메뉴 건너뛰기




Volumn 189, Issue 16, 2007, Pages 5987-5995

Crystal structures of the receiver domain of the response regulator PhoP from Escherichia coli in the absence and presence of the phosphoryl analog beryllofiuoride

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BERYLLOFLUORIDE; FLUORIDE; OUTER MEMBRANE PROTEIN REGULATOR; PHOP PROTEIN; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 34547743126     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00049-07     Document Type: Article
Times cited : (68)

References (54)
  • 1
    • 24344476732 scopus 로고    scopus 로고
    • Mechanism of activation for transcription factor PhoB suggested by different modes of dimerization in the inactive and active states
    • Bachhawat, P., G. V. Swapna, G. T. Montelione, and A. M. Stock. 2005. Mechanism of activation for transcription factor PhoB suggested by different modes of dimerization in the inactive and active states. Structure 13:1353-1363.
    • (2005) Structure , vol.13 , pp. 1353-1363
    • Bachhawat, P.1    Swapna, G.V.2    Montelione, G.T.3    Stock, A.M.4
  • 2
    • 1942475365 scopus 로고    scopus 로고
    • Crystal structure of the response regulator 02 receiver domain, the essential YycF two-component system of Streptococcus pneumoniae in both complexed and native states
    • Bent, C. J., N. W. Isaacs, T. J. Mitchell, and A. Riboldi- Tunnicliffe. 2004. Crystal structure of the response regulator 02 receiver domain, the essential YycF two-component system of Streptococcus pneumoniae in both complexed and native states. J. Bacteriol. 186:2872-2879.
    • (2004) J. Bacteriol , vol.186 , pp. 2872-2879
    • Bent, C.J.1    Isaacs, N.W.2    Mitchell, T.J.3    Riboldi- Tunnicliffe, A.4
  • 3
    • 21244435631 scopus 로고    scopus 로고
    • The PhoP/PhoQ system controls the intramacrophage type three secretion system of Salmonella enterica
    • Bijlsma, J. J., and E. A. Groisman. 2005. The PhoP/PhoQ system controls the intramacrophage type three secretion system of Salmonella enterica. Mol. Microbiol. 57:85-96.
    • (2005) Mol. Microbiol , vol.57 , pp. 85-96
    • Bijlsma, J.J.1    Groisman, E.A.2
  • 4
    • 0037215598 scopus 로고    scopus 로고
    • The crystal structure of the phosphorylation domain in PhoP reveals a functional tandem association mediated by an asymmetric interface
    • Birck, C., Y. Chen, F. M. Hulett, and J. P. Samama. 2003. The crystal structure of the phosphorylation domain in PhoP reveals a functional tandem association mediated by an asymmetric interface. J. Bacteriol. 185:254-261.
    • (2003) J. Bacteriol , vol.185 , pp. 254-261
    • Birck, C.1    Chen, Y.2    Hulett, F.M.3    Samama, J.P.4
  • 6
    • 0036174746 scopus 로고    scopus 로고
    • Evidence of intradomain and interdomain flexibility in an OmpR/PhoB homolog from Thermotoga maritima
    • Buckler, D. R., Y. Zhou, and A. M. Stock. 2002. Evidence of intradomain and interdomain flexibility in an OmpR/PhoB homolog from Thermotoga maritima. Structure 10:153-164.
    • (2002) Structure , vol.10 , pp. 153-164
    • Buckler, D.R.1    Zhou, Y.2    Stock, A.M.3
  • 7
    • 0037215521 scopus 로고    scopus 로고
    • Residue R113 is essential for PhoP dimerization and function: A residue buried in the asymmetric PhoP dimer interface determined in the PhoPN three-dimensional crystal structure
    • Chen, Y., C. Birck, J. P. Samama, and F. M. Hulett. 2003. Residue R113 is essential for PhoP dimerization and function: a residue buried in the asymmetric PhoP dimer interface determined in the PhoPN three-dimensional crystal structure. J. Bacteriol. 185:262-273.
