메뉴 건너뛰기




Volumn 53, Issue 2, 2004, Pages 555-572

DNA-binding specificity of AdpA, a transcriptional activator in the A-factor regulatory cascade in Streptomyces griseus

Author keywords

[No Author keywords available]

Indexed keywords

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DIMERIZATION; DNA BINDING; GENE CONTROL; GENE SEQUENCE; GENE TARGETING; GENETIC VARIABILITY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; STREPTOMYCES GRISEUS; TRANSCRIPTION INITIATION;

EID: 3242891579     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2004.04153.x     Document Type: Article
Times cited : (91)

References (63)
  • 1
    • 0034035345 scopus 로고    scopus 로고
    • Transcription activation at the Escherichia coli melAB promoter: The role of MelR and the cyclic AMP receptor protein
    • Belyaeva, T.A., Wade, J.T., Webster, C.L., Howard, V.J., Thomas, M.S., Hyde, E.I., and Busby, S.J.W. (2000) Transcription activation at the Escherichia coli melAB promoter: the role of MelR and the cyclic AMP receptor protein. Mol Microbiol 36: 211-222.
    • (2000) Mol Microbiol , vol.36 , pp. 211-222
    • Belyaeva, T.A.1    Wade, J.T.2    Webster, C.L.3    Howard, V.J.4    Thomas, M.S.5    Hyde, E.I.6    Busby, S.J.W.7
  • 3
    • 0027078718 scopus 로고
    • In vitro evolution of intrinsically bent DNA
    • Beutel, B.A., and Gold, L. (1992) In vitro evolution of intrinsically bent DNA. J Mol Biol 228: 803-812.
    • (1992) J Mol Biol , vol.228 , pp. 803-812
    • Beutel, B.A.1    Gold, L.2
  • 4
    • 0033885504 scopus 로고    scopus 로고
    • BldN, an extracytoplasmic function RNA polymerase sigma factor required for aerial mycelium formation in Streptomyces coelicolor A3(2)
    • BldN, an extracytoplasmic function RNA polymerase sigma factor required for aerial mycelium formation in Streptomyces coelicolor A3(2). J Bacteriol 182: 4606-4616.
    • (2000) J Bacteriol , vol.182 , pp. 4606-4616
    • Bibb, M.J.1    Molle, V.2    Buttner, M.J.3
  • 5
    • 0037428241 scopus 로고    scopus 로고
    • Mutations in the DJ-1 gene associated with autosomal recessive early-onset Parkinsonism
    • Bonifati, V., Rizzu, P., van Baren, M.J., Schaap, O., Breedveld, G.J., Krieger, E., et al. (2003) Mutations in the DJ-1 gene associated with autosomal recessive early-onset Parkinsonism. Science 299: 256-259.
    • (2003) Science , vol.299 , pp. 256-259
    • Bonifati, V.1    Rizzu, P.2    Van Baren, M.J.3    Schaap, O.4    Breedveld, G.J.5    Krieger, E.6
  • 6
    • 0030786451 scopus 로고    scopus 로고
    • DNA binding and DNA bending by the MelR transcription activator protein from Escherichia coli
    • Bourgerie, S.J., Michán, C.M., Thomas, M.S., Busby, S.J.W., and Hyde, E.I. (1997) DNA binding and DNA bending by the MelR transcription activator protein from Escherichia coli. Nucleic Acids Res 25: 1685-1693.
    • (1997) Nucleic Acids Res , vol.25 , pp. 1685-1693
    • Bourgerie, S.J.1    Michán, C.M.2    Thomas, M.S.3    Busby, S.J.W.4    Hyde, E.I.5
  • 7
    • 0023425411 scopus 로고
    • Missing contact probing of DNA-protein interactions
    • Brunelle, A., and Schleif, R.F. (1987) Missing contact probing of DNA-protein interactions. Proc Natl Acad Sci USA 84: 6673-6676.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 6673-6676
    • Brunelle, A.1    Schleif, R.F.2
  • 8
    • 0024357841 scopus 로고
    • Determining residue-base interactions between AraC protein and aral DNA
    • Brunelle, A., and Schleif, R. (1989) Determining residue-base interactions between AraC protein and aral DNA. J Mol Biol 209: 607-622.
