메뉴 건너뛰기




Volumn 9, Issue 11, 2014, Pages

Regulation of the ahpC gene encoding alkyl hydroperoxide reductase in Mycobacterium smegmatis

Author keywords

[No Author keywords available]

Indexed keywords

ALKYL HYDROPEROXIDE REDUCTASE; CYCLIC AMP; CYCLIC AMP RECEPTOR; FERRIC UPTAKE REGULATOR; GENOMIC DNA; MESSENGER RNA; OXIDOREDUCTASE; PEROXIDE; PEROXYNITRITE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; PEROXIREDOXIN;

EID: 84909619252     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0111680     Document Type: Article
Times cited : (24)

References (66)
  • 3
    • 0034648827 scopus 로고    scopus 로고
    • Peroxynitrite reductase activity of bacterial peroxiredoxins
    • Bryk R, Griffin P, Nathan C (2000) Peroxynitrite reductase activity of bacterial peroxiredoxins. Nature 407: 211-215.
    • (2000) Nature , vol.407 , pp. 211-215
    • Bryk, R.1    Griffin, P.2    Nathan, C.3
  • 4
    • 0032060482 scopus 로고    scopus 로고
    • Alkyl hydroperoxide reductase subunit C (AhpC) protects bacterial and human cells against reactive nitrogen intermediates
    • Chen L, Xie QW, Nathan C (1998) Alkyl hydroperoxide reductase subunit C (AhpC) protects bacterial and human cells against reactive nitrogen intermediates. Mol Cell 1: 795-805.
    • (1998) Mol Cell , vol.1 , pp. 795-805
    • Chen, L.1    Xie, Q.W.2    Nathan, C.3
  • 5
    • 0036772990 scopus 로고    scopus 로고
    • Oxidative stress response genes in Mycobacterium tuberculosis: Role of ahpC in resistance to peroxynitrite and stage-specific survival in macrophages
    • Master SS, Springer B, Sander P, Boettger EC, Deretic V, et al. (2002) Oxidative stress response genes in Mycobacterium tuberculosis: role of ahpC in resistance to peroxynitrite and stage-specific survival in macrophages. Microbiology 148: 3139-3144.
    • (2002) Microbiology , vol.148 , pp. 3139-3144
    • Master, S.S.1    Springer, B.2    Sander, P.3    Boettger, E.C.4    Deretic, V.5
  • 6
    • 2642535136 scopus 로고    scopus 로고
    • Intermolecular interactions in the AhpC/AhpD antioxidant defense system of Mycobacterium tuberculosis
    • Koshkin A, Knudsen GM, Ortiz De Montellano PR (2004) Intermolecular interactions in the AhpC/AhpD antioxidant defense system of Mycobacterium tuberculosis. Arch Biochem Biophys 427: 41-47.
    • (2004) Arch Biochem Biophys , vol.427 , pp. 41-47
    • Koshkin, A.1    Knudsen, G.M.2    Ortiz De Montellano, P.R.3
  • 7
    • 21844442599 scopus 로고    scopus 로고
    • Structure and mechanism of the alkyl hydroperoxidase AhpC, a key element of the Mycobacterium tuberculosis defense system against oxidative stress
    • Guimaraes BG, Souchon H, Honore N, Saint-Joanis B, Brosch R, et al. (2005) Structure and mechanism of the alkyl hydroperoxidase AhpC, a key element of the Mycobacterium tuberculosis defense system against oxidative stress. J Biol Chem 280: 25735-25742.
    • (2005) J Biol Chem , vol.280 , pp. 25735-25742
    • Guimaraes, B.G.1    Souchon, H.2    Honore, N.3    Saint-Joanis, B.4    Brosch, R.5
  • 8
    • 0036799732 scopus 로고    scopus 로고
    • Site-directed mutagenesis reveals a novel catalytic mechanism of Mycobacterium tuberculosis alkylhydroperoxidase C
    • Chauhan R, Mande SC (2002) Site-directed mutagenesis reveals a novel catalytic mechanism of Mycobacterium tuberculosis alkylhydroperoxidase C. Biochem J 367: 255-261.
    • (2002) Biochem J , vol.367 , pp. 255-261
    • Chauhan, R.1    Mande, S.C.2
  • 9
    • 0037039818 scopus 로고    scopus 로고
    • Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein
    • Bryk R, Lima CD, Erdjument-Bromage H, Tempst P, Nathan C (2002) Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein. Science 295: 1073-1077.