    • (2003) J. Bacteriol , vol.185 , pp. 262-273
    • Chen, Y.1    Birck, C.2    Samama, J.P.3    Hulett, F.M.4
  • 8
    • 0029036255 scopus 로고
    • A superior host strain for the over-expression of cloned genes using the T7 promoter based vectors
    • Doherty, A. J., S. R. Ashford, J. A. Brannigan, and D. B. Wigley. 1995. A superior host strain for the over-expression of cloned genes using the T7 promoter based vectors. Nucleic Acids Res. 23:2074-2075.
    • (1995) Nucleic Acids Res , vol.23 , pp. 2074-2075
    • Doherty, A.J.1    Ashford, S.R.2    Brannigan, J.A.3    Wigley, D.B.4
  • 9
    • 0029164694 scopus 로고
    • A common switch in activation of the response regulators NtrC and PhoB: Phosphorylation induces dimerization of the receiver modules
    • Fiedler, U., and V. Weiss. 1995. A common switch in activation of the response regulators NtrC and PhoB: phosphorylation induces dimerization of the receiver modules. EMBO J. 14:3696-3705.
    • (1995) EMBO J , vol.14 , pp. 3696-3705
    • Fiedler, U.1    Weiss, V.2
  • 10
    • 0001528720 scopus 로고    scopus 로고
    • Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules
    • Fraczkiewicz, R., and W. Braun. 1998. Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules. J. Comput. Chem. 19:319-333.
    • (1998) J. Comput. Chem , vol.19 , pp. 319-333
    • Fraczkiewicz, R.1    Braun, W.2
  • 11
    • 34250177264 scopus 로고    scopus 로고
    • Domain orientation in the inactive response regulator Mycobacterium tuberculosis MtrA provides a barrier to activation
    • Friedland, N., T. R. Mack, M. Yu, L.-W. Hung, T. C. Terwilliger, G. S. Waldo, and A. M. Stock. 2007. Domain orientation in the inactive response regulator Mycobacterium tuberculosis MtrA provides a barrier to activation. Biochemistry 46:6733-6743.
    • (2007) Biochemistry , vol.46 , pp. 6733-6743
    • Friedland, N.1    Mack, T.R.2    Yu, M.3    Hung, L.-W.4    Terwilliger, T.C.5    Waldo, G.S.6    Stock, A.M.7
  • 12
    • 0035105303 scopus 로고    scopus 로고
    • The pleiotropic two-component regulatory system PhoP-PhoQ
    • Groisman, E. A. 2001. The pleiotropic two-component regulatory system PhoP-PhoQ. J. Bacteriol. 183:1835-1842.
    • (2001) J. Bacteriol , vol.183 , pp. 1835-1842
    • Groisman, E.A.1
  • 13
    • 0343575172 scopus 로고
    • Salmonella typhimurium phoP virulence gene is a transcriptional regulator
    • Groisman, E. A., E. Chiao, C. J. Lipps, and F. Heffron. 1989. Salmonella typhimurium phoP virulence gene is a transcriptional regulator. Proc. Natl. Acad. Sci. USA 86:7077-7081.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 7077-7081
    • Groisman, E.A.1    Chiao, E.2    Lipps, C.J.3    Heffron, F.4
  • 14
    • 0030984298 scopus 로고    scopus 로고
    • Regulation of lipid A modifications by Salmonella typhimurium virulence genes phoP-phoQ
    • Guo, L., K. B. Lim, J. S. Gunn, B. Bainbridge, R. P. Darveau, M. Hackett, and S. I. Miller. 1997. Regulation of lipid A modifications by Salmonella typhimurium virulence genes phoP-phoQ. Science 276:250-253.
