메뉴 건너뛰기




Volumn 375, Issue 1, 2008, Pages 59-69

XylS-Pm Promoter Interactions through Two Helix-Turn-Helix Motifs: Identifying XylS Residues Important for DNA Binding and Activation

Author keywords

AraC family; DNA contacts; Pseudomonas; transcriptional regulators; XylS

Indexed keywords

ALANINE; ARGININE; ASPARAGINE; BINDING PROTEIN; DINUCLEOTIDE; GLUTAMIC ACID; HELIX LOOP HELIX PROTEIN; LYSINE; NUCLEOTIDE DERIVATIVE; PROTEIN XYLS; RNA POLYMERASE; SIGMA FACTOR; UNCLASSIFIED DRUG;

EID: 36349009319     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.10.047     Document Type: Article
Times cited : (14)

References (62)
  • 2
    • 0034936966 scopus 로고    scopus 로고
    • Identification of the domains of UreR, an AraC-like transcriptional regulator of the urease gene cluster in Proteus mirabilis
    • Poore C.A., Coker C., Dattelbaum J.D., and Mobley H.L. Identification of the domains of UreR, an AraC-like transcriptional regulator of the urease gene cluster in Proteus mirabilis. J. Bacteriol. 183 (2001) 4526-4535
    • (2001) J. Bacteriol. , vol.183 , pp. 4526-4535
    • Poore, C.A.1    Coker, C.2    Dattelbaum, J.D.3    Mobley, H.L.4
  • 3
    • 27944462141 scopus 로고    scopus 로고
    • Characterization of functional domains of the Vibrio cholerae virulence regulator ToxT
    • Prouty M.G., Osorio C.R., and Klose K.E. Characterization of functional domains of the Vibrio cholerae virulence regulator ToxT. Mol. Microbiol. 58 (2005) 1143-1156
    • (2005) Mol. Microbiol. , vol.58 , pp. 1143-1156
    • Prouty, M.G.1    Osorio, C.R.2    Klose, K.E.3
  • 4
    • 0037628879 scopus 로고    scopus 로고
    • Leucines 193 and 194 at the N-terminal domain of the XylS protein, the positive transcriptional regulator of the TOL meta-cleavage pathway, are involved in dimerization
    • Ruíz R., Marqués S., and Ramos J.L. Leucines 193 and 194 at the N-terminal domain of the XylS protein, the positive transcriptional regulator of the TOL meta-cleavage pathway, are involved in dimerization. J. Bacteriol. 185 (2003) 3036-3041
    • (2003) J. Bacteriol. , vol.185 , pp. 3036-3041
    • Ruíz, R.1    Marqués, S.2    Ramos, J.L.3
  • 5
    • 0036510756 scopus 로고    scopus 로고
    • Residues 137 and 153 at the N terminus of the XylS protein influence the effector profile of this transcriptional regulator and the sigma factor used by RNA polymerase to stimulate transcription from its cognate promoter
    • Ruíz R., and Ramos J.L. Residues 137 and 153 at the N terminus of the XylS protein influence the effector profile of this transcriptional regulator and the sigma factor used by RNA polymerase to stimulate transcription from its cognate promoter. J. Biol. Chem. 277 (2002) 7282-7286
    • (2002) J. Biol. Chem. , vol.277 , pp. 7282-7286
    • Ruíz, R.1    Ramos, J.L.2
  • 7
    • 0030582731 scopus 로고    scopus 로고
    • How AraC interacts specifically with its target DNAs
    • Niland P., Huhne R., and Muller-Hill B. How AraC interacts specifically with its target DNAs. J. Mol. Biol. 264 (1996) 667-674
    • (1996) J. Mol. Biol. , vol.264 , pp. 667-674
    • Niland, P.1    Huhne, R.2    Muller-Hill, B.3
  • 8
    • 0024357841 scopus 로고
    • Determining residue-base interactions between AraC protein and araI DNA
    • Brunelle A., and Schleif R. Determining residue-base interactions between AraC protein and araI DNA. J. Mol. Biol. 209 (1989) 607-622
    • (1989) J. Mol. Biol. , vol.209 , pp. 607-622
    • Brunelle, A.1    Schleif, R.2
  • 9
    • 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. 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 (1999) 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
  • 10
    • 0030004590 scopus 로고    scopus 로고
    • Autoactivation of the marRAB multiple antibiotic resistance operon by the MarA transcriptional activator in Escherichia coli