    • (2002) Science , vol.295 , pp. 1073-1077
    • Bryk, R.1    Lima, C.D.2    Erdjument-Bromage, H.3    Tempst, P.4    Nathan, C.5
  • 10
    • 1042278885 scopus 로고    scopus 로고
    • Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis
    • Jaeger T, Budde H, Flohe L, Menge U, Singh M, et al. (2004) Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis. Archives of Biochemistry and Biophysics 423: 182-191.
    • (2004) Archives of Biochemistry and Biophysics , vol.423 , pp. 182-191
    • Jaeger, T.1    Budde, H.2    Flohe, L.3    Menge, U.4    Singh, M.5
  • 11
    • 84862970518 scopus 로고    scopus 로고
    • Mycobacterium smegmatis RoxY is a repressor of oxyS and contributes to resistance to oxidative stress and bactericidal ubiquitin-derived peptides
    • Daugherty A, Powers KM, Standley MS, Kim CS, Purdy GE (2011) Mycobacterium smegmatis RoxY is a repressor of oxyS and contributes to resistance to oxidative stress and bactericidal ubiquitin-derived peptides. J Bacteriol 193: 6824-6833.
    • (2011) J Bacteriol , vol.193 , pp. 6824-6833
    • Daugherty, A.1    Powers, K.M.2    Standley, M.S.3    Kim, C.S.4    Purdy, G.E.5
  • 12
    • 0031660550 scopus 로고    scopus 로고
    • Oxidative stress response and characterization of the oxyR-ahpC and furA-katG loci in Mycobacterium marinum
    • Pagan-Ramos E, Song J, McFalone M, Mudd MH, Deretic V (1998) Oxidative stress response and characterization of the oxyR-ahpC and furA-katG loci in Mycobacterium marinum. J Bacteriol 180: 4856-4864.
    • (1998) J Bacteriol , vol.180 , pp. 4856-4864
    • Pagan-Ramos, E.1    Song, J.2    McFalone, M.3    Mudd, M.H.4    Deretic, V.5
  • 13
    • 0028882958 scopus 로고
    • Mycobacterium tuberculosis is a natural mutant with an inactivated oxidativestress regulatory gene: Implications for sensitivity to isoniazid
    • Deretic V, Philipp W, Dhandayuthapani S, Mudd MH, Curcic R, et al. (1995) Mycobacterium tuberculosis is a natural mutant with an inactivated oxidativestress regulatory gene: implications for sensitivity to isoniazid. Mol Microbiol 17: 889-900.
    • (1995) Mol Microbiol , vol.17 , pp. 889-900
    • Deretic, V.1    Philipp, W.2    Dhandayuthapani, S.3    Mudd, M.H.4    Curcic, R.5
  • 15
    • 0029888258 scopus 로고    scopus 로고
    • Oxidative stress response and its role in sensitivity to isoniazid in mycobacteria: Characterization and inducibility of ahpC by peroxides in Mycobacterium smegmatis and lack of expression in M. Aurum and M. Tuberculosis
    • Dhandayuthapani S, Zhang Y, Mudd MH, Deretic V (1996) Oxidative stress response and its role in sensitivity to isoniazid in mycobacteria: characterization and inducibility of ahpC by peroxides in Mycobacterium smegmatis and lack of expression in M. aurum and M. tuberculosis. J Bacteriol 178: 3641-3649.
    • (1996) J Bacteriol , vol.178 , pp. 3641-3649
    • Dhandayuthapani, S.1    Zhang, Y.2    Mudd, M.H.3    Deretic, V.4
  • 16
    • 0034826633 scopus 로고    scopus 로고
    • Silencing of oxidative stress response in Mycobacterium tuberculosis: Expression patterns of ahpC in virulent and avirulent strains and effect of ahpC inactivation
    • Springer B, Master S, Sander P, Zahrt T, McFalone M, et al. (2001) Silencing of oxidative stress response in Mycobacterium tuberculosis: expression patterns of ahpC in virulent and avirulent strains and effect of ahpC inactivation. Infect Immun 69: 5967-5973.
    • (2001) Infect Immun , vol.69 , pp. 5967-5973
    • Springer, B.1    Master, S.2    Sander, P.3    Zahrt, T.4    McFalone, M.5
  • 17
    • 0038141898 scopus 로고    scopus 로고
    • The senX3-regX3 two-component regulatory system of Mycobacterium tuberculosis is required for virulence
    • Parish T, Smith DA, Roberts G, Betts J, Stoker NG (2003) The senX3-regX3 two-component regulatory system of Mycobacterium tuberculosis is required for virulence. Microbiology 149: 1423-1435.
