메뉴 건너뛰기




Volumn 193, Issue 16, 2011, Pages 4069-4074

Crystal Structure of the Pseudomonas aeruginosa Virulence Factor Regulator

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CYCLIC AMP RECEPTOR; DNA BINDING PROTEIN; UNCLASSIFIED DRUG; VIRULENCE FACTOR; VIRULENCE FACTOR REGULATOR;

EID: 79961160738     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00666-10     Document Type: Article
Times cited : (14)

References (42)
  • 2
    • 0036286616 scopus 로고    scopus 로고
    • Differential regulation of twitching motility and elastase production by Vfr in Pseudomonas aeruginosa
    • Beatson, S. A., C. B. Whitchurch, J. L. Sargent, R. C. Levesque, and J. S. Mattick. 2002. Differential regulation of twitching motility and elastase production by Vfr in Pseudomonas aeruginosa. J. Bacteriol. 184:3605-3613.
    • (2002) J. Bacteriol. , vol.184 , pp. 3605-3613
    • Beatson, S.A.1    Whitchurch, C.B.2    Sargent, J.L.3    Levesque, R.C.4    Mattick, J.S.5
  • 3
    • 0037200079 scopus 로고    scopus 로고
    • Structural basis of transcription activation: the CAPalpha CTD-DNA complex
    • Benoff, B., et al. 2002. Structural basis of transcription activation: the CAPalpha CTD-DNA complex. Science 297:1562-1566.
    • (2002) Science , vol.297 , pp. 1562-1566
    • Benoff, B.1
  • 4
    • 84873799110 scopus 로고
    • Studies on lysogenesis I. The mode of phage liberation by lysogenic Escherichia coli
    • Bertani, G. 1951. Studies on lysogenesis. I. The mode of phage liberation by lysogenic Escherichia coli. J. Bacteriol. 62:293-300.
    • (1951) J. Bacteriol. , vol.62 , pp. 293-300
    • Bertani, G.1
  • 5
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and the NMR system: a new software suite for macromolecular structure determination
    • Brunger, A. T., et al. 1998. Crystallography and the NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54:905-921.
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 6
    • 33845654362 scopus 로고    scopus 로고
    • Non-canonical CRP sites control competence regulons in Escherichia coli and many other gamma-proteobacteria
    • Cameron, A. D., and R. J. Redfield. 2006. Non-canonical CRP sites control competence regulons in Escherichia coli and many other gamma-proteobacteria. Nucleic Acids Res. 34:6001-6014.
    • (2006) Nucleic Acids Res , vol.34 , pp. 6001-6014
    • Cameron, A.D.1    Redfield, R.J.2
  • 7
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project No.4
    • Collaborative Computational Project No. 4. 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50:760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 9
    • 0036778160 scopus 로고    scopus 로고
    • fleQ, the gene encoding the major flagellar regulator of Pseudomonas aeruginosa, is sigma70 dependent and is downregulated by Vfr, a homolog of Escherichia coli cyclic AMP receptor protein
    • Dasgupta, N., E. P. Ferrell, K. J. Kanack, S. E. West, and R. Ramphal. 2002. fleQ, the gene encoding the major flagellar regulator of Pseudomonas aeruginosa, is sigma70 dependent and is downregulated by Vfr, a homolog of Escherichia coli cyclic AMP receptor protein. J. Bacteriol. 184:5240-5250.
    • (2002) J. Bacteriol. , vol.184 , pp. 5240-5250
    • Dasgupta, N.1    Ferrell, E.P.2    Kanack, K.J.3    West, S.E.4    Ramphal, R.5
  • 11
    • 17144398027 scopus 로고    scopus 로고
    • The mutation G145S in PrfA, a key virulence regulator of Listeria monocytogenes, increases DNA-binding affinity by stabilizing the HTH motif
    • Eiting, M., G. Hageluken, W. D. Schubert, and D. W. Heinz. 2005. The mutation G145S in PrfA, a key virulence regulator of Listeria monocytogenes, increases DNA-binding affinity by stabilizing the HTH motif. Mol. Microbiol. 56:433-446.
    • (2005) Mol. Microbiol. , vol.56 , pp. 433-446
    • Eiting, M.1    Hageluken, G.2    Schubert, W.D.3    Heinz, D.W.4
  • 12
    • 0000819850 scopus 로고
    • Adenosine 3':5'-cyclic monophosphate as mediator of catabolite repression in Escherichia coli
    • Epstein, W., L. B. Rothman-Denes, and J. Hesse. 1975. Adenosine 3':5'-cyclic monophosphate as mediator of catabolite repression in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 72:2300-2304.