    • (1989) J Mol Biol , vol.209 , pp. 607-622
    • Brunelle, A.1    Schleif, R.2
  • 9
    • 0027463760 scopus 로고
    • Variation of half-site organization and DNA looping by AraC protein
    • Carra, J.H., and Schleif, R.F. (1993) Variation of half-site organization and DNA looping by AraC protein. EMBO J 12: 35-44.
    • (1993) EMBO J , vol.12 , pp. 35-44
    • Carra, J.H.1    Schleif, R.F.2
  • 10
    • 0033145727 scopus 로고    scopus 로고
    • A subfamily of MalT-related ATP-dependent regulators in the LuxR family
    • De Schrijver, A., and De Mot, R. (1999) A subfamily of MalT-related ATP-dependent regulators in the LuxR family. Microbiology 145: 1287-1288.
    • (1999) Microbiology , vol.145 , pp. 1287-1288
    • De Schrijver, A.1    De Mot, R.2
  • 11
    • 0027176389 scopus 로고
    • Uracil-DNA glycosylase as a probe for protein-DNA interactions
    • Devchand, P.R., McGhee, J.D., and van de Sande, J.H. (1993) Uracil-DNA glycosylase as a probe for protein-DNA interactions. Nucleic Acids Res 21: 3437-3443.
    • (1993) Nucleic Acids Res , vol.21 , pp. 3437-3443
    • Devchand, P.R.1    McGhee, J.D.2    Van De Sande, J.H.3
  • 12
    • 0034687746 scopus 로고    scopus 로고
    • Crystal structure of an intracellular protease from Pyrococcus horikoshii at 2-Å resolution
    • Du, X., Choi, I.-G., Kim, R., Wang, W., Jancarik, J., Yokola. H., and Kim, S.-H. (2000) Crystal structure of an intracellular protease from Pyrococcus horikoshii at 2-Å resolution. Proc Natl Acad Sci USA 97: 14079-14084.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 14079-14084
    • Du, X.1    Choi, I.-G.2    Kim, R.3    Wang, W.4    Jancarik, J.5    Yokola, H.6    Kim, S.-H.7
  • 13
    • 0028173180 scopus 로고
    • DNA-dependent renaturation of an insoluble DNA binding protein. Identification of the RhaS binding site at rhaBAD
    • Egan, S.M., and Schleif, R.F. (1994) DNA-dependent renaturation of an insoluble DNA binding protein. Identification of the RhaS binding site at rhaBAD. J Mol Biol 243: 821-829.
    • (1994) J Mol Biol , vol.243 , pp. 821-829
    • Egan, S.M.1    Schleif, R.F.2
  • 16
    • 0343330922 scopus 로고    scopus 로고
    • Critical nucleotides in the upstream region of the XylS-dependent TOL meta-cleavage pathway operon promoter as deduced from analysis of mutants
    • González-Pérez, M.M., Ramos, J.L., Gallegos, M.-T., and Marqués, S. (1999) Critical nucleotides in the upstream region of the XylS-dependent TOL meta-cleavage pathway operon promoter as deduced from analysis of mutants. J Biol Chem 274: 2286-2290.
    • (1999) J Biol Chem , vol.274 , pp. 2286-2290
    • González-Pérez, M.M.1    Ramos, J.L.2    Gallegos, M.-T.3    Marqués, S.4
  • 17
    • 0034968749 scopus 로고    scopus 로고
    • Systematic mutagenesis of the DNA binding sites for SoxS in the Escherichia coli zwf and fpr promoters: Identifying nucleotides required for DNA binding and transcription activation
    • Griffith, K.L., and Wolf, R.E., Jr (2001) Systematic mutagenesis of the DNA binding sites for SoxS in the Escherichia coli zwf and fpr promoters: identifying nucleotides required for DNA binding and transcription activation. Mol Microbiol 40: 1141-1154.
    • (2001) Mol Microbiol , vol.40 , pp. 1141-1154
    • Griffith, K.L.1    Wolf Jr., R.E.2
  • 18
    • 0029864566 scopus 로고    scopus 로고
    • Sequence, expression in Escherichia coli, and analysis of the gene encoding a novel intracellular protease (Pfpl) from the hyperthermophilic archaeon Pyrococcus furiosus
    • Halio, S.B., Blumentals, I.I., Short, S.A., Merrill, B.M., and Kelly, R.M. (1996) Sequence, expression in Escherichia coli, and analysis of the gene encoding a novel intracellular protease (Pfpl) from the hyperthermophilic archaeon Pyrococcus furiosus. J Bacteriol 178: 2605-2612.