    • Martin R.G., Jair K.W., Wolf Jr. R.E., and Rosner J.L. Autoactivation of the marRAB multiple antibiotic resistance operon by the MarA transcriptional activator in Escherichia coli. J. Bacteriol. 178 (1996) 2216-2223
    • (1996) J. Bacteriol. , vol.178 , pp. 2216-2223
    • Martin, R.G.1    Jair, K.W.2    Wolf Jr., R.E.3    Rosner, J.L.4
  • 11
    • 0024388316 scopus 로고
    • The Escherichia coli melR gene encodes a DNA-binding protein with affinity for specific sequences located in the melibiose-operon regulatory region
    • Webster C., Gardner L., and Busby S. The Escherichia coli melR gene encodes a DNA-binding protein with affinity for specific sequences located in the melibiose-operon regulatory region. Gene 83 (1989) 207-213
    • (1989) Gene , vol.83 , pp. 207-213
    • Webster, C.1    Gardner, L.2    Busby, S.3
  • 12
    • 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. A novel DNA-binding motif in MarA: the first structure for an AraC family transcriptional activator. Proc. Natl. Acad. Sci. USA 95 (1998) 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
  • 13
    • 0001759947 scopus 로고    scopus 로고
    • Crystal structure of the Escherichia coli Rob transcription factor in complex with DNA
    • Kwon H.J., Bennik M.H., Demple B., and Ellenberger T. Crystal structure of the Escherichia coli Rob transcription factor in complex with DNA. Nat. Struct. Biol. 7 (2000) 424-430
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 424-430
    • Kwon, H.J.1    Bennik, M.H.2    Demple, B.3    Ellenberger, T.4
  • 15
    • 0022432285 scopus 로고
    • Altered DNA contacts made by a mutant AraC protein
    • Brunelle A., Hendrickson W., and Schleif R. Altered DNA contacts made by a mutant AraC protein. Nucleic Acids Res. 13 (1985) 5019-5026
    • (1985) Nucleic Acids Res. , vol.13 , pp. 5019-5026
    • Brunelle, A.1    Hendrickson, W.2    Schleif, R.3
  • 16
    • 0026743036 scopus 로고
    • Overexpression, purification and characterization of the Escherichia coli MelR transcription activator protein
    • Caswell R., Williams J., Lyddiatt A., and Busby S. Overexpression, purification and characterization of the Escherichia coli MelR transcription activator protein. Biochem. J. 287 (1992) 493-499
    • (1992) Biochem. J. , vol.287 , pp. 493-499
    • Caswell, R.1    Williams, J.2    Lyddiatt, A.3    Busby, S.4
  • 17
    • 33646266716 scopus 로고    scopus 로고
    • Mutational analysis of the Escherichia coli melR gene suggests a two-state concerted model to explain transcriptional activation and repression in the melibiose operon
    • Kahramanoglou C., Webster C.L., El-Robh M.S., Belyaeva T.A., and Busby S.J. Mutational analysis of the Escherichia coli melR gene suggests a two-state concerted model to explain transcriptional activation and repression in the melibiose operon. J. Bacteriol. 188 (2006) 3199-3207
    • (2006) J. Bacteriol. , vol.188 , pp. 3199-3207
    • Kahramanoglou, C.1    Webster, C.L.2    El-Robh, M.S.3    Belyaeva, T.A.4    Busby, S.J.5
  • 18
    • 34447527767 scopus 로고    scopus 로고
    • Transcription activation by the DNA binding domain of the AraC family protein RhaS in the absence of its effector-binding domain
    • Wickstrum J.R., Skredenske J.M., Kolin A., Jin D.J., Fang J., and Egan S.M. Transcription activation by the DNA binding domain of the AraC family protein RhaS in the absence of its effector-binding domain. J. Bacteriol. 189 (2007) 4984-4993
    • (2007) J. Bacteriol. , vol.189 , pp. 4984-4993
    • Wickstrum, J.R.1    Skredenske, J.M.2    Kolin, A.3    Jin, D.J.4    Fang, J.5    Egan, S.M.6
  • 19
    • 1542616357 scopus 로고    scopus 로고
    • Transcription activation at the Escherichia coli melAB promoter: interactions of MelR with its DNA target site and with domain 4 of the RNA polymerase sigma subunit
