메뉴 건너뛰기




Volumn 35, Issue 14, 2007, Pages 4755-4766

Probing key DNA contacts in AraR-mediated transcriptional repression of the Bacillus subtilis arabinose regulon

Author keywords

[No Author keywords available]

Indexed keywords

ARABINOSE; CIS ACTING ELEMENT; NUCLEOPROTEIN; PALINDROMIC DNA; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR ARAR; UNCLASSIFIED DRUG;

EID: 34547863494     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkm509     Document Type: Article
Times cited : (16)

References (33)
  • 1
    • 1842364869 scopus 로고    scopus 로고
    • The Bacillus subtilis L-arabinose (ara) operon: Nucleotide sequence, genetic organization and expression
    • Sá-Nogueira,I., Nogueira,T.V., Soares,S. and de Lencastre,H. (1997) The Bacillus subtilis L-arabinose (ara) operon: Nucleotide sequence, genetic organization and expression. Microbiology, 143 (Pt 3), 957-969.
    • (1997) Microbiology , vol.143 , Issue.PART 3 , pp. 957-969
    • Sá-Nogueira, I.1    Nogueira, T.V.2    Soares, S.3    de Lencastre, H.4
  • 2
    • 0030733946 scopus 로고    scopus 로고
    • Cloning, functional analysis, and transcriptional regulation of the Bacillus subtilis araE gene involved in L-arabinose utilization
    • Sá-Nogueira,I. and Ramos,S.S. (1997) Cloning, functional analysis, and transcriptional regulation of the Bacillus subtilis araE gene involved in L-arabinose utilization. J. Bacteriol., 179, 7705-7711.
    • (1997) J. Bacteriol , vol.179 , pp. 7705-7711
    • Sá-Nogueira, I.1    Ramos, S.S.2
  • 3
    • 0031039351 scopus 로고    scopus 로고
    • Negative regulation of L-arabinose metabolism in Bacillus subtilis: Characterization of the araR (araC) gene
    • Sá-Nogueira,I. and Mota,L.J. (1997) Negative regulation of L-arabinose metabolism in Bacillus subtilis: Characterization of the araR (araC) gene. J. Bacteriol., 179, 1598-1608.
    • (1997) J. Bacteriol , vol.179 , pp. 1598-1608
    • Sá-Nogueira, I.1    Mota, L.J.2
  • 4
    • 10744227664 scopus 로고    scopus 로고
    • Transcriptional regulation of genes encoding arabinan-degrading enzymes in Bacillus subtilis
    • Raposo,M.P., Inácio,J.M., Mota,L.J. and de Sá-Nogueira,I. (2004) Transcriptional regulation of genes encoding arabinan-degrading enzymes in Bacillus subtilis. J. Bacteriol., 186, 1287-1296.
    • (2004) J. Bacteriol , vol.186 , pp. 1287-1296
    • Raposo, M.P.1    Inácio, J.M.2    Mota, L.J.3    de Sá-Nogueira, I.4
  • 5
    • 0031780217 scopus 로고    scopus 로고
    • The Bacillus subtilis AraE protein displays a broad substrate specificity for several different sugars
    • Krispin,O. and Allmansberger,R. (1998) The Bacillus subtilis AraE protein displays a broad substrate specificity for several different sugars. J. Bacteriol., 180, 3250-3252.
    • (1998) J. Bacteriol , vol.180 , pp. 3250-3252
    • Krispin, O.1    Allmansberger, R.2
  • 6
    • 0032810168 scopus 로고    scopus 로고
    • Mode of action of AraR, the key regulator of L-arabinose metabolism in Bacillus subtilis
    • Mota,L.J., Tavares,P. and Sá-Nogueira,I. (1999) Mode of action of AraR, the key regulator of L-arabinose metabolism in Bacillus subtilis. Mol. Microbiol., 33, 476-489.
    • (1999) Mol. Microbiol , vol.33 , pp. 476-489
    • Mota, L.J.1    Tavares, P.2    Sá-Nogueira, I.3