    • (2003) Microbiology , vol.149 , pp. 1423-1435
    • Parish, T.1    Smith, D.A.2    Roberts, G.3    Betts, J.4    Stoker, N.G.5
  • 18
    • 19944418509 scopus 로고    scopus 로고
    • A member of the cAMP receptor protein family of transcription regulators in Mycobacterium tuberculosis is required for virulence in mice and controls transcription of the rpfA gene coding for a resuscitation promoting factor
    • Rickman L, Scott C, Hunt DM, Hutchinson T, Menendez MC, et al. (2005) A member of the cAMP receptor protein family of transcription regulators in Mycobacterium tuberculosis is required for virulence in mice and controls transcription of the rpfA gene coding for a resuscitation promoting factor. Mol Microbiol 56: 1274-1286.
    • (2005) Mol Microbiol , vol.56 , pp. 1274-1286
    • Rickman, L.1    Scott, C.2    Hunt, D.M.3    Hutchinson, T.4    Menendez, M.C.5
  • 19
    • 0034902327 scopus 로고    scopus 로고
    • Role of OxyS of Mycobacterium tuberculosis in oxidative stress: Overexpression confers increased sensitivity to organic hydroperoxides
    • Domenech P, Honore N, Heym B, Cole ST (2001) Role of OxyS of Mycobacterium tuberculosis in oxidative stress: overexpression confers increased sensitivity to organic hydroperoxides. Microbes Infect 3: 713-721.
    • (2001) Microbes Infect , vol.3 , pp. 713-721
    • Domenech, P.1    Honore, N.2    Heym, B.3    Cole, S.T.4
  • 20
    • 84866029444 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis WhiB4 regulates oxidative stress response to modulate survival and dissemination in vivo
    • Chawla M, Parikh P, Saxena A, Munshi M, Mehta M, et al. (2012) Mycobacterium tuberculosis WhiB4 regulates oxidative stress response to modulate survival and dissemination in vivo. Mol Microbiol 85: 1148-1165.
    • (2012) Mol Microbiol , vol.85 , pp. 1148-1165
    • Chawla, M.1    Parikh, P.2    Saxena, A.3    Munshi, M.4    Mehta, M.5
  • 21
    • 77952046005 scopus 로고    scopus 로고
    • The SigF regulon in Mycobacterium smegmatis reveals roles in adaptation to stationary phase, heat, and oxidative stress
    • Humpel A, Gebhard S, Cook GM, Berney M (2010) The SigF regulon in Mycobacterium smegmatis reveals roles in adaptation to stationary phase, heat, and oxidative stress. J Bacteriol 192: 2491-2502.
    • (2010) J Bacteriol , vol.192 , pp. 2491-2502
    • Humpel, A.1    Gebhard, S.2    Cook, G.M.3    Berney, M.4
  • 22
    • 2442655332 scopus 로고    scopus 로고
    • Transcriptome analysis of Crp-dependent catabolite control of gene expression in Escherichia coli
    • Gosset G, Zhang Z, Nayyar S, Cuevas WA, Saier MH Jr (2004) Transcriptome analysis of Crp-dependent catabolite control of gene expression in Escherichia coli. J Bacteriol 186: 3516-3524.
    • (2004) J Bacteriol , vol.186 , pp. 3516-3524
    • Gosset, G.1    Zhang, Z.2    Nayyar, S.3    Cuevas, W.A.4    Saier, M.H.J.R.5
  • 23
    • 73649126198 scopus 로고    scopus 로고
    • Structural insights into the mechanism of the allosteric transitions of Mycobacterium tuberculosis cAMP receptor protein
    • Reddy MC, Palaninathan SK, Bruning JB, Thurman C, Smith D, et al. (2009) Structural insights into the mechanism of the allosteric transitions of Mycobacterium tuberculosis cAMP receptor protein. J Biol Chem 284: 36581-36591.
    • (2009) J Biol Chem , vol.284 , pp. 36581-36591
    • Reddy, M.C.1    Palaninathan, S.K.2    Bruning, J.B.3    Thurman, C.4    Smith, D.5
  • 24
    • 67649745795 scopus 로고    scopus 로고
    • Profound asymmetry in the structure of the cAMP-free cAMP Receptor Protein (CRP) from Mycobacterium tuberculosis
    • Gallagher DT, Smith N, Kim SK, Robinson H, Reddy PT (2009) Profound asymmetry in the structure of the cAMP-free cAMP Receptor Protein (CRP) from Mycobacterium tuberculosis. J Biol Chem 284: 8228-8232.