    • Grainger D.C., Webster C.L., Belyaeva T.A., Hyde E.I., and Busby S.J. Transcription activation at the Escherichia coli melAB promoter: interactions of MelR with its DNA target site and with domain 4 of the RNA polymerase sigma subunit. Mol. Microbiol. 51 (2004) 1297-1309
    • (2004) Mol. Microbiol. , vol.51 , pp. 1297-1309
    • Grainger, D.C.1    Webster, C.L.2    Belyaeva, T.A.3    Hyde, E.I.4    Busby, S.J.5
  • 20
    • 0032860246 scopus 로고    scopus 로고
    • Amino acid-DNA contacts by RhaS: an AraC family transcription activator
    • Bhende P.M., and Egan S.M. Amino acid-DNA contacts by RhaS: an AraC family transcription activator. J. Bacteriol. 181 (1999) 5185-5192
    • (1999) J. Bacteriol. , vol.181 , pp. 5185-5192
    • Bhende, P.M.1    Egan, S.M.2
  • 21
    • 4444255499 scopus 로고    scopus 로고
    • Amino acid contacts between sigma 70 domain 4 and the transcription activators RhaS and RhaR
    • Wickstrum J.R., and Egan S.M. Amino acid contacts between sigma 70 domain 4 and the transcription activators RhaS and RhaR. J. Bacteriol. 186 (2004) 6277-6285
    • (2004) J. Bacteriol. , vol.186 , pp. 6277-6285
    • Wickstrum, J.R.1    Egan, S.M.2
  • 22
    • 0026658601 scopus 로고
    • Studies on the binding of the Escherichia coli MelR transcription activator protein to operator sequences at the MelAB promoter
    • Caswell R., Webster C., and Busby S. Studies on the binding of the Escherichia coli MelR transcription activator protein to operator sequences at the MelAB promoter. Biochem. J. 287 (1992) 501-508
    • (1992) Biochem. J. , vol.287 , pp. 501-508
    • Caswell, R.1    Webster, C.2    Busby, S.3
  • 23
    • 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. DNA-dependent renaturation of an insoluble DNA binding protein. Identification of the RhaS binding site at rhaBAD. J. Mol. Biol. 243 (1994) 821-829
    • (1994) J. Mol. Biol. , vol.243 , pp. 821-829
    • Egan, S.M.1    Schleif, R.F.2
  • 24
    • 0036083835 scopus 로고    scopus 로고
    • AraC-XylS database: a family of positive transcriptional regulators in bacteria
    • Tobes R., and Ramos J.L. AraC-XylS database: a family of positive transcriptional regulators in bacteria. Nucleic Acids Res. 30 (2002) 318-321
    • (2002) Nucleic Acids Res. , vol.30 , pp. 318-321
    • Tobes, R.1    Ramos, J.L.2
  • 26
    • 0030860391 scopus 로고    scopus 로고
    • Transcriptional control of the Pseudomonas TOL plasmid catabolic operons is achieved through an interplay of host factors and plasmid-encoded regulators
    • Ramos J.L., Marques S., and Timmis K.N. Transcriptional control of the Pseudomonas TOL plasmid catabolic operons is achieved through an interplay of host factors and plasmid-encoded regulators. Annu. Rev. Microbiol. 51 (1997) 341-373
    • (1997) Annu. Rev. Microbiol. , vol.51 , pp. 341-373
    • Ramos, J.L.1    Marques, S.2    Timmis, K.N.3
  • 27
    • 0025299804 scopus 로고
    • A family of positive regulators related to the Pseudomonas putida TOL plasmid XylS and the Escherichia coli AraC activators
    • Ramos J.L., Rojo F., Zhou L., and Timmis K.N. A family of positive regulators related to the Pseudomonas putida TOL plasmid XylS and the Escherichia coli AraC activators. Nucleic Acids Res. 18 (1990) 2149-2152
    • (1990) Nucleic Acids Res. , vol.18 , pp. 2149-2152
    • Ramos, J.L.1    Rojo, F.2    Zhou, L.3    Timmis, K.N.4
  • 28
    • 0025371323 scopus 로고
    • Mutations leading to constitutive expression from the TOL plasmid meta-cleavage pathway operon are located at the C-terminal end of the positive regulator protein XylS
    • Zhou L.M., Timmis K.N., and Ramos J.L. Mutations leading to constitutive expression from the TOL plasmid meta-cleavage pathway operon are located at the C-terminal end of the positive regulator protein XylS. J. Bacteriol. 172 (1990) 3707-3710
