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Volumn 149, Issue 12, 2003, Pages 3383-3394

Differential regulation of the Proteus mirabilis urease gene cluster by UreR and H-NS

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIA; CARBON DIOXIDE; CURVED DNA; DNA FRAGMENT; HYBRID PROTEIN; MYC PROTEIN; POLYADENYLIC ACID; REGULATOR PROTEIN; SPACER DNA; UREA; UREASE; VIRULENCE FACTOR;

EID: 0346252350     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.26624-0     Document Type: Article
Times cited : (44)

References (44)
  • 1
    • 0034002290 scopus 로고    scopus 로고
    • H-NS is a repressor of the Proteus mirabilis urease transcriptional activator gene ureR
    • Coker, C., Bakare, O. O. & Mobley, H. L. (2000). H-NS is a repressor of the Proteus mirabilis urease transcriptional activator gene ureR. J Bacteriol 182, 2649-2653.
    • (2000) J. Bacteriol. , vol.182 , pp. 2649-2653
    • Coker, C.1    Bakare, O.O.2    Mobley, H.L.3
  • 2
    • 0029084928 scopus 로고
    • H-NS regulation of virulence gene expression in enteroinvasive Escherichia coli harboring the virulence plasmid integrated into the host chromosome
    • 7 other authors
    • Colonna, B., Casalino, M., Fradiani, P. A. & 7 other authors (1995). H-NS regulation of virulence gene expression in enteroinvasive Escherichia coli harboring the virulence plasmid integrated into the host chromosome. J Bacteriol 177, 4703-4712.
    • (1995) J. Bacteriol. , vol.177 , pp. 4703-4712
    • Colonna, B.1    Casalino, M.2    Fradiani, P.A.3
  • 3
    • 0027191825 scopus 로고
    • The plasmid-encoded urease gene cluster of the family Enterobacteriaceae is positively regulated by UreR, a member of the AraC family of transcriptional activators
    • D'Orazio, S. E. & Collins, C. M. (1993). The plasmid-encoded urease gene cluster of the family Enterobacteriaceae is positively regulated by UreR, a member of the AraC family of transcriptional activators. J Bacteriol 175, 3459-3467.
    • (1993) J. Bacteriol. , vol.175 , pp. 3459-3467
    • D'Orazio, S.E.1    Collins, C.M.2
  • 4
    • 0028902206 scopus 로고
    • UreR activates transcription at multiple promoters within the plasmid-encoded urease locus of the Enterobacteriaceae
    • D'Orazio, S. E. & Collins, C. M. (1995). UreR activates transcription at multiple promoters within the plasmid-encoded urease locus of the Enterobacteriaceae. Mol Microbiol 16, 145-155.
    • (1995) Mol. Microbiol. , vol.16 , pp. 145-155
    • D'Orazio, S.E.1    Collins, C.M.2
  • 5
    • 0029835150 scopus 로고    scopus 로고
    • Activation of transcription at divergent urea-dependent promoters by the urease gene regulator UreR
    • D'Orazio, S. E., Thomas, V. & Collins, C. M. (1996). Activation of transcription at divergent urea-dependent promoters by the urease gene regulator UreR. Mol Microbiol 21, 643-655.
    • (1996) Mol. Microbiol. , vol.21 , pp. 643-655
    • D'Orazio, S.E.1    Thomas, V.2    Collins, C.M.3
  • 6
    • 0025342874 scopus 로고
    • DNA supercoiling and environmental regulation of virulence gene expression in Shigella flexneri
    • Dorman, C. J., Bhriain, N. N. & Higgins, C. F. (1990). DNA supercoiling and environmental regulation of virulence gene expression in Shigella flexneri. Nature 344, 789-792.
    • (1990) Nature , vol.344 , pp. 789-792
    • Dorman, C.J.1    Bhriain, N.N.2    Higgins, C.F.3
  • 7