    • (2009) J Biol Chem , vol.284 , pp. 8228-8232
    • Gallagher, D.T.1    Smith, N.2    Kim, S.K.3    Robinson, H.4    Reddy, P.T.5
  • 25
    • 77049087556 scopus 로고    scopus 로고
    • Mapping conformational transitions in cyclic AMP receptor protein: Crystal structure and normal-mode analysis of Mycobacterium tuberculosis apo-cAMP receptor protein
    • Kumar P, Joshi DC, Akif M, Akhter Y, Hasnain SE, et al. (2010) Mapping conformational transitions in cyclic AMP receptor protein: crystal structure and normal-mode analysis of Mycobacterium tuberculosis apo-cAMP receptor protein. Biophys J 98: 305-314.
    • (2010) Biophys J , vol.98 , pp. 305-314
    • Kumar, P.1    Joshi, D.C.2    Akif, M.3    Akhter, Y.4    Hasnain, S.E.5
  • 26
    • 77951243882 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis cAMP receptor protein (Rv3676) differs from the Escherichia coli paradigm in its cAMP binding and DNA binding properties and transcription activation properties
    • Stapleton M, Haq I, Hunt DM, Arnvig KB, Artymiuk PJ, et al. (2010) Mycobacterium tuberculosis cAMP receptor protein (Rv3676) differs from the Escherichia coli paradigm in its cAMP binding and DNA binding properties and transcription activation properties. J Biol Chem 285: 7016-7027.
    • (2010) J Biol Chem , vol.285 , pp. 7016-7027
    • Stapleton, M.1    Haq, I.2    Hunt, D.M.3    Arnvig, K.B.4    Artymiuk, P.J.5
  • 27
    • 84893474292 scopus 로고    scopus 로고
    • Cyclic-AMP and bacterial cyclic-AMP receptor proteins revisited: Adaptation for different ecological niches
    • Green J, Stapleton MR, Smith LJ, Artymiuk PJ, Kahramanoglou C, et al. (2014) Cyclic-AMP and bacterial cyclic-AMP receptor proteins revisited: adaptation for different ecological niches. Curr Opin Microbiol 18: 1-7.
    • (2014) Curr Opin Microbiol , vol.18 , pp. 1-7
    • Green, J.1    Stapleton, M.R.2    Smith, L.J.3    Artymiuk, P.J.4    Kahramanoglou, C.5
  • 28
    • 58149291646 scopus 로고    scopus 로고
    • CAMP levels within Mycobacterium tuberculosis and Mycobacterium bovis BCG increase upon infection of macrophages
    • Bai G, Schaak DD, McDonough KA (2009) cAMP levels within Mycobacterium tuberculosis and Mycobacterium bovis BCG increase upon infection of macrophages. FEMS Immunol Med Microbiol 55: 68-73.
    • (2009) FEMS Immunol Med Microbiol , vol.55 , pp. 68-73
    • Bai, G.1    Schaak, D.D.2    McDonough, K.A.3
  • 29
    • 2142763090 scopus 로고    scopus 로고
    • Increased mitogen-activated protein kinase activity and TNF-A production associated with Mycobacterium smegmatisbut not Mycobacterium avium-infected macrophages requires prolonged stimulation of the calmodulin/calmodulin kinase and cyclic AMP/protein kinase A pathways
    • Yadav M, Roach SK, Schorey JS (2004) Increased mitogen-activated protein kinase activity and TNF-a production associated with Mycobacterium smegmatisbut not Mycobacterium avium-infected macrophages requires prolonged stimulation of the calmodulin/calmodulin kinase and cyclic AMP/protein kinase A pathways. J Immunol 172: 5588-5597.
    • (2004) J Immunol , vol.172 , pp. 5588-5597
    • Yadav, M.1    Roach, S.K.2    Schorey, J.S.3
  • 30
    • 0344172832 scopus 로고    scopus 로고
    • Opening the iron box: Transcriptional metalloregulation by the fur protein
    • Escolar L, Perez-Martin J, de Lorenzo V (1999) Opening the iron box: transcriptional metalloregulation by the Fur protein. J Bacteriol 181: 6223-6229.