    • (1990) J. Bacteriol. , vol.172 , pp. 3707-3710
    • Zhou, L.M.1    Timmis, K.N.2    Ramos, J.L.3
  • 29
    • 0033967976 scopus 로고    scopus 로고
    • Functional domains of the TOL plasmid transcription factor XylS
    • Kaldalu N., Toots U., de Lorenzo V., and Ustav M. Functional domains of the TOL plasmid transcription factor XylS. J. Bacteriol. 182 (2000) 1118-1126
    • (2000) J. Bacteriol. , vol.182 , pp. 1118-1126
    • Kaldalu, N.1    Toots, U.2    de Lorenzo, V.3    Ustav, M.4
  • 30
    • 0034617418 scopus 로고    scopus 로고
    • Mutational analysis of the highly conserved C-terminal residues of the XylS protein, a member of the AraC family of transcriptional regulators
    • Manzanera M., Marques S., and Ramos J.L. Mutational analysis of the highly conserved C-terminal residues of the XylS protein, a member of the AraC family of transcriptional regulators. FEBS Lett. 476 (2000) 312-317
    • (2000) FEBS Lett. , vol.476 , pp. 312-317
    • Manzanera, M.1    Marques, S.2    Ramos, J.L.3
  • 31
    • 0028879546 scopus 로고
    • Purification and regulatory properties of MarA protein, a transcriptional activator of Escherichia coli multiple antibiotic and superoxide resistance promoters
    • Jair K.W., Martin R.G., Rosner J.L., Fujita N., Ishihama A., and Wolf Jr. R.E. Purification and regulatory properties of MarA protein, a transcriptional activator of Escherichia coli multiple antibiotic and superoxide resistance promoters. J. Bacteriol. 177 (1995) 7100-7104
    • (1995) J. Bacteriol. , vol.177 , pp. 7100-7104
    • Jair, K.W.1    Martin, R.G.2    Rosner, J.L.3    Fujita, N.4    Ishihama, A.5    Wolf Jr., R.E.6
  • 32
    • 0029068277 scopus 로고
    • The Escherichia coli MelR transcription activator: production of a stable fragment containing the DNA-binding domain
    • Michán C.M., Busby S.J., and Hyde E.I. The Escherichia coli MelR transcription activator: production of a stable fragment containing the DNA-binding domain. Nucleic Acids Res. 23 (1995) 1518-1523
    • (1995) Nucleic Acids Res. , vol.23 , pp. 1518-1523
    • Michán, C.M.1    Busby, S.J.2    Hyde, E.I.3
  • 33
    • 0032949361 scopus 로고    scopus 로고
    • Binding site recognition by Rns, a virulence regulator in the AraC family
    • Munson G.P., and Scott J.R. Binding site recognition by Rns, a virulence regulator in the AraC family. J. Bacteriol. 181 (1999) 2110-2117
    • (1999) J. Bacteriol. , vol.181 , pp. 2110-2117
    • Munson, G.P.1    Scott, J.R.2
  • 35
    • 0038687706 scopus 로고    scopus 로고
    • Binding of the Escherichia coli MelR protein to the melAB promoter: orientation of MelR subunits and investigation of MelR-DNA contacts
    • Grainger D.C., Belyaeva T.A., Lee D.J., Hyde E.I., and Busby S.J. Binding of the Escherichia coli MelR protein to the melAB promoter: orientation of MelR subunits and investigation of MelR-DNA contacts. Mol. Microbiol. 48 (2003) 335-348
    • (2003) Mol. Microbiol. , vol.48 , pp. 335-348
    • Grainger, D.C.1    Belyaeva, T.A.2    Lee, D.J.3    Hyde, E.I.4    Busby, S.J.5
  • 36
    • 1842271665 scopus 로고
    • A dimer of AraC protein contacts three adjacent major groove regions of the araI DNA site
    • Hendrickson W., and Schleif R. A dimer of AraC protein contacts three adjacent major groove regions of the araI DNA site. Proc. Natl. Acad. Sci. USA 82 (1985) 3129-3133
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 3129-3133
    • Hendrickson, W.1    Schleif, R.2
  • 37
    • 36349001463 scopus 로고    scopus 로고
    • Domínguez-Cuevas, P., Ramos, J. L. & Marqués, S. (2007). Sequential and cooperative XylS-C domain binding to the Pm promoter provokes DNA bending essential for activation. Nucleic Acids Res. Submitted.