    • (1996) J Bacteriol , vol.178 , pp. 2605-2612
    • Halio, S.B.1    Blumentals, I.I.2    Short, S.A.3    Merrill, B.M.4    Kelly, R.M.5
  • 19
    • 0033103726 scopus 로고    scopus 로고
    • Identification and characterization of a novel protein that regulates RNA-protein interaction
    • Hod, Y., Pentyala, S.N., Whyard, T.C., and El-Maghrabi, M.R. (1999) Identification and characterization of a novel protein that regulates RNA-protein interaction. J Cell Biochem 72: 435-444.
    • (1999) J Cell Biochem , vol.72 , pp. 435-444
    • Hod, Y.1    Pentyala, S.N.2    Whyard, T.C.3    El-Maghrabi, M.R.4
  • 21
    • 0036778196 scopus 로고    scopus 로고
    • A microbial hormone, A-factor, as a master switch for morphological differentiation and secondary metabolism in Streptomyces griseus
    • Horinouchi, S. (2002) A microbial hormone, A-factor, as a master switch for morphological differentiation and secondary metabolism in Streptomyces griseus. Front Biosci 7: d2045-d2057.
    • (2002) Front Biosci , vol.7
    • Horinouchi, S.1
  • 22
    • 0028245937 scopus 로고
    • A-factor as a microbial hormone that controls cellular differentiation and secondary metabolism in Streptomyces griseus
    • Horinouchi, S., and Beppu, T. (1994) A-factor as a microbial hormone that controls cellular differentiation and secondary metabolism in Streptomyces griseus. Mol Microbiol 12: 859-864.
    • (1994) Mol Microbiol , vol.12 , pp. 859-864
    • Horinouchi, S.1    Beppu, T.2
  • 23
    • 0002277528 scopus 로고    scopus 로고
    • Isolation of DNA fragments bound by transcriptional factors, AdpA and ArpA, in the A-factor regulatory cascade
    • Horinouchi, S., Onaka, H., Yamazaki, H., Kameyama, S., and Ohnishi, Y. (2000) Isolation of DNA fragments bound by transcriptional factors, AdpA and ArpA, in the A-factor regulatory cascade. Actinomycetologica 14: 37-42.
    • (2000) Actinomycetologica , vol.14 , pp. 37-42
    • Horinouchi, S.1    Onaka, H.2    Yamazaki, H.3    Kameyama, S.4    Ohnishi, Y.5
  • 24
    • 0035254935 scopus 로고    scopus 로고
    • The C-terminal domain of HPII catalase is a member of the type I glutamine amidotransferase superfamily
    • Horvath, M.M., and Grishin, N.V. (2001) The C-terminal domain of HPII catalase is a member of the type I glutamine amidotransferase superfamily. Proteins 42: 230-236.
    • (2001) Proteins , vol.42 , pp. 230-236
    • Horvath, M.M.1    Grishin, N.V.2
  • 25
    • 0027410919 scopus 로고
    • Transposon mutagenesis by Tn4560 and applications with avermectin-producing Streptomyces avermitilis
    • Ikeda, H., Takada, Y., Pang, C.H., Tanaka, H., and Omura, S. (1993) Transposon mutagenesis by Tn4560 and applications with avermectin-producing Streptomyces avermitilis. J Bacteriol 175: 2077-2082,
    • (1993) J Bacteriol , vol.175 , pp. 2077-2082
    • Ikeda, H.1    Takada, Y.2    Pang, C.H.3    Tanaka, H.4    Omura, S.5
  • 26
    • 0033578297 scopus 로고    scopus 로고
    • Organization of the biosynthetic gene cluster for the polyketide anthelmintic macrolide avermectin in Streptomyces avermitilis
    • Ikeda, H., Nonomiya, T., Usami, M., Ohta, T., and Omura, S. (1999) Organization of the biosynthetic gene cluster for the polyketide anthelmintic macrolide avermectin in Streptomyces avermitilis. Proc Natl Acad Sci USA 96: 9509-9514.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9509-9514
    • Ikeda, H.1    Nonomiya, T.2    Usami, M.3    Ohta, T.4    Omura, S.5
  • 27
    • 0038561132 scopus 로고    scopus 로고
    • Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis
    • Ikeda, H., Ishikawa, J., Hanamoto, A., Shinose, M., Kikuchi, H., Shiba, T., et al. (2003) Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis. Nature Biotechnol 21: 526-531.