    • (1997) Science , vol.276 , pp. 250-253
    • Guo, L.1    Lim, K.B.2    Gunn, J.S.3    Bainbridge, B.4    Darveau, R.P.5    Hackett, M.6    Miller, S.I.7
  • 15
    • 0028875660 scopus 로고
    • Tandem binding of six OmpR proteins to the ompF upstream regulatory sequence of Escherichia coli
    • Harlocker, S. L., L. Bergstrom, and M. Inouye. 1995. Tandem binding of six OmpR proteins to the ompF upstream regulatory sequence of Escherichia coli. J. Biol. Chem. 270:26849-26856.
    • (1995) J. Biol. Chem , vol.270 , pp. 26849-26856
    • Harlocker, S.L.1    Bergstrom, L.2    Inouye, M.3
  • 16
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure
    • Hendrickson, W. A., J. R. Horton, and D. M. LeMaster. 1990. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure. EMBO J. 9:1665-1672.
    • (1990) EMBO J , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    LeMaster, D.M.3
  • 17
    • 0035798619 scopus 로고    scopus 로고
    • Multimerization of phosphorylated and non-phosphorylated ArcA is necessary for the response regulator function of the Arc two-component signal transduction system
    • Jeon, Y., Y. S. Lee, J. S. Han, J. B. Kim, and D. S. Hwang. 2001. Multimerization of phosphorylated and non-phosphorylated ArcA is necessary for the response regulator function of the Arc two-component signal transduction system. J. Biol. Chem. 276:40873-40879.
    • (2001) J. Biol. Chem , vol.276 , pp. 40873-40879
    • Jeon, Y.1    Lee, Y.S.2    Han, J.S.3    Kim, J.B.4    Hwang, D.S.5
  • 19
    • 14644435718 scopus 로고    scopus 로고
    • CpxR/OmpR interplay regulates curli gene expression in response to osmolarity in Escherichia coli
    • Jubelin, G., A. Vianney, C. Beloin, J. M. Ghigo, J. C. Lazzaroni, P. Lejeune, and C. Dorel. 2005. CpxR/OmpR interplay regulates curli gene expression in response to osmolarity in Escherichia coli. J. Bacteriol. 187:2038-2049.
    • (2005) J. Bacteriol , vol.187 , pp. 2038-2049
    • Jubelin, G.1    Vianney, A.2    Beloin, C.3    Ghigo, J.M.4    Lazzaroni, J.C.5    Lejeune, P.6    Dorel, C.7
  • 20
    • 4444240880 scopus 로고    scopus 로고
    • Connecting two-component regulatory systems by a protein that protects a response regulator from dephosphorylation by its cognate sensor
    • Kato, A., and E. A. Groisman. 2004. Connecting two-component regulatory systems by a protein that protects a response regulator from dephosphorylation by its cognate sensor. Genes Dev. 18:2302-2313.
    • (2004) Genes Dev , vol.18 , pp. 2302-2313
    • Kato, A.1    Groisman, E.A.2
  • 22
    • 0033599026 scopus 로고    scopus 로고
    • Structure of a transiently phosphorylated switch in bacterial signal transduction
    • Kern, D., B. F. Volkman, P. Luginbuhl, M. J. Nohaile, S. Kustu, and D. E. Wemmer. 1999. Structure of a transiently phosphorylated switch in bacterial signal transduction. Nature 40:894-898.
    • (1999) Nature , vol.40 , pp. 894-898
    • Kern, D.1    Volkman, B.F.2    Luginbuhl, P.3    Nohaile, M.J.4    Kustu, S.5    Wemmer, D.E.6
  • 23
    • 0018379252 scopus 로고
    • Regulation of non-specific acid phosphatase in Salmonella: PhoN and phoP genes
    • Kier, L. D., R. M. Weppelman, and B. N. Ames. 1979. Regulation of non-specific acid phosphatase in Salmonella: phoN and phoP genes. J. Bacteriol. 138:155-161.