  • 39
    • 0036385497 scopus 로고    scopus 로고
    • A comprehensive alanine scanning mutagenesis of the Escherichia coli transcriptional activator SoxS: identifying amino acids important for DNA binding and transcription activation
    • Griffith K.L., and Wolf Jr. R.E. A comprehensive alanine scanning mutagenesis of the Escherichia coli transcriptional activator SoxS: identifying amino acids important for DNA binding and transcription activation. J. Mol. Biol. 322 (2002) 237-257
    • (2002) J. Mol. Biol. , vol.322 , pp. 237-257
    • Griffith, K.L.1    Wolf Jr., R.E.2
  • 40
    • 0034705326 scopus 로고    scopus 로고
    • Probing the Escherichia coli transcriptional activator MarA using alanine-scanning mutagenesis: residues important for DNA binding and activation
    • Gillette W.K., Martin R.G., and Rosner J.L. Probing the Escherichia coli transcriptional activator MarA using alanine-scanning mutagenesis: residues important for DNA binding and activation. J. Mol. Biol. 299 (2000) 1245-1255
    • (2000) J. Mol. Biol. , vol.299 , pp. 1245-1255
    • Gillette, W.K.1    Martin, R.G.2    Rosner, J.L.3
  • 41
    • 33845410556 scopus 로고    scopus 로고
    • Mutational analysis to define an activating region on the redox-sensitive transcriptional regulator OxyR
    • Wang X., Mukhopadnyay P., Wood M.J., Outten F.W., Opdyke J.A., and Storz G. Mutational analysis to define an activating region on the redox-sensitive transcriptional regulator OxyR. J. Bacteriol. 188 (2006) 8335-8342
    • (2006) J. Bacteriol. , vol.188 , pp. 8335-8342
    • Wang, X.1    Mukhopadnyay, P.2    Wood, M.J.3    Outten, F.W.4    Opdyke, J.A.5    Storz, G.6
  • 42
    • 0028096854 scopus 로고
    • Characterization of the activating region of Escherichia coli catabolite gene activator (CAP). I. alanine scanning mutagenesis
    • Niu W., Zhou Y., Dong Q., and Ebright R.H. Characterization of the activating region of Escherichia coli catabolite gene activator (CAP). I. alanine scanning mutagenesis. J. Mol. Biol. 243 (1994) 595-602
    • (1994) J. Mol. Biol. , vol.243 , pp. 595-602
    • Niu, W.1    Zhou, Y.2    Dong, Q.3    Ebright, R.H.4
  • 43
    • 0030813090 scopus 로고    scopus 로고
    • Molecular recognition on signal transduction: the interaction of surfaces of the Spo0F response regulator with its cognate phosphorelay proteins revealed by alanine-scanning mutagenesis
    • Tzeng Y.-L., and Hoch J.A. Molecular recognition on signal transduction: the interaction of surfaces of the Spo0F response regulator with its cognate phosphorelay proteins revealed by alanine-scanning mutagenesis. J. Mol. Biol. 272 (1997) 200-212
    • (1997) J. Mol. Biol. , vol.272 , pp. 200-212
    • Tzeng, Y.-L.1    Hoch, J.A.2
  • 44
    • 0024403619 scopus 로고
    • High-resolution epitope mapping hGH-receptor interactions by alanine-scanning mutagenesis
    • Cunningham B.C., and Wells J.A. High-resolution epitope mapping hGH-receptor interactions by alanine-scanning mutagenesis. Science 244 (1989) 1081-1085
    • (1989) Science , vol.244 , pp. 1081-1085
    • Cunningham, B.C.1    Wells, J.A.2
  • 45
    • 0026356038 scopus 로고
    • Identification of amino acid-base pair contacts by genetic methods
    • Ebright R.H. Identification of amino acid-base pair contacts by genetic methods. Methods Enzymol. 208 (1991) 620-640
    • (1991) Methods Enzymol. , vol.208 , pp. 620-640
    • Ebright, R.H.1
  • 46
    • 0022351389 scopus 로고