  • 7
    • 0034977070 scopus 로고    scopus 로고
    • Control of the arabinose regulon in Bacillus subtilis by AraR in vivo: Crucial roles of operators, cooperativity, and DNA looping
    • Mota,L.J., Sarmento,L.M. and de Sá-Nogueira,I. (2001) Control of the arabinose regulon in Bacillus subtilis by AraR in vivo: Crucial roles of operators, cooperativity, and DNA looping. J. Bacteriol., 183, 4190-4201.
    • (2001) J. Bacteriol , vol.183 , pp. 4190-4201
    • Mota, L.J.1    Sarmento, L.M.2    de Sá-Nogueira, I.3
  • 8
    • 33646003235 scopus 로고    scopus 로고
    • Functional domains of the Bacillus subtilis transcription factor AraR and identification of amino acids important for nucleoprotein complex assembly and effector binding
    • Franco,I.S., Mota,L.J., Soares,C.M. and de Sá-Nogueira,I. (2006) Functional domains of the Bacillus subtilis transcription factor AraR and identification of amino acids important for nucleoprotein complex assembly and effector binding. J. Bacteriol., 188, 3024-3036.
    • (2006) J. Bacteriol , vol.188 , pp. 3024-3036
    • Franco, I.S.1    Mota, L.J.2    Soares, C.M.3    de Sá-Nogueira, I.4
  • 9
    • 0025905579 scopus 로고
    • A new family of bacterial regulatory proteins
    • Haydon,D.J. and Guest,J.R. (1991) A new family of bacterial regulatory proteins. FEMS Microbiol. Lett., 63, 291-295.
    • (1991) FEMS Microbiol. Lett , vol.63 , pp. 291-295
    • Haydon, D.J.1    Guest, J.R.2
  • 10
    • 0026724966 scopus 로고
    • A family of bacterial regulators homologous to Gal and Lac repressors
    • Weickert,M.J. and Adhya,S. (1992) A family of bacterial regulators homologous to Gal and Lac repressors. J. Biol. Chem., 267, 15869-15874.
    • (1992) J. Biol. Chem , vol.267 , pp. 15869-15874
    • Weickert, M.J.1    Adhya, S.2
  • 11
    • 0037066712 scopus 로고    scopus 로고
    • Subdivision of the helix-turn-helix GntR family of bacterial regulators in the FadR, HutC, MocR and YtrA subfamilies
    • Rigali,S., Derouaux,A., Giannotta,F. and Dusart,J. (2002) Subdivision of the helix-turn-helix GntR family of bacterial regulators in the FadR, HutC, MocR and YtrA subfamilies. J. Biol. Chem., 277, 12507-12515.
    • (2002) J. Biol. Chem , vol.277 , pp. 12507-12515
    • Rigali, S.1    Derouaux, A.2    Giannotta, F.3    Dusart, J.4
  • 12
    • 0041313851 scopus 로고    scopus 로고
    • PlmA, a new member of the GntR family, has plasmid maintenance functions in Anabaena sp. strain PCC 7120
    • Lee,M.H., Scherer,M., Rigali,S. and Golden,J.W. (2003) PlmA, a new member of the GntR family, has plasmid maintenance functions in Anabaena sp. strain PCC 7120. J. Bacteriol., 185, 4315-4325.
    • (2003) J. Bacteriol , vol.185 , pp. 4315-4325
    • Lee, M.H.1    Scherer, M.2    Rigali, S.3    Golden, J.W.4
  • 13
  • 14
    • 0027270989 scopus 로고
    • Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5
    • Clark,K.L., Halay,E.D., Lai,E. and Burley,S.K. (1993) Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5. Nature, 364, 412-420.
    • (1993) Nature , vol.364 , pp. 412-420
    • Clark, K.L.1    Halay, E.D.2    Lai, E.3    Burley, S.K.4
  • 16
    • 0036074510 scopus 로고    scopus 로고
    • Protein-DNA interactions: Amino acid conservation and the effects of mutations on binding specificity