    • (1999) J Bacteriol , vol.181 , pp. 6223-6229
    • Escolar, L.1    Perez-Martin, J.2    De Lorenzo, V.3
  • 31
    • 0035013527 scopus 로고    scopus 로고
    • Regulation of catalase-peroxidase (KatG) expression, isoniazid sensitivity and virulence by furA of Mycobacterium tuberculosis
    • Pym AS, Domenech P, Honore N, Song J, Deretic V, et al. (2001) Regulation of catalase-peroxidase (KatG) expression, isoniazid sensitivity and virulence by furA of Mycobacterium tuberculosis. Mol Microbiol 40: 879-889.
    • (2001) Mol Microbiol , vol.40 , pp. 879-889
    • Pym, A.S.1    Domenech, P.2    Honore, N.3    Song, J.4    Deretic, V.5
  • 32
    • 33846640080 scopus 로고    scopus 로고
    • Global analysis of the Mycobacterium tuberculosis Zur (FurB) regulon
    • Maciag A, Dainese E, Rodriguez GM, Milano A, Provvedi R, et al. (2007) Global analysis of the Mycobacterium tuberculosis Zur (FurB) regulon. J Bacteriol 189: 730-740.
    • (2007) J Bacteriol , vol.189 , pp. 730-740
    • Maciag, A.1    Dainese, E.2    Rodriguez, G.M.3    Milano, A.4    Provvedi, R.5
  • 34
    • 0025081151 scopus 로고
    • Isolation and characterization of efficient plasmid transformation mutants of Mycobacterium smegmatis
    • Snapper SB, Melton RE, Mustafa S, Kieser T, Jacobs WR Jr (1990) Isolation and characterization of efficient plasmid transformation mutants of Mycobacterium smegmatis. Mol Microbiol 4: 1911-1919.
    • (1990) Mol Microbiol , vol.4 , pp. 1911-1919
    • Snapper, S.B.1    Melton, R.E.2    Mustafa, S.3    Kieser, T.4    Jacobs, W.R.J.R.5
  • 35
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko KA, Wanner BL (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci U S A 97: 6640-6645.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 36
    • 0036774617 scopus 로고    scopus 로고
    • Specialized transduction: An efficient method for generating marked and unmarked targeted gene disruptions in Mycobacterium tuberculosis, M. Bovis BCG and M. Smegmatis
    • Bardarov S, Bardarov S Jr, PavelkaMS Jr, Sambandamurthy V, Larsen M, et al. (2002) Specialized transduction: an efficient method for generating marked and unmarked targeted gene disruptions in Mycobacterium tuberculosis, M. bovis BCG and M. smegmatis. Microbiology 148: 3007-3017.
    • (2002) Microbiology , vol.148 , pp. 3007-3017
    • Bardarov, S.1    Bardarov, S.2    Pavelka, M.S.3    Sambandamurthy, V.4    Larsen, M.5
  • 37
    • 77957327437 scopus 로고    scopus 로고
    • Different roles of DosS and DosT in the hypoxic adaptation of Mycobacteria
    • Kim MJ, Park KJ, Ko IJ, Kim YM, Oh JI (2010) Different roles of DosS and DosT in the hypoxic adaptation of Mycobacteria. J Bacteriol 192: 4868-4875.
    • (2010) J Bacteriol , vol.192 , pp. 4868-4875
    • Kim, M.J.1    Park, K.J.2    Ko, I.J.3    Kim, Y.M.4    Oh, J.I.5
  • 38
    • 0031774285 scopus 로고    scopus 로고
    • Redox-dependent gene regulation in Rhodobacter sphaeroides 2. 4.1T: Effects on dimethyl sulfoxide reductase (dor) gene expression
    • Mouncey NJ, Kaplan S (1998) Redox-dependent gene regulation in Rhodobacter sphaeroides 2.4.1T: effects on dimethyl sulfoxide reductase (dor) gene expression. J Bacteriol 180: 5612-5618.
    • (1998) J Bacteriol , vol.180 , pp. 5612-5618
    • Mouncey, N.J.1    Kaplan, S.2
  • 39
    • 0033514508 scopus 로고    scopus 로고
    • The cbb3 terminal oxidase of Rhodobacter sphaeroides 2.4.1: Structural and functional implications for the regulation of spectral complex formation
    • Oh JI, Kaplan S (1999) The cbb3 terminal oxidase of Rhodobacter sphaeroides 2.4.1: structural and functional implications for the regulation of spectral complex formation. Biochemistry 38: 2688-2696.