    • (2003) Nature Biotechnol , vol.21 , pp. 526-531
    • Ikeda, H.1    Ishikawa, J.2    Hanamoto, A.3    Shinose, M.4    Kikuchi, H.5    Shiba, T.6
  • 28
    • 0032942468 scopus 로고    scopus 로고
    • FramePlot: A new implementation of the frame analysis for predicting protein-coding regions in bacterial DNA with a high G+C content
    • Ishikawa, J., and Hotta, K. (1999) FramePlot: a new implementation of the frame analysis for predicting protein-coding regions in bacterial DNA with a high G+C content. FEMS Microbiol Lett 174: 251-253.
    • (1999) FEMS Microbiol Lett , vol.174 , pp. 251-253
    • Ishikawa, J.1    Hotta, K.2
  • 29
    • 0034098739 scopus 로고    scopus 로고
    • Cooperative action of the catabolite activator protein and AraC in vitro at the araFGH promoter
    • Johnson, C.M., and Schleif, R.F. (2000) Cooperative action of the catabolite activator protein and AraC in vitro at the araFGH promoter. J Bacteriol 182: 1995-2000.
    • (2000) J Bacteriol , vol.182 , pp. 1995-2000
    • Johnson, C.M.1    Schleif, R.F.2
  • 30
    • 0036837749 scopus 로고    scopus 로고
    • Control by A-factor of a metalloendopeptidase gene involved in aerial mycelium formation in Streptomyces griseus
    • Kato, J., Suzuki, A., Yamazaki, H., Ohnishi, Y., and Horinouchi, S. (2002) Control by A-factor of a metalloendopeptidase gene involved in aerial mycelium formation in Streptomyces griseus. J Bacteriol 184: 6016-6025.
    • (2002) J Bacteriol , vol.184 , pp. 6016-6025
    • Kato, J.1    Suzuki, A.2    Yamazaki, H.3    Ohnishi, Y.4    Horinouchi, S.5
  • 31
    • 0031968766 scopus 로고    scopus 로고
    • Developmental regulation of transcription of whiE, a locus specifying the polyketide spore pigment in Streptomyces coelicolor A3(2)
    • Kelemen, G.H., Brian, P., Flärdh, K., Chamberlin, L., Chater, K.F., and Buttner, M.J. (1998) Developmental regulation of transcription of whiE, a locus specifying the polyketide spore pigment in Streptomyces coelicolor A3(2). J Bacteriol 180: 2515-2521.
    • (1998) J Bacteriol , vol.180 , pp. 2515-2521
    • Kelemen, G.H.1    Brian, P.2    Flärdh, K.3    Chamberlin, L.4    Chater, K.F.5    Buttner, M.J.6
  • 32
    • 0001759947 scopus 로고    scopus 로고
    • Crystal structure of the Escherichia coli Rob transcription factor in complex with DNA
    • Kwon, H.J., Bennik, M.H.J., Demple, B., and Ellenberger, T. (2000) Crystal structure of the Escherichia coli Rob transcription factor in complex with DNA. Nature Struct Biol 7: 424-430.
    • (2000) Nature Struct Biol , vol.7 , pp. 424-430
    • Kwon, H.J.1    Bennik, M.H.J.2    Demple, B.3    Ellenberger, T.4
  • 33
    • 0242497815 scopus 로고    scopus 로고
    • Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain
    • Lee, S.-J., Kim, S.J., Kim, I.-K., Ko, J., Jeong, C.-S., Kim, G.-H., et al. (2003) Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain. J Biol Chem 278: 44552-44559.
    • (2003) J Biol Chem , vol.278 , pp. 44552-44559
    • Lee, S.-J.1    Kim, S.J.2    Kim, I.-K.3    Ko, J.4    Jeong, C.-S.5    Kim, G.-H.6
  • 34
    • 0029951890 scopus 로고    scopus 로고
    • Sequence specificity for DNA binding by Escherichia coli SoxS and Rob proteins
    • Li, Z., and Demple, B. (1996) Sequence specificity for DNA binding by Escherichia coli SoxS and Rob proteins. Mol Microbiol 20: 937-945.