    • Luscombe,N.M. and Thornton,J.M. (2002) Protein-DNA interactions: Amino acid conservation and the effects of mutations on binding specificity. J. Mol. Biol., 320, 991-1009.
    • (2002) J. Mol. Biol , vol.320 , pp. 991-1009
    • Luscombe, N.M.1    Thornton, J.M.2
  • 17
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NYC, USA
    • Miller,J. (1972) Experiments in Molecular Genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NYC, USA.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.1
  • 18
    • 0015191725 scopus 로고
    • Characterization of two sucrase activities in Bacillus subtilis Marburg
    • Pascal,M., Kunst,F., Lepesant,J.A. and Dedonder,R. (1971) Characterization of two sucrase activities in Bacillus subtilis Marburg. Biochimie, 53, 1059-1066.
    • (1971) Biochimie , vol.53 , pp. 1059-1066
    • Pascal, M.1    Kunst, F.2    Lepesant, J.A.3    Dedonder, R.4
  • 21
    • 0030597337 scopus 로고    scopus 로고
    • Plasmids for ectopic integration in Bacillus subtilis
    • Guerout-Fleury,A.M., Frandsen,N. and Stragier,P. (1996) Plasmids for ectopic integration in Bacillus subtilis. Gene, 180, 57-61.
    • (1996) Gene , vol.180 , pp. 57-61
    • Guerout-Fleury, A.M.1    Frandsen, N.2    Stragier, P.3
  • 22
    • 0002694056 scopus 로고
    • A method for random mutagenesis of a defined DNA segment using a modified polymerase chain reaction
    • Leung,D., Chen,E. and Goeddel,D.V. (1989) A method for random mutagenesis of a defined DNA segment using a modified polymerase chain reaction. Technique, 1, 11-15.
    • (1989) Technique , vol.1 , pp. 11-15
    • Leung, D.1    Chen, E.2    Goeddel, D.V.3
  • 23
    • 0038261974 scopus 로고    scopus 로고
    • Functional dissection of the Bacillus subtilis pur operator site
    • Bera,A.K., Zhu,J., Zalkin,H. and Smith,J.L. (2003) Functional dissection of the Bacillus subtilis pur operator site. J. Bacteriol., 185, 4099-4109.
    • (2003) J. Bacteriol , vol.185 , pp. 4099-4109
    • Bera, A.K.1    Zhu, J.2    Zalkin, H.3    Smith, J.L.4
  • 24
    • 0035901537 scopus 로고    scopus 로고
    • The structural basis of acyl coenzyme A-dependent regulation of the transcription factor FadR
    • van Aalten,D.M., DiRusso,C.C. and Knudsen,J. (2001) The structural basis of acyl coenzyme A-dependent regulation of the transcription factor FadR. EMBO J., 20, 2041-2050.
    • (2001) EMBO J , vol.20 , pp. 2041-2050
    • van Aalten, D.M.1    DiRusso, C.C.2    Knudsen, J.3
  • 25
    • 0014965617 scopus 로고
    • Lac repressor-operator interaction. I. Equilibrium studies
    • Riggs,A.D., Suzuki,H. and Bourgeois,S. (1970) Lac repressor-operator interaction. I. Equilibrium studies. J. Mol. Biol., 48, 67-83.
    • (1970) J. Mol. Biol , vol.48 , pp. 67-83
    • Riggs, A.D.1    Suzuki, H.2    Bourgeois, S.3
  • 26
    • 0030692787 scopus 로고    scopus 로고
    • Characterization of the fatty acid-responsive transcription factor FadR: Biochemical and genetic analyses of the native conformation and functional domains
    • Raman,N., Black,P.N. and DiRusso,C.C. (1997) Characterization of the fatty acid-responsive transcription factor FadR: Biochemical and genetic analyses of the native conformation and functional domains. J. Biol. Chem., 272, 30645-30650.