    • (1979) J. Bacteriol , vol.138 , pp. 155-161
    • Kier, L.D.1    Weppelman, R.M.2    Ames, B.N.3
  • 24
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., M. W. McArthur, D. S. Moss, and J. M. Thornton. 1993. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26:282-291.
    • (1993) J. Appl. Crystallogr , vol.26 , pp. 282-291
    • Laskowski, R.A.1    McArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 27
    • 0029896773 scopus 로고    scopus 로고
    • The activation of PhoB by acetylphosphate
    • McCleary, W. R. 1996. The activation of PhoB by acetylphosphate. Mol. Microbiol. 20:1155-1163.
    • (1996) Mol. Microbiol , vol.20 , pp. 1155-1163
    • McCleary, W.R.1
  • 28
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit: A versatile program for manipulating atomic coordinates and electron density
    • McRee, D. E. 1999. XtalView/Xfit: a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125:156-165.
    • (1999) J. Struct. Biol , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 29
    • 0003582512 scopus 로고
    • A two-component regulatory system (PhoP/ PhoQ) controls Salmonella typhimurium virulence
    • Miller, S. I., A. M. Kukral, and J. J. Mekalanos. 1989. A two-component regulatory system (PhoP/ PhoQ) controls Salmonella typhimurium virulence. Proc. Natl. Acad. Sci. USA 86:5054-5058.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5054-5058
    • Miller, S.I.1    Kukral, A.M.2    Mekalanos, J.J.3
  • 31
    • 0034518521 scopus 로고    scopus 로고
    • The regulatory protein PhoP controls susceptibility to the host inflammatory response in Shigella fiexneri
    • Moss, J. E., P. E. Fisher, B. Vick, E. A. Groisman, and A. Zychlinsky. 2000. The regulatory protein PhoP controls susceptibility to the host inflammatory response in Shigella fiexneri. Cell. Microbiol. 2:443-452.
    • (2000) Cell. Microbiol , vol.2 , pp. 443-452
    • Moss, J.E.1    Fisher, P.E.2    Vick, B.3    Groisman, E.A.4    Zychlinsky, A.5
  • 32
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., A. A. Vagin, and E. J. Dodson. 1997. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53:240-255.
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 33
    • 33646898275 scopus 로고    scopus 로고
    • The structural basis of signal transduction for the response regulator PrrA from Mycobacterium tuberculosis
    • Nowak, E., S. Panjikar, P. Konarev, D. I. Svergun, and P. A. Tucker. 2006. The structural basis of signal transduction for the response regulator PrrA from Mycobacterium tuberculosis. J. Biol. Chem. 281:9659-9666.
    • (2006) J. Biol. Chem , vol.281 , pp. 9659-9666
    • Nowak, E.1    Panjikar, S.2    Konarev, P.3    Svergun, D.I.4    Tucker, P.A.5
  • 34
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and W. Minor. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 35
    • 0034079245 scopus 로고    scopus 로고
    • The response regulator PhoP is important for survival under conditions of macrophage-induced stress and virulence in Yersinia pestis
    • Oyston, P. C., N. Dorrell, K. Williams, S. R. Li, M. Green, R. W. Titball, and B. W. Wren. 2000. The response regulator PhoP is important for survival under conditions of macrophage-induced stress and virulence in Yersinia pestis. Infect. Immun. 68:3419-3425.
    • (2000) Infect. Immun , vol.68 , pp. 3419-3425
    • Oyston, P.C.1    Dorrell, N.2    Williams, K.3    Li, S.R.4    Green, M.5    Titball, R.W.6    Wren, B.W.7
  • 36
    • 29244483427 scopus 로고    scopus 로고
    • Dimerization and DNA binding of the Salmonella enterica PhoP response regulator are phosphorylation independent
    • Perron-Savard, P., G. De Crescenzo, and H. Le Moual. 2005. Dimerization and DNA binding of the Salmonella enterica PhoP response regulator are phosphorylation independent. Microbiology 151:3979-3987.