    • (1999) Biochemistry , vol.38 , pp. 2688-2696
    • Oh, J.I.1    Kaplan, S.2
  • 41
    • 0036776767 scopus 로고    scopus 로고
    • DNA gyrase genes in Mycobacterium tuberculosis: A single operon driven by multiple promoters
    • Unniraman S, Chatterji M, Nagaraja V (2002) DNA gyrase genes in Mycobacterium tuberculosis: a single operon driven by multiple promoters. J Bacteriol 184: 5449-5456.
    • (2002) J Bacteriol , vol.184 , pp. 5449-5456
    • Unniraman, S.1    Chatterji, M.2    Nagaraja, V.3
  • 42
    • 0023894726 scopus 로고
    • Selection of DNA binding sites by regulatory proteins. II. The binding specificity of cyclic AMP receptor protein to recognition sites
    • Berg OG, von Hippel PH (1988) Selection of DNA binding sites by regulatory proteins. II. The binding specificity of cyclic AMP receptor protein to recognition sites. J Mol Biol 200: 709-723.
    • (1988) J Mol Biol , vol.200 , pp. 709-723
    • Berg, O.G.1    Von Hippel, P.H.2
  • 43
    • 0042337280 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis FurA autoregulates its own expression
    • Sala C, Forti F, Di Florio E, Canneva F, Milano A, et al. (2003) Mycobacterium tuberculosis FurA autoregulates its own expression. J Bacteriol 185: 5357-5362.
    • (2003) J Bacteriol , vol.185 , pp. 5357-5362
    • Sala, C.1    Forti, F.2    Di Florio, E.3    Canneva, F.4    Milano, A.5
  • 44
    • 0029805172 scopus 로고    scopus 로고
    • Nitric oxide, superoxide, and peroxynitrite: The good, the bad, and ugly
    • Beckman JS, Koppenol WH (1996) Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly. Am J Physiol 271: C1424-1437.
    • (1996) Am J Physiol , vol.271 , pp. C1424-1437
    • Beckman, J.S.1    Koppenol, W.H.2
  • 45
    • 27744449032 scopus 로고    scopus 로고
    • Characterization of Mycobacterium tuberculosis Rv3676 (CRPMt), a cyclic AMP receptor protein-like DNA binding protein
    • Bai G, McCue LA, McDonough KA (2005) Characterization of Mycobacterium tuberculosis Rv3676 (CRPMt), a cyclic AMP receptor protein-like DNA binding protein. J Bacteriol 187: 7795-7804.
    • (2005) J Bacteriol , vol.187 , pp. 7795-7804
    • Bai, G.1    McCue, L.A.2    McDonough, K.A.3
  • 46
    • 0023664923 scopus 로고
    • Ferric uptake regulation protein acts as a repressor, employing iron (II) as a cofactor to bind the operator of an iron transport operon in Escherichia coli
    • Bagg A, Neilands JB (1987) Ferric uptake regulation protein acts as a repressor, employing iron (II) as a cofactor to bind the operator of an iron transport operon in Escherichia coli. Biochemistry 26: 5471-5477.
    • (1987) Biochemistry , vol.26 , pp. 5471-5477
    • Bagg, A.1    Neilands, J.B.2
  • 47
    • 0032698634 scopus 로고    scopus 로고
    • Transcription activation by catabolite activator protein (CAP)
    • Busby S, Ebright RH (1999) Transcription activation by catabolite activator protein (CAP). J Mol Biol 293: 199-213.
    • (1999) J Mol Biol , vol.293 , pp. 199-213
    • Busby, S.1    Ebright, R.H.2
  • 48
    • 84905594249 scopus 로고    scopus 로고
    • Genomic mapping of cAMP receptor protein (CRPMt) in Mycobacterium tuberculosis: Relation to transcriptional start sites and the role of CRPMt as a transcription factor
    • Kahramanoglou C, Cortes T, Matange N, Hunt DM, Visweswariah SS, et al. (2014) Genomic mapping of cAMP receptor protein (CRPMt) in Mycobacterium tuberculosis: relation to transcriptional start sites and the role of CRPMt as a transcription factor. Nucleic Acids Res 42: 8320-8329.