    • (1975) Proc. Natl. Acad. Sci. U. S. A. , vol.72 , pp. 2300-2304
    • Epstein, W.1    Rothman-Denes, L.B.2    Hesse, J.3
  • 14
    • 40849086263 scopus 로고    scopus 로고
    • Emergence of secretion-defective sublines of Pseudomonas aeruginosa PAO1 resulting from spontaneous mutations in the vfr global regulatory gene
    • Fox, A., et al. 2008. Emergence of secretion-defective sublines of Pseudomonas aeruginosa PAO1 resulting from spontaneous mutations in the vfr global regulatory gene. Appl. Environ. Microbiol. 74:1902-1908.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 1902-1908
    • Fox, A.1
  • 15
    • 77954412702 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa Vfr regulator controls global virulence factor expression through cyclic AMP-dependent and -independent mechanisms
    • Fuchs, E. L., et al. 2010. The Pseudomonas aeruginosa Vfr regulator controls global virulence factor expression through cyclic AMP-dependent and -independent mechanisms. J. Bacteriol. 192:3553-3564.
    • (2010) J. Bacteriol. , vol.192 , pp. 3553-3564
    • Fuchs, E.L.1
  • 16
    • 0028335423 scopus 로고
    • Fluorescence study on the nonspecific binding of cyclic-AMP receptor protein to DNA: effect of pH
    • Giraud-Panis, M. J., F. Toulme, B. Blazy, J. C. Maurizot, and F. Culard. 1994. Fluorescence study on the nonspecific binding of cyclic-AMP receptor protein to DNA: effect of pH. Biochimie 76:133-139.
    • (1994) Biochimie , vol.76 , pp. 133-139
    • Giraud-Panis, M.J.1    Toulme, F.2    Blazy, B.3    Maurizot, J.C.4    Culard, F.5
  • 17
    • 0035810698 scopus 로고    scopus 로고
    • Allosteric regulation of the cAMP receptor protein
    • Harman, J. G. 2001. Allosteric regulation of the cAMP receptor protein. Biochim. Biophys. Acta 1547:1-17.
    • (2001) Biochim. Biophys. Acta , vol.1547 , pp. 1-17
    • Harman, J.G.1
  • 18
    • 0347692875 scopus 로고    scopus 로고
    • Malonate: a versatile cryoprotectant and stabilizing solution for salt-grown macromolecular crystals
    • Holyoak, T., et al. 2003. Malonate: a versatile cryoprotectant and stabilizing solution for salt-grown macromolecular crystals. Acta Crystallogr. D 59: 2356-2358.
    • (2003) Acta Crystallogr. D , vol.59 , pp. 2356-2358
    • Holyoak, T.1
  • 19
    • 73949094255 scopus 로고    scopus 로고
    • Three-dimensional EM structure of an intact activator-dependent transcription initiation complex
    • Hudson, B. P., et al. 2009. Three-dimensional EM structure of an intact activator-dependent transcription initiation complex. Proc. Natl. Acad. Sci. U. S. A. 106:19830-19835.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 19830-19835
    • Hudson, B.P.1
  • 20
    • 33845984522 scopus 로고    scopus 로고
    • Characterization of DNA-binding specificity and analysis of binding sites of the Pseudomonas aeruginosa global regulator, Vfr, a homologue of the Escherichia coli cAMP receptor protein
    • Kanack, K. J., L. J. Runyen-Janecky, E. P. Ferrell, S. J. Suh, and S. E. West. 2006. Characterization of DNA-binding specificity and analysis of binding sites of the Pseudomonas aeruginosa global regulator, Vfr, a homologue of the Escherichia coli cAMP receptor protein. Microbiology 152:3485-3496.
    • (2006) Microbiology , vol.152 , pp. 3485-3496
    • Kanack, K.J.1    Runyen-Janecky, L.J.2    Ferrell, E.P.3    Suh, S.J.4    West, S.E.5
  • 21
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E., and K. Henrick. 2007. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372:774-797.