    • (2005) Microbiology , vol.151 , pp. 3979-3987
    • Perron-Savard, P.1    De Crescenzo, G.2    Le Moual, H.3
  • 37
    • 1842848075 scopus 로고    scopus 로고
    • Domain arrangement of Der, a switch protein containing two GTPase domains
    • Robinson, V. L., J. Hwang, E. Fox, M. Inouye, and A. M. Stock. 2002. Domain arrangement of Der, a switch protein containing two GTPase domains. Structure 10:1649-1658.
    • (2002) Structure , vol.10 , pp. 1649-1658
    • Robinson, V.L.1    Hwang, J.2    Fox, E.3    Inouye, M.4    Stock, A.M.5
  • 38
    • 0038154011 scopus 로고    scopus 로고
    • Structural analysis of the domain interface in DrrB, a response regulator of the OmpR/PhoB subfamily
    • Robinson, V. L., T. Wu, and A. M. Stock. 2003. Structural analysis of the domain interface in DrrB, a response regulator of the OmpR/PhoB subfamily. J. Bacteriol. 185:4186-4194.
    • (2003) J. Bacteriol , vol.185 , pp. 4186-4194
    • Robinson, V.L.1    Wu, T.2    Stock, A.M.3
  • 39
    • 0028103275 scopus 로고    scopus 로고
    • SERC (UK) Collaborative Computational Project. 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50:760-763.
    • SERC (UK) Collaborative Computational Project. 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50:760-763.
  • 41
    • 3142592449 scopus 로고    scopus 로고
    • PhoP-regulated Salmonella resistance to the antimicrobial peptides magainin 2 and polymyxin B
    • Shi, Y., M. J. Cromie, F. F. Hsu, J. Turk, and E. A. Groisman. 2004. PhoP-regulated Salmonella resistance to the antimicrobial peptides magainin 2 and polymyxin B. Mol. Microbiol. 53:229-241.
    • (2004) Mol. Microbiol , vol.53 , pp. 229-241
    • Shi, Y.1    Cromie, M.J.2    Hsu, F.F.3    Turk, J.4    Groisman, E.A.5
  • 42
    • 14244270197 scopus 로고    scopus 로고
    • Signal-dependent binding of the response regulators PhoP and PmrA to their target promoters in vivo
    • Shin, D., and E. A. Groisman. 2005. Signal-dependent binding of the response regulators PhoP and PmrA to their target promoters in vivo. J. Biol. Chem. 280:4089-4094.
    • (2005) J. Biol. Chem , vol.280 , pp. 4089-4094
    • Shin, D.1    Groisman, E.A.2
  • 43
    • 33845458915 scopus 로고    scopus 로고
    • A positive feedback loop promotes transcription surge that jump-starts Salmonella virulence circuit
    • Shin, D., E. J. Lee, H. Huang, and E. A. Groisman. 2006. A positive feedback loop promotes transcription surge that jump-starts Salmonella virulence circuit. Science 314:1607-1609.
    • (2006) Science , vol.314 , pp. 1607-1609
    • Shin, D.1    Lee, E.J.2    Huang, H.3    Groisman, E.A.4
  • 44
    • 0344142378 scopus 로고    scopus 로고
    • Three-dimensional crystal structure of the transcription factor PhoB receiver domain
    • Solà, M., F. X. Gomis-Rüth, L. Serrano, A. González, and M. Coll. 1999. Three-dimensional crystal structure of the transcription factor PhoB receiver domain. J. Mol. Biol. 285:675-687.
    • (1999) J. Mol. Biol , vol.285 , pp. 675-687
    • Solà, M.1    Gomis-Rüth, F.X.2    Serrano, L.3    González, A.4    Coll, M.5
  • 45
    • 3042613550 scopus 로고    scopus 로고
    • Likelihood-enhanced fast rotation functions
    • Storoni, L. C., A. J. McCoy, and R. J. Read. 2004. Likelihood-enhanced fast rotation functions. Acta Crystallogr. D 60:432-438.