    • (2014) Nucleic Acids Res , vol.42 , pp. 8320-8329
    • Kahramanoglou, C.1    Cortes, T.2    Matange, N.3    Hunt, D.M.4    Visweswariah, S.S.5
  • 49
    • 0029996734 scopus 로고    scopus 로고
    • Compensatory ahpC gene expression in isoniazid-resistant Mycobacterium tuberculosis
    • Sherman DR, Mdluli K, Hickey MJ, Arain TM, Morris SL, et al. (1996) Compensatory ahpC gene expression in isoniazid-resistant Mycobacterium tuberculosis. Science 272: 1641-1643.
    • (1996) Science , vol.272 , pp. 1641-1643
    • Sherman, D.R.1    Mdluli, K.2    Hickey, M.J.3    Arain, T.M.4    Morris, S.L.5
  • 51
    • 2942538880 scopus 로고    scopus 로고
    • Role of KatG catalase-peroxidase in mycobacterial pathogenesis: Countering the phagocyte oxidative burst
    • Ng VH, Cox JS, Sousa AO, MacMicking JD, McKinney JD (2004) Role of KatG catalase-peroxidase in mycobacterial pathogenesis: countering the phagocyte oxidative burst. Mol Microbiol 52: 1291-1302.
    • (2004) Mol Microbiol , vol.52 , pp. 1291-1302
    • Ng, V.H.1    Cox, J.S.2    Sousa, A.O.3    Macmicking, J.D.4    McKinney, J.D.5
  • 52
    • 0035164513 scopus 로고    scopus 로고
    • Transcriptional regulation of furA and katG upon oxidative stress in Mycobacterium smegmatis
    • Milano A, Forti F, Sala C, Riccardi G, Ghisotti D (2001) Transcriptional regulation of furA and katG upon oxidative stress in Mycobacterium smegmatis. J Bacteriol 183: 6801-6806.
    • (2001) J Bacteriol , vol.183 , pp. 6801-6806
    • Milano, A.1    Forti, F.2    Sala, C.3    Riccardi, G.4    Ghisotti, D.5
  • 53
    • 0035100597 scopus 로고    scopus 로고
    • Mycobacterial FurA is a negative regulator of catalase-peroxidase gene katG
    • Zahrt TC, Song J, Siple J, Deretic V (2001) Mycobacterial FurA is a negative regulator of catalase-peroxidase gene katG. Mol Microbiol 39: 1174-1185.
    • (2001) Mol Microbiol , vol.39 , pp. 1174-1185
    • Zahrt, T.C.1    Song, J.2    Siple, J.3    Deretic, V.4
  • 54
    • 0037168511 scopus 로고    scopus 로고
    • Direct inhibition by nitric oxide of the transcriptional ferric uptake regulation protein via nitrosylation of the iron
    • D'Autreaux B, Touati D, Bersch B, Latour JM, Michaud-Soret I (2002) Direct inhibition by nitric oxide of the transcriptional ferric uptake regulation protein via nitrosylation of the iron. Proc Natl Acad Sci U S A 99: 16619-16624.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 16619-16624
    • D'autreaux, B.1    Touati, D.2    Bersch, B.3    Latour, J.M.4    Michaud-Soret, I.5
  • 55
    • 34247472147 scopus 로고    scopus 로고
    • Submicromolar hydrogen peroxide disrupts the ability of fur protein to control free-iron levels in Escherichia coli
    • Varghese S, Wu A, Park S, Imlay KR, Imlay JA (2007) Submicromolar hydrogen peroxide disrupts the ability of Fur protein to control free-iron levels in Escherichia coli. Mol Microbiol 64: 822-830.
    • (2007) Mol Microbiol , vol.64 , pp. 822-830
    • Varghese, S.1    Wu, A.2    Park, S.3    Imlay, K.R.4    Imlay, J.A.5
  • 57
    • 84905454398 scopus 로고    scopus 로고
    • Hypoxia-activated cytochrome bd expression in Mycobacterium smegmatis is cyclic AMP receptor protein dependent
    • Aung HL, Berney M, Cook GM (2014) Hypoxia-activated cytochrome bd expression in Mycobacterium smegmatis is cyclic AMP receptor protein dependent. J Bacteriol 196: 3091-3097.
    • (2014) J Bacteriol , vol.196 , pp. 3091-3097
    • Aung, H.L.1    Berney, M.2    Cook, G.M.3
  • 58
    • 0344321893 scopus 로고    scopus 로고
    • Architecture of a protein central to iron homeostasis: Crystal structure and spectroscopic analysis of the ferric uptake regulator
    • Pohl E, Haller JC, Mijovilovich A, Meyer-Klaucke W, Garman E, et al. (2003) Architecture of a protein central to iron homeostasis: crystal structure and spectroscopic analysis of the ferric uptake regulator. Mol Microbiol 47: 903-915.