    • (1996) Mol Microbiol , vol.20 , pp. 937-945
    • Li, Z.1    Demple, B.2
  • 36
    • 0035067086 scopus 로고    scopus 로고
    • The AraC transcriptional activators
    • Martin, R.G., and Rosner, J.L. (2001) The AraC transcriptional activators. Curr Opin Microbiol 4: 132-137.
    • (2001) Curr Opin Microbiol , vol.4 , pp. 132-137
    • Martin, R.G.1    Rosner, J.L.2
  • 37
    • 0032746803 scopus 로고    scopus 로고
    • Structural requirements for marbox function in transcriptional activation of mar/sox/rob regulon promoters in Escherichia coli: Sequence, orientation and spatial relationship to the core promoter
    • Martin, R.G., Gillette, W.K., Rhee, S., and Rosner, J.L. (1999) Structural requirements for marbox function in transcriptional activation of mar/sox/rob regulon promoters in Escherichia coli: sequence, orientation and spatial relationship to the core promoter. Mol Microbiol 34: 431-441.
    • (1999) Mol Microbiol , vol.34 , pp. 431-441
    • Martin, R.G.1    Gillette, W.K.2    Rhee, S.3    Rosner, J.L.4
  • 38
    • 0018846636 scopus 로고
    • Sequencing end-labeled DNA with base-specific chemical cleavages
    • Maxam, A.M., and Gilbert, W. (1980) Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol 65: 499-560.
    • (1980) Methods Enzymol , vol.65 , pp. 499-560
    • Maxam, A.M.1    Gilbert, W.2
  • 39
    • 0032992583 scopus 로고    scopus 로고
    • Cloning and characterization of the thiD/J gene of Escherichia coli encoding a thiamin-synthesizing bifunctional enzyme, hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase
    • Mizote, T., Tsuda, M., Smith, D.D.S., Nakayama, H., and Nakazawa, T. (1999) Cloning and characterization of the thiD/J gene of Escherichia coli encoding a thiamin-synthesizing bifunctional enzyme, hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase. Microbiology 145: 495-501.
    • (1999) Microbiology , vol.145 , pp. 495-501
    • Mizote, T.1    Tsuda, M.2    Smith, D.D.S.3    Nakayama, H.4    Nakazawa, T.5
  • 40
    • 0033923860 scopus 로고    scopus 로고
    • Rns, a virulence regulator within the AraC family, requires binding sites upstream and downstream of its own promoter to function as an activator
    • Munson, G.P., and Scott, J.R. (2000) Rns, a virulence regulator within the AraC family, requires binding sites upstream and downstream of its own promoter to function as an activator. Mol Microbiol 36: 1391-1402.
    • (2000) Mol Microbiol , vol.36 , pp. 1391-1402
    • Munson, G.P.1    Scott, J.R.2
  • 42
    • 0345529055 scopus 로고    scopus 로고
    • Colonial differentiation in Streptomyces coelicolor depends on translation of a specific codon within the adpA gene
    • Nguyen, K.T., Tenor, J., Stettler, H., Nguyen, L.T., Nguyen, L.D., and Thompson, C.J. (2003) Colonial differentiation in Streptomyces coelicolor depends on translation of a specific codon within the adpA gene. J Bacteriol 185: 7291-7296.
    • (2003) J Bacteriol , vol.185 , pp. 7291-7296
    • Nguyen, K.T.1    Tenor, J.2    Stettler, H.3    Nguyen, L.T.4    Nguyen, L.D.5    Thompson, C.J.6
  • 43
    • 0030582731 scopus 로고    scopus 로고
    • How AraC interacts specifically with its target DNAs
    • Niland, P., Hühne, R., and Müller-Hill, B. (1996) How AraC interacts specifically with its target DNAs. J Mol Biol 264: 667-674.
    • (1996) J Mol Biol , vol.264 , pp. 667-674
    • Niland, P.1    Hühne, R.2    Müller-Hill, B.3
  • 44
    • 0032847109 scopus 로고    scopus 로고
    • The A-factor regulatory cascade leading to streptomycin biosynthesis in Streptomyces griseus: Identification of a target gene of the A-factor receptor
    • Ohnishi, Y., Kameyama, S., Onaka, H., and Horinouchi, S. (1999) The A-factor regulatory cascade leading to streptomycin biosynthesis in Streptomyces griseus: identification of a target gene of the A-factor receptor. Mol Microbiol 34: 102-111.