    • Use of "loss-of-contact" substitutions to identify residues involved in an amino acid-base pair contact: effect of substitution of Gln18 of lac repressor by Gly, Ser, and Leu
    • Ebright R.H. Use of "loss-of-contact" substitutions to identify residues involved in an amino acid-base pair contact: effect of substitution of Gln18 of lac repressor by Gly, Ser, and Leu. J. Biomol. Struct. Dyn. 3 (1985) 281-297
    • (1985) J. Biomol. Struct. Dyn. , vol.3 , pp. 281-297
    • Ebright, R.H.1
  • 47
    • 0141630791 scopus 로고
    • On the specificity of DNA-protein interactions
    • von Hippel P.H., and Berg O.G. On the specificity of DNA-protein interactions. Proc. Natl. Acad. Sci. USA 83 (1986) 1608-1612
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 1608-1612
    • von Hippel, P.H.1    Berg, O.G.2
  • 48
    • 0019956313 scopus 로고
    • The molecular basis of DNA-protein recognition inferred from the structure of cro repressor
    • Ohlendorf D.H., Anderson W.F., Fisher R.G., Takeda Y., and Matthews B.W. The molecular basis of DNA-protein recognition inferred from the structure of cro repressor. Nature 298 (1982) 718-723
    • (1982) Nature , vol.298 , pp. 718-723
    • Ohlendorf, D.H.1    Anderson, W.F.2    Fisher, R.G.3    Takeda, Y.4    Matthews, B.W.5
  • 49
    • 0032530555 scopus 로고    scopus 로고
    • DNA sequence-dependent deformability deduced from protein-DNA crystal complexes
    • Olson W.K., Gorin A.A., Lu X.J., Hock L.M., and Zhurkin V.B. DNA sequence-dependent deformability deduced from protein-DNA crystal complexes. Proc. Natl. Acad. Sci. USA 95 (1998) 11163-11168
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11163-11168
    • Olson, W.K.1    Gorin, A.A.2    Lu, X.J.3    Hock, L.M.4    Zhurkin, V.B.5
  • 50
    • 20544460658 scopus 로고    scopus 로고
    • Protein-DNA recognition patterns and predictions
    • Sarai A., and Kono H. Protein-DNA recognition patterns and predictions. Annu. Rev. Biophys. Biomol. Struct. 34 (2005) 379-398
    • (2005) Annu. Rev. Biophys. Biomol. Struct. , vol.34 , pp. 379-398
    • Sarai, A.1    Kono, H.2
  • 51
    • 29244480001 scopus 로고    scopus 로고
    • RNA polymerase holoenzymes can share a single transcription start site for the Pm promoter. Critical nucleotides in the - 7 to - 18 region are needed to select between RNA polymerase with sigma38 or sigma32
    • Domínguez-Cuevas P., Marín P., Ramos J.L., and Marqués S. RNA polymerase holoenzymes can share a single transcription start site for the Pm promoter. Critical nucleotides in the - 7 to - 18 region are needed to select between RNA polymerase with sigma38 or sigma32. J. Biol. Chem. 280 (2005) 41315-41323
    • (2005) J. Biol. Chem. , vol.280 , pp. 41315-41323
    • Domínguez-Cuevas, P.1    Marín, P.2    Ramos, J.L.3    Marqués, S.4
  • 52
    • 0031025674 scopus 로고    scopus 로고
    • Chromosomal insertion of the entire Escherichia coli lactose operon, into two strains of Pseudomonas, using a modified mini-Tn5 delivery system
    • Hansen L.H., Sorensen S.J., and Jensen L.B. Chromosomal insertion of the entire Escherichia coli lactose operon, into two strains of Pseudomonas, using a modified mini-Tn5 delivery system. Gene 186 (1997) 167-173
    • (1997) Gene , vol.186 , pp. 167-173
    • Hansen, L.H.1    Sorensen, S.J.2    Jensen, L.B.3
  • 53
    • 0033058086 scopus 로고    scopus 로고
    • The Escherichia coli Ada protein can interact with two distinct determinants in the sigma70 subunit of RNA polymerase according to promoter architecture: identification of the target of Ada activation at the alkA promoter