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 22
    • 1342345189 scopus 로고    scopus 로고
    • Catabolite activator protein: DNA binding and transcription activation
    • Lawson, C. L., et al. 2004. Catabolite activator protein: DNA binding and transcription activation. Curr. Opin. Struct. Biol. 14:10-20.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 10-20
    • Lawson, C.L.1
  • 23
    • 70350436270 scopus 로고    scopus 로고
    • Cyclic di-GMP allosterically inhibits the CRP-like protein (Clp) of Xanthomonas axonopodis pv. citri
    • Leduc, J. L., and G. P. Roberts. 2009. Cyclic di-GMP allosterically inhibits the CRP-like protein (Clp) of Xanthomonas axonopodis pv. citri. J. Bacteriol. 191:7121-7122.
    • (2009) J. Bacteriol. , vol.191 , pp. 7121-7122
    • Leduc, J.L.1    Roberts, G.P.2
  • 24
    • 34948829648 scopus 로고    scopus 로고
    • The cyclic AMP receptor protein modulates quorum sensing, motility and multiple genes that affect intestinal colonization in Vibrio cholerae
    • Liang, W., A. Pascual-Montano, A. J. Silva, and J. A. Benitez. 2007. The cyclic AMP receptor protein modulates quorum sensing, motility and multiple genes that affect intestinal colonization in Vibrio cholerae. Microbiology 153:2964-2975.
    • (2007) Microbiology , vol.153 , pp. 2964-2975
    • Liang, W.1    Pascual-Montano, A.2    Silva, A.J.3    Benitez, J.A.4
  • 25
    • 0036786881 scopus 로고    scopus 로고
    • Communications between the high-affinity cyclic nucleotide binding sites in Escherichia coli cyclic AMP receptor protein: effect of single site mutations
    • Lin, S. H., and J. C. Lee. 2002. Communications between the high-affinity cyclic nucleotide binding sites in Escherichia coli cyclic AMP receptor protein: effect of single site mutations. Biochemistry 41:11857-11867.
    • (2002) Biochemistry , vol.41 , pp. 11857-11867
    • Lin, S.H.1    Lee, J.C.2
  • 26
    • 0029887308 scopus 로고    scopus 로고
    • Fluorescence polarization analysis of protein-DNA and protein-protein interactions
    • Lundblad, J. R., M. Laurance, and R. H. Goodman. 1996. Fluorescence polarization analysis of protein-DNA and protein-protein interactions. Mol. Endocrinol. 10:607-612.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 607-612
    • Lundblad, J.R.1    Laurance, M.2    Goodman, R.H.3
  • 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
    • 0032781898 scopus 로고    scopus 로고
    • Functional roles of the two cyclic AMP-dependent forms of cyclic AMP receptor protein from Escherichia coli
    • Mukhopadhyay, J., R. Sur, and P. Parrack. 1999. Functional roles of the two cyclic AMP-dependent forms of cyclic AMP receptor protein from Escherichia coli. FEBS Lett. 453:215-218.
    • (1999) FEBS Lett , vol.453 , pp. 215-218
    • Mukhopadhyay, J.1    Sur, R.2    Parrack, P.3
  • 30
    • 33644768313 scopus 로고    scopus 로고
    • Indirect readout of DNA sequence at the primary-kink site in the CAP-DNA complex: recognition of pyrimidine-purine and purine-purine steps
    • Napoli, A. A., C. L. Lawson, R. H. Ebright, and H. M. Berman. 2006. Indirect readout of DNA sequence at the primary-kink site in the CAP-DNA complex: recognition of pyrimidine-purine and purine-purine steps. J. Mol. Biol. 357:173-183.
    • (2006) J. Mol. Biol. , vol.357 , pp. 173-183
    • Napoli, A.A.1    Lawson, C.L.2    Ebright, R.H.3    Berman, H.M.4
  • 31
    • 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
  • 32
    • 0034671172 scopus 로고    scopus 로고
    • Modeling the cAMPinduced allosteric transition using the crystal structure of CAP-cAMP at 2 1 Å resolution
    • Passner, J. M., S. C. Schultz, and T. A. Steitz. 2000. Modeling the cAMPinduced allosteric transition using the crystal structure of CAP-cAMP at 2.1 Å resolution. J. Mol. Biol. 304:847-859.