    • (2003) Mol Microbiol , vol.47 , pp. 903-915
    • Pohl, E.1    Haller, J.C.2    Mijovilovich, A.3    Meyer-Klaucke, W.4    Garman, E.5
  • 59
    • 0002768724 scopus 로고
    • New subcloning efficiency. Competent cells:.16106 transformants/ mg
    • Jessee J (1986) New subcloning efficiency. Competent cells:.16106 transformants/ mg. Focus 8: 9.
    • (1986) Focus , vol.8 , pp. 9
    • Jessee, J.1
  • 60
    • 0042532056 scopus 로고    scopus 로고
    • Identification of a regulated alkaline phosphatase, a cell surface-associated lipoprotein, in Mycobacterium smegmatis
    • Kriakov J, Lee S, Jacobs WR Jr (2003) Identification of a regulated alkaline phosphatase, a cell surface-associated lipoprotein, in Mycobacterium smegmatis. J Bacteriol 185: 4983-4991.
    • (2003) J Bacteriol , vol.185 , pp. 4983-4991
    • Kriakov, J.1    Lee, S.2    Jacobs, W.R.J.R.3
  • 61
    • 84886802465 scopus 로고    scopus 로고
    • Development of new vector systems as genetic tools applicable to mycobacteria
    • Jeong JA, Lee HN, Ko IJ, Oh JI (2013) Development of new vector systems as genetic tools applicable to mycobacteria. Journal of Life Science 23: 290-298.
    • (2013) Journal of Life Science , vol.23 , pp. 290-298
    • Jeong, J.A.1    Lee, H.N.2    Ko, I.J.3    Oh, J.I.4
  • 62
    • 37449032052 scopus 로고    scopus 로고
    • Identification of the dehydratase component of the mycobacterial mycolic acid-synthesizing fatty acid synthase-II complex
    • Brown AK, Bhatt A, Singh A, Saparia E, Evans AF, et al. (2007) Identification of the dehydratase component of the mycobacterial mycolic acid-synthesizing fatty acid synthase-II complex. Microbiology 153: 4166-4173.
    • (2007) Microbiology , vol.153 , pp. 4166-4173
    • Brown, A.K.1    Bhatt, A.2    Singh, A.3    Saparia, E.4    Evans, A.F.5
  • 64
    • 77955293228 scopus 로고    scopus 로고
    • Identification of trans-and cis-control elements involved in regulation of the carbon monoxide dehydrogenase genes in Mycobacterium sp. Strain JC1 DSM 3803
    • Oh JI, Park SJ, Shin SJ, Ko IJ, Han SJ, et al. (2010) Identification of trans-and cis-control elements involved in regulation of the carbon monoxide dehydrogenase genes in Mycobacterium sp. strain JC1 DSM 3803. J Bacteriol 192: 3925-3933.
    • (2010) J Bacteriol , vol.192 , pp. 3925-3933
    • Oh, J.I.1    Park, S.J.2    Shin, S.J.3    Ko, I.J.4    Han, S.J.5
  • 65
    • 23044488472 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis serine/threonine kinases PknA and PknB: Substrate identification and regulation of cell shape
    • Kang CM, Abbott DW, Park ST, Dascher CC, Cantley LC, et al. (2005) The Mycobacterium tuberculosis serine/threonine kinases PknA and PknB: substrate identification and regulation of cell shape. Genes Dev 19: 1692-1704.
    • (2005) Genes Dev , vol.19 , pp. 1692-1704
    • Kang, C.M.1    Abbott, D.W.2    Park, S.T.3    Dascher, C.C.4    Cantley, L.C.5
  • 66
    • 84896502723 scopus 로고    scopus 로고
    • Expression of a subset of heat stress induced genes of Mycobacterium tuberculosis is regulated by 39,59-cyclic AMP
    • Choudhary E, Bishai W, Agarwal N (2014) Expression of a subset of heat stress induced genes of Mycobacterium tuberculosis is regulated by 39,59-cyclic AMP. PLoS ONE 9: e89759.
    • (2014) PLoS ONE , vol.9 , pp. e89759
    • Choudhary, E.1    Bishai, W.2    Agarwal, N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.