    • (1999) Mol Microbiol , vol.34 , pp. 102-111
    • Ohnishi, Y.1    Kameyama, S.2    Onaka, H.3    Horinouchi, S.4
  • 47
    • 0030836620 scopus 로고    scopus 로고
    • DNA-binding activity of the A-factor receptor protein and its recognition sequences
    • Onaka, H., and Horinouchi, S. (1997) DNA-binding activity of the A-factor receptor protein and its recognition sequences. Mol Microbiol 24: 991-1000.
    • (1997) Mol Microbiol , vol.24 , pp. 991-1000
    • Onaka, H.1    Horinouchi, S.2
  • 48
    • 0026603423 scopus 로고
    • Uracil interference, a rapid and general method for defining protein-DNA interactions involving the 5-methyl group of thymines: The GCN4-DNA complex
    • Pu, W.T., and Struhl, K. (1992) Uracil interference, a rapid and general method for defining protein-DNA interactions involving the 5-methyl group of thymines: the GCN4-DNA complex. Nucleic Acids Res 20: 771-775.
    • (1992) Nucleic Acids Res , vol.20 , pp. 771-775
    • Pu, W.T.1    Struhl, K.2
  • 49
    • 0037453026 scopus 로고    scopus 로고
    • The 1.6-Å crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad
    • Quigley, P.M., Korotkov, K., Baneyx, F., and Hol, W.G.J. (2003) The 1.6-Å crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad. Proc Natl Acad Sci USA 100: 3137-3142.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 3137-3142
    • Quigley, P.M.1    Korotkov, K.2    Baneyx, F.3    Hol, W.G.J.4
  • 50
    • 0032169864 scopus 로고    scopus 로고
    • A novel DNA-binding motif in MarA: The first structure for an AraC family transcriptional activator
    • Rhee, S., Martin, R.G., Rosner, J.L., and Davies, D.R. (1998) A novel DNA-binding motif in MarA: the first structure for an AraC family transcriptional activator. Proc Natl Acad Sci USA 95: 10413-10418.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 10413-10418
    • Rhee, S.1    Martin, R.G.2    Rosner, J.L.3    Davies, D.R.4
  • 51
    • 0035281992 scopus 로고    scopus 로고
    • Fine structure of E. coli RNA polymerase-promoter interactions: A subunit binding to the UP element minor groove
    • Ross, W., Ernst, A., and Gourse, R.L. (2001) Fine structure of E. coli RNA polymerase-promoter interactions: a subunit binding to the UP element minor groove. Genes Dev 15: 491-506.
    • (2001) Genes Dev , vol.15 , pp. 491-506
    • Ross, W.1    Ernst, A.2    Gourse, R.L.3
  • 52
    • 0037337551 scopus 로고    scopus 로고
    • AraC protein: A love-hate relationship
    • Schleif, R. (2003) AraC protein: a love-hate relationship. Bioessays 25: 274-282.
    • (2003) Bioessays , vol.25 , pp. 274-282
    • Schleif, R.1
  • 54
    • 0040754730 scopus 로고    scopus 로고
    • Expression of the gap gene encoding glyceraldehyde-3-phosphate dehydrogenase of Streptomyces aureofaciens requires GapR, a member of the AraC/XylS family of transcriptional activators
    • Sprušanský, O., Řežuchová, B., Homerová, D., and Kormanec, J. (2001) Expression of the gap gene encoding glyceraldehyde-3-phosphate dehydrogenase of Streptomyces aureofaciens requires GapR, a member of the AraC/XylS family of transcriptional activators. Microbiology 147: 1291-1301.
    • (2001) Microbiology , vol.147 , pp. 1291-1301
    • Sprušanský, O.1    Řežuchová, B.2    Homerová, D.3    Kormanec, J.4
  • 55
    • 0142125295 scopus 로고    scopus 로고
    • A rare leucine codon in adpA is implicated in the morphological defect of bldA mutants of Streptomyces coelicolor
    • Takano, E., Tao, M., Long, F., Bibb, M.J., Wang, L., Li, W., et al. (2003) A rare leucine codon in adpA is implicated in the morphological defect of bldA mutants of Streptomyces coelicolor. Mol Microbiol 50: 475-486.
    • (2003) Mol Microbiol , vol.50 , pp. 475-486
    • Takano, E.1    Tao, M.2    Long, F.3    Bibb, M.J.4    Wang, L.5    Li, W.6
  • 56
    • 0042232039 scopus 로고    scopus 로고
    • Crystal structure of human DJ-1, a protein associated with early onset Parkinson's disease
    • Tao, X., and Tong, L. (2003) Crystal structure of human DJ-1, a protein associated with early onset Parkinson's disease. J Biol Chem 278: 31372-31379.