    • (2000) J. Mol. Biol. , vol.304 , pp. 847-859
    • Passner, J.M.1    Schultz, S.C.2    Steitz, T.A.3
  • 33
    • 0000445736 scopus 로고    scopus 로고
    • The structure of a CAP-DNA complex having two cAMP molecules bound to each monomer
    • Passner, J. M., and T. A. Steitz. 1997. The structure of a CAP-DNA complex having two cAMP molecules bound to each monomer. Proc. Natl. Acad. Sci. U. S. A. 94:2843-2847.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 2843-2847
    • Passner, J.M.1    Steitz, T.A.2
  • 34
    • 0021694058 scopus 로고
    • The change of DNA structure by specific binding of the cAMP receptor protein from rotation diffusion and dichroism measurements
    • Porschke, D., W. Hillen, and M. Takahashi. 1984. The change of DNA structure by specific binding of the cAMP receptor protein from rotation diffusion and dichroism measurements. EMBO J. 3:2873-2878.
    • (1984) EMBO J , vol.3 , pp. 2873-2878
    • Porschke, D.1    Hillen, W.2    Takahashi, M.3
  • 35
    • 0030033622 scopus 로고    scopus 로고
    • Mode of selectivity in cyclic AMP receptor protein-dependent promoters in Escherichia coli
    • Pyles, E. A., and J. C. Lee. 1996. Mode of selectivity in cyclic AMP receptor protein-dependent promoters in Escherichia coli. Biochemistry 35:1162- 1172.
    • (1996) Biochemistry , vol.35 , pp. 1162-1172
    • Pyles, E.A.1    Lee, J.C.2
  • 36
    • 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., 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
  • 37
    • 70349734666 scopus 로고    scopus 로고
    • Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding
    • Sharma, H., S. Yu, J. Kong, J. Wang, and T. A. Steitz. 2009. Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding. Proc. Natl. Acad. Sci. U. S. A. 106:16604-16609.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 16604-16609
    • Sharma, H.1    Yu, S.2    Kong, J.3    Wang, J.4    Steitz, T.A.5
  • 38
    • 1342281326 scopus 로고    scopus 로고
    • An adenylate cyclasecontrolled signaling network regulates Pseudomonas aeruginosa virulence in a mouse model of acute pneumonia
    • Smith, R. S., M. C. Wolfgang, and S. Lory. 2004. An adenylate cyclasecontrolled signaling network regulates Pseudomonas aeruginosa virulence in a mouse model of acute pneumonia. Infect. Immun. 72:1677-1684.
    • (2004) Infect. Immun. , vol.72 , pp. 1677-1684
    • Smith, R.S.1    Wolfgang, M.C.2    Lory, S.3
  • 39
    • 0036263766 scopus 로고    scopus 로고
    • Effect of vfr mutation on global gene expression and catabolite repression control of Pseudomonas aeruginosa
    • Suh, S. J., et al. 2002. Effect of vfr mutation on global gene expression and catabolite repression control of Pseudomonas aeruginosa. Microbiology 148: 1561-1569.
    • (2002) Microbiology , vol.148 , pp. 1561-1569
    • Suh, S.J.1
  • 40
    • 0028131681 scopus 로고
    • The vfr gene product, required for Pseudomonas aeruginosa exotoxin A and protease production, belongs to the cyclic AMP receptor protein family
    • West, S. E., A. K. Sample, and L. J. Runyen-Janecky. 1994. The vfr gene product, required for Pseudomonas aeruginosa exotoxin A and protease production, belongs to the cyclic AMP receptor protein family. J. Bacteriol. 176:7532-7542.
    • (1994) J. Bacteriol. , vol.176 , pp. 7532-7542
    • West, S.E.1    Sample, A.K.2    Runyen-Janecky, L.J.3
  • 41
    • 0037322193 scopus 로고    scopus 로고
    • Coordinate regulation of bacterial virulence genes by a novel adenylate cyclase-dependent signaling pathway
    • Wolfgang, M. C., V. T. Lee, M. E. Gilmore, and S. Lory. 2003. Coordinate regulation of bacterial virulence genes by a novel adenylate cyclase-dependent signaling pathway. Dev. Cell 4:253-263.
    • (2003) Dev. Cell , vol.4 , pp. 253-263
    • Wolfgang, M.C.1    Lee, V.T.2    Gilmore, M.E.3    Lory, S.4
  • 42
    • 0034649356 scopus 로고    scopus 로고
    • Structural understanding of the allosteric conformational change of cyclic AMP receptor protein by cyclic AMP binding
    • Won, H. S., et al. 2000. Structural understanding of the allosteric conformational change of cyclic AMP receptor protein by cyclic AMP binding. Biochemistry 39:13953-13962.
    • (2000) Biochemistry , vol.39 , pp. 13953-13962
    • Won, H.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.