    • Landini P., and Busby S.J. The Escherichia coli Ada protein can interact with two distinct determinants in the sigma70 subunit of RNA polymerase according to promoter architecture: identification of the target of Ada activation at the alkA promoter. J. Bacteriol. 181 (1999) 1524-1529
    • (1999) J. Bacteriol. , vol.181 , pp. 1524-1529
    • Landini, P.1    Busby, S.J.2
  • 54
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan D. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166 (1983) 557-580
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 55
    • 0026020230 scopus 로고
    • Identification of a central regulator of stationary-phase gene expression in Escherichia coli
    • Lange R., and Hengge-Aronis R. Identification of a central regulator of stationary-phase gene expression in Escherichia coli. Mol. Microbiol. 5 (1991) 49-59
    • (1991) Mol. Microbiol. , vol.5 , pp. 49-59
    • Lange, R.1    Hengge-Aronis, R.2
  • 56
    • 0343419040 scopus 로고
    • Altered effector specificities in regulators of gene expression: TOL plasmid xylS mutants and their use to engineer expansion of the range of aromatics degraded by bacteria
    • Ramos J.L., Stolz A., Reineke W., and Timmis K.N. Altered effector specificities in regulators of gene expression: TOL plasmid xylS mutants and their use to engineer expansion of the range of aromatics degraded by bacteria. Proc. Natl. Acad. Sci. USA 83 (1986) 8467-8471
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8467-8471
    • Ramos, J.L.1    Stolz, A.2    Reineke, W.3    Timmis, K.N.4
  • 57
    • 0023443646 scopus 로고
    • Regulatory circuits controlling transcription of TOL plasmid operon encoding meta-cleavage pathway for degradation of alkylbenzoates by Pseudomonas
    • Ramos J.L., Mermod N., and Timmis K.N. Regulatory circuits controlling transcription of TOL plasmid operon encoding meta-cleavage pathway for degradation of alkylbenzoates by Pseudomonas. Mol. Microbiol. 1 (1987) 293-300
    • (1987) Mol. Microbiol. , vol.1 , pp. 293-300
    • Ramos, J.L.1    Mermod, N.2    Timmis, K.N.3
  • 59
    • 0001823786 scopus 로고
    • PCR protocols. A guide to methods and applications
    • Academic Press, San Diego, CA
    • Higushi R. PCR protocols. A guide to methods and applications. Recombinant PCR (1990), Academic Press, San Diego, CA 177-183
    • (1990) Recombinant PCR , pp. 177-183
    • Higushi, R.1
  • 60
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • Miller J. Experiments in Molecular Genetics (1972), Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 352-355
    • (1972) Experiments in Molecular Genetics , pp. 352-355
    • Miller, J.1
  • 61
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 62
    • 0141960050 scopus 로고    scopus 로고
    • Antibiotic-dependent induction of Pseudomonas putida DOT-T1E TtgABC efflux pump is mediated by the drug binding repressor TtgR
    • Terán W., Felipe A., Segura A., Rojas A., Ramos J.L., and Gallegos M.T. Antibiotic-dependent induction of Pseudomonas putida DOT-T1E TtgABC efflux pump is mediated by the drug binding repressor TtgR. Antimicrob. Agents Chemother. 47 (2003) 3067-3072
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 3067-3072
    • Terán, W.1    Felipe, A.2    Segura, A.3    Rojas, A.4    Ramos, J.L.5    Gallegos, M.T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.