamonas testosteroni comb. nov. with an emended description of the genus Comamonas
    • Tamaoka J, Ha DM, Komagata K. 1987. Reclassification of Pseudomonas acidovorans den Dooren de Jong 1926 and Pseudomonas testosteroni Marcus and Talahay 1956 as Comamonas acidovorans comb. nov. and Comamonas testosteroni comb. nov. with an emended description of the genus Comamonas. Int. J. Syst. Bacteriol. 37:52-59.
    • (1987) Int. J. Syst. Bacteriol. , vol.37 , pp. 52-59
    • Tamaoka, J.1    Ha, D.M.2    Komagata, K.3
  • 35
    • 0030000879 scopus 로고    scopus 로고
    • Crystal structures of the binary and ternary complexes of 7α-hydroxysteroid dehydrogenase from Escherichia coli
    • Tanaka N, et al. 1996. Crystal structures of the binary and ternary complexes of 7α-hydroxysteroid dehydrogenase from Escherichia coli. Biochemistry 35:7715-7730.
    • (1996) Biochemistry , vol.35 , pp. 7715-7730
    • Tanaka, N.1
  • 36
    • 0025740524 scopus 로고
    • Characterization of the Pseudomonas sp. strain P51 gene tcbR, a LysR-type transcriptional activator of the tcbCDEF chlorocatechol oxidative operon, and analyses of the regulatory region
    • van der Meer JR, et al. 1991. Characterization of the Pseudomonas sp. strain P51 gene tcbR, a LysR-type transcriptional activator of the tcbCDEF chlorocatechol oxidative operon, and analyses of the regulatory region. J. Bacteriol. 173:3700-3708.
    • (1991) J. Bacteriol. , vol.173 , pp. 3700-3708
    • van der Meer, J.R.1
  • 37
    • 34247516876 scopus 로고    scopus 로고
    • The conformational quality of insoluble recombinant proteins is enhanced at low growth temperatures
    • Vera A, Gonzalez-Montalban N, Aris A, Villaverde A. 2007. The conformational quality of insoluble recombinant proteins is enhanced at low growth temperatures. Biotechnol. Bioeng. 96:1101-1106.
    • (2007) Biotechnol. Bioeng. , vol.96 , pp. 1101-1106
    • Vera, A.1    Gonzalez-Montalban, N.2    Aris, A.3    Villaverde, A.4
  • 38
    • 0035971088 scopus 로고    scopus 로고
    • Regulation of the steroid-inducible 3α-hydroxysteroid dehydrogenase/carbonyl reductase gene in Comamonas testosteroni
    • Xiong G, Maser E. 2001. Regulation of the steroid-inducible 3α-hydroxysteroid dehydrogenase/carbonyl reductase gene in Comamonas testosteroni. J. Biol. Chem. 276:9961-9970.
    • (2001) J. Biol. Chem. , vol.276 , pp. 9961-9970
    • Xiong, G.1    Maser, E.2
  • 39
    • 0346850869 scopus 로고    scopus 로고
    • Identification and characterization of a novel translational repressor of the steroid-inducible 3α-hydroxysteroid dehydrogenase/carbonyl reductase gene in Comamonas testosteroni
    • Xiong G, Martin HJ, Maser E. 2003. Identification and characterization of a novel translational repressor of the steroid-inducible 3α-hydroxysteroid dehydrogenase/carbonyl reductase gene in Comamonas testosteroni. J. Biol. Chem. 278:47400-47407.
    • (2003) J. Biol. Chem. , vol.278 , pp. 47400-47407
    • Xiong, G.1    Martin, H.J.2    Maser, E.3
  • 40
    • 0037330103 scopus 로고    scopus 로고
    • Regulation of 3α-hydroxysteroid dehydrogenase/carbonyl reductase in Comamonas testosteroni: function and relationship of two operators
    • Xiong G, Markowetz S, Maser E. 2003. Regulation of 3α-hydroxysteroid dehydrogenase/carbonyl reductase in Comamonas testosteroni: function and relationship of two operators. Chem. Biol. Interact. 143-144:411-423.
    • (2003) Chem. Biol. Interact. , vol.143-144 , pp. 411-423
    • Xiong, G.1    Markowetz, S.2    Maser, E.3
  • 41
    • 79957555816 scopus 로고    scopus 로고
    • Characterization of the steroid degrading bacterium S19-1 from the Baltic Sea at Kiel Germany
    • Zhang T, Xiong G, Maser E. 2011. Characterization of the steroid degrading bacterium S19-1 from the Baltic Sea at Kiel, Germany. Chem. Biol. Interact. 191:83-88.
    • (2011) Chem. Biol. Interact. , vol.191 , pp. 83-88
    • Zhang, T.1    Xiong, G.2    Maser, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.