    • (2004) Acta Crystallogr. D , vol.60 , pp. 432-438
    • Storoni, L.C.1    McCoy, A.J.2    Read, R.J.3
  • 46
    • 0021919826 scopus 로고
    • A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes
    • Tabor, S., and C. C. Richardson. 1985. A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes. Proc. Natl. Acad. Sci. USA 84:1074-1078.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1074-1078
    • Tabor, S.1    Richardson, C.C.2
  • 47
    • 18144411635 scopus 로고    scopus 로고
    • Structural analysis and solution studies of the activated regulatory domain of the response regulator ArcA: A symmetric dimer mediated by the α4-p5-α5 face
    • Toro-Roman, A., T. R. Mack, and A. M. Stock. 2005. Structural analysis and solution studies of the activated regulatory domain of the response regulator ArcA: a symmetric dimer mediated by the α4-p5-α5 face. J. Mol. Biol. 349:11-26.
    • (2005) J. Mol. Biol , vol.349 , pp. 11-26
    • Toro-Roman, A.1    Mack, T.R.2    Stock, A.M.3
  • 48
    • 28844432653 scopus 로고    scopus 로고
    • A common dimerization interface in bacterial response regulators KdpE and TorR
    • Toro-Roman, A., T. Wu, and A. M. Stock. 2005. A common dimerization interface in bacterial response regulators KdpE and TorR. Protein Sci. 14:3077-3088.
    • (2005) Protein Sci , vol.14 , pp. 3077-3088
    • Toro-Roman, A.1    Wu, T.2    Stock, A.M.3
  • 49
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • Vaguine, A. A., J. Richelle, and S. J. Wodak. 1999. SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model. Acta Crystallogr. D 55: 191-205.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 50
    • 0035937443 scopus 로고    scopus 로고
    • Two-state allosteric behavior in a single domain signaling protein
    • Volkman, B. F., D. Lipson, D. E. Wemmer, and D. Kern. 2001. Two-state allosteric behavior in a single domain signaling protein. Science 291:2429-2433.
    • (2001) Science , vol.291 , pp. 2429-2433
    • Volkman, B.F.1    Lipson, D.2    Wemmer, D.E.3    Kern, D.4
  • 51
    • 0030797034 scopus 로고    scopus 로고
    • Involvement of the amino-terminal phosphorylation module of UhpA in activation of uhpT transcription in Escherichia coli
    • Webber, C. A., and R. J. Kadner. 1997. Involvement of the amino-terminal phosphorylation module of UhpA in activation of uhpT transcription in Escherichia coli. Mol. Microbiol. 24:1039-1048.
    • (1997) Mol. Microbiol , vol.24 , pp. 1039-1048
    • Webber, C.A.1    Kadner, R.J.2
  • 52
    • 28844503098 scopus 로고    scopus 로고
    • Beryllofluoride binding mimics phosphorylation of aspartate in response regulators
    • Wemmer, D. E., and D. Kern. 2005. Beryllofluoride binding mimics phosphorylation of aspartate in response regulators. J. Bacteriol. 187:8229-8230.
    • (2005) J. Bacteriol , vol.187 , pp. 8229-8230
    • Wemmer, D.E.1    Kern, D.2
  • 53
    • 33745219470 scopus 로고    scopus 로고
    • Transcription regulation of ompF and ompC by a single transcription factor, OmpR
    • Yoshida, T., L. Qin, L. A. Egger, and M. Inouye. 2006. Transcription regulation of ompF and ompC by a single transcription factor, OmpR. J. Biol. Chem. 281:17114-17123.
    • (2006) J. Biol. Chem , vol.281 , pp. 17114-17123
    • Yoshida, T.1    Qin, L.2    Egger, L.A.3    Inouye, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.