    • (1997) J. Biol. Chem , vol.272 , pp. 30645-30650
    • Raman, N.1    Black, P.N.2    DiRusso, C.C.3
  • 27
    • 0034597011 scopus 로고    scopus 로고
    • Crystal structure of FadR, a fatty acid-responsive transcription factor with a novel acyl coenzyme A-binding fold
    • van Aalten,D.M., DiRusso,C.C., Knudsen,J. and Wierenga,R.K. (2000) Crystal structure of FadR, a fatty acid-responsive transcription factor with a novel acyl coenzyme A-binding fold. EMBO J., 19, 5167-5177.
    • (2000) EMBO J , vol.19 , pp. 5167-5177
    • van Aalten, D.M.1    DiRusso, C.C.2    Knudsen, J.3    Wierenga, R.K.4
  • 28
    • 0035907285 scopus 로고    scopus 로고
    • The FadR.DNA complex. Transcriptional control of fatty acid metabolism in Escherichia coli
    • Xu,Y., Heath,R.J., Li,Z., Rock,C.O. and White,S.W. (2001) The FadR.DNA complex. Transcriptional control of fatty acid metabolism in Escherichia coli. J. Biol. Chem., 276, 17373-17379
    • (2001) J. Biol. Chem , vol.276 , pp. 17373-17379
    • Xu, Y.1    Heath, R.J.2    Li, Z.3    Rock, C.O.4    White, S.W.5
  • 29
    • 0027298712 scopus 로고
    • Missense mutations in the Bacillus subtilis gnt repressor that diminish operator binding ability
    • Yoshida,K., Fujita,Y. and Sarai,A. (1993) Missense mutations in the Bacillus subtilis gnt repressor that diminish operator binding ability. J. Mol. Biol., 231, 167-174.
    • (1993) J. Mol. Biol , vol.231 , pp. 167-174
    • Yoshida, K.1    Fujita, Y.2    Sarai, A.3
  • 30
    • 0035910178 scopus 로고    scopus 로고
    • Transcriptional regulation of pentose utilisation systems in the Bacillus/Clostridium group of bacteria
    • Rodionov,D.A., Mironov,A.A. and Gelfand,M.S. (2001) Transcriptional regulation of pentose utilisation systems in the Bacillus/Clostridium group of bacteria. FEMS Microbiol. Lett., 205, 305-314.
    • (2001) FEMS Microbiol. Lett , vol.205 , pp. 305-314
    • Rodionov, D.A.1    Mironov, A.A.2    Gelfand, M.S.3
  • 31
    • 0036158163 scopus 로고    scopus 로고
    • Identification of two myo-inositol transporter genes of Bacillus subtilis
    • Yoshida,K., Yamamoto,Y., Omae,K., Yamamoto,M. and Fujita,Y. (2002) Identification of two myo-inositol transporter genes of Bacillus subtilis. J. Bacteriol., 184, 983-991.
    • (2002) J. Bacteriol , vol.184 , pp. 983-991
    • Yoshida, K.1    Yamamoto, Y.2    Omae, K.3    Yamamoto, M.4    Fujita, Y.5
  • 32
    • 0035393302 scopus 로고    scopus 로고
    • Amino acid-base interactions: A three-dimensional analysis of protein-DNA interactions at an atomic level
    • Luscombe,N.M., Laskowski,R.A. and Thornton,J.M. (2001) Amino acid-base interactions: A three-dimensional analysis of protein-DNA interactions at an atomic level. Nucleic Acids Res., 29, 2860-2874.
    • (2001) Nucleic Acids Res , vol.29 , pp. 2860-2874
    • Luscombe, N.M.1    Laskowski, R.A.2    Thornton, J.M.3
  • 33
    • 2142738304 scopus 로고    scopus 로고
    • Crooks,G.E., Hon.G., Chandonia,J.M. and Brenner,S.E. (2004) WebLogo: A sequence logo generator. Genome Res., 14, 1188-1190.
    • Crooks,G.E., Hon.G., Chandonia,J.M. and Brenner,S.E. (2004) WebLogo: A sequence logo generator. Genome Res., 14, 1188-1190.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.