    • (2003) J Biol Chem , vol.278 , pp. 31372-31379
    • Tao, X.1    Tong, L.2
  • 57
    • 0032568948 scopus 로고    scopus 로고
    • Thiamin biosynthesis in Escherichia coli. Identification of this thiocarboxylate as the immediate sulfur donor in the thiazole formation
    • Taylor, S.V., Kelleher, N.L., Kinsland, C., Chiu, H.-J., Costello, C.A., Backstrom, A.D., et al. (1998) Thiamin biosynthesis in Escherichia coli. Identification of this thiocarboxylate as the immediate sulfur donor in the thiazole formation. J Biol Chem 273: 16555-16560.
    • (1998) J Biol Chem , vol.273 , pp. 16555-16560
    • Taylor, S.V.1    Kelleher, N.L.2    Kinsland, C.3    Chiu, H.-J.4    Costello, C.A.5    Backstrom, A.D.6
  • 58
    • 0036083835 scopus 로고    scopus 로고
    • AraC-XylS database: A family of positive transcriptional regulators in bacteria
    • Tobes, R., and Ramos, J.L. (2002) AraC-XylS database: a family of positive transcriptional regulators in bacteria. Nucleic Acids Res 30: 318-321.
    • (2002) Nucleic Acids Res , vol.30 , pp. 318-321
    • Tobes, R.1    Ramos, J.L.2
  • 59
    • 0035031304 scopus 로고    scopus 로고
    • Characterization and analysis of the PikD regulatory factor in the pikromycin biosynthetic pathway of Streptomyces venezuelae
    • Wilson, D.J., Xue, Y., Reynolds, K.A., and Sherman, D.H. (2001) Characterization and analysis of the PikD regulatory factor in the pikromycin biosynthetic pathway of Streptomyces venezuelae. J Bacteriol 183: 3468-3475.
    • (2001) J Bacteriol , vol.183 , pp. 3468-3475
    • Wilson, D.J.1    Xue, Y.2    Reynolds, K.A.3    Sherman, D.H.4
  • 60
    • 0033877257 scopus 로고    scopus 로고
    • AdsA) that is essential for morphological development in Streptomyces griseus
    • AdsA) that is essential for morphological development in Streptomyces griseus. J Bacteriol 182: 4596-4605.
    • (2000) J Bacteriol , vol.182 , pp. 4596-4605
    • Yamazaki, H.1    Ohnishi, Y.2    Horinouchi, S.3
  • 61
    • 0037317582 scopus 로고    scopus 로고
    • Transcriptional switch on of ssgA by A-factor, which is essential for spore septum formation in Streptomyces griseus
    • Yamazaki, H., Ohnishi, Y., and Horinouchi, S. (2003a) Transcriptional switch on of ssgA by A-factor, which is essential for spore septum formation in Streptomyces griseus. J Bacteriol 185: 1273-1283.
    • (2003) J Bacteriol , vol.185 , pp. 1273-1283
    • Yamazaki, H.1    Ohnishi, Y.2    Horinouchi, S.3
  • 62
    • 0344395007 scopus 로고    scopus 로고
    • amfR, an essential gene for aerial mycelium formation, is a member of the AdpA regulon in the A-factor regulatory cascade in Streptomyces griseus
    • Yamazaki, H., Takano, Y., Ohnishi, Y., and Horinouchi, S. (2003b) amfR, an essential gene for aerial mycelium formation, is a member of the AdpA regulon in the A-factor regulatory cascade in Streptomyces griseus. Mol Microbiol 50: 1173-1187.
    • (2003) Mol Microbiol , vol.50 , pp. 1173-1187
    • Yamazaki, H.1    Takano, Y.2    Ohnishi, Y.3    Horinouchi, S.4
  • 63
    • 0029928896 scopus 로고    scopus 로고
    • Transcription activation parameters at ara pBAD
    • Zhang, X., Reeder, T., and Schleif, R. (1996) Transcription activation parameters at ara pBAD. J Mol Biol 258: 14-24.
    • (1996) J Mol Biol , vol.258 , pp. 14-24
    • Zhang, X.1    Reeder, T.2    Schleif, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.