    • 0032401769 scopus 로고    scopus 로고
    • Thermoregulation of Shigella and Escherichia coli EIEC pathogenicity. A temperature-dependent structural transition of DNA modulates accessibility of virF promoter to transcriptional repressor H-NS
    • Falconi, M., Colonna, B., Prosseda, G., Micheli, G. & Gualerzi, C. O. (1998). Thermoregulation of Shigella and Escherichia coli EIEC pathogenicity. A temperature-dependent structural transition of DNA modulates accessibility of virF promoter to transcriptional repressor H-NS. EMBO J 17, 7033-7043.
    • (1998) EMBO J. , vol.17 , pp. 7033-7043
    • Falconi, M.1    Colonna, B.2    Prosseda, G.3    Micheli, G.4    Gualerzi, C.O.5
  • 8
    • 0028198980 scopus 로고
    • Regulation of cholera toxin by temperature, pH, and osmolarity
    • Gardel, C. L. & Mekalanos, J. J. (1994). Regulation of cholera toxin by temperature, pH, and osmolarity. Methods Enzymol 235, 517-526.
    • (1994) Methods Enzymol. , vol.235 , pp. 517-526
    • Gardel, C.L.1    Mekalanos, J.J.2
  • 9
    • 0037020167 scopus 로고    scopus 로고
    • Urea-dependent signal transduction by the virulence regular or UreR
    • Gendlina, I., Gutman, D. M., Thomas, V. & Collins, C. M. (2002). Urea-dependent signal transduction by the virulence regular or UreR. J Biol Chem 277, 37349-37358.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37349-37358
    • Gendlina, I.1    Gutman, D.M.2    Thomas, V.3    Collins, C.M.4
  • 10
    • 0018628289 scopus 로고
    • Urease stones
    • Griffith, D. P. (1979). Urease stones. Urol Res 7, 215-221.
    • (1979) Urol. Res. , vol.7 , pp. 215-221
    • Griffith, D.P.1
  • 11
    • 0017238988 scopus 로고
    • Urease. The primary cause of infection-induced urinary stories
    • Griffith, D. P., Musher, D. M. & Itin, C. (1976). Urease. The primary cause of infection-induced urinary stories. Invest Urol 13, 346-350.
    • (1976) Invest. Urol. , vol.13 , pp. 346-350
    • Griffith, D.P.1    Musher, D.M.2    Itin, C.3
  • 12
    • 0026649243 scopus 로고
    • Temperature regulation of Shigella virulence: Identification of the repressor gene virR, an analogue of hns, and partial complementation by tyrosyl transfer RNA (tRNA1(Tyr))
    • Hromockyj, A. E., Tucker, S. C. & Maurelli, A. T. (1992). Temperature regulation of Shigella virulence: identification of the repressor gene virR, an analogue of hns, and partial complementation by tyrosyl transfer RNA (tRNA1(Tyr)). Mol Microbiol 6, 2113-2124.
    • (1992) Mol. Microbiol. , vol.6 , pp. 2113-2124
    • Hromockyj, A.E.1    Tucker, S.C.2    Maurelli, A.T.3
  • 13
    • 0029564163 scopus 로고
    • Proteus mirabilis urease: Operon fusion and linker insertion analysis of ure gene organization, regulation, and function
    • Island, M. D. & Mobley, H. L. (1995). Proteus mirabilis urease: operon fusion and linker insertion analysis of ure gene organization, regulation, and function. J Bacteriol 177, 5653-5660.
    • (1995) J. Bacteriol. , vol.177 , pp. 5653-5660
    • Island, M.D.1    Mobley, H.L.2
  • 14
    • 0027200202 scopus 로고
    • Contribution of Proteus mirabilis urease to persistence, urolithiasis, and acute pyelonephritis in a mouse model of ascending urinary tract infection
    • Johnson, D. E., Russell, R. G., Lockatell, C. V., Zulty, J. C., Warren, J. W. & Mobley, H. L. (1993). Contribution of Proteus mirabilis urease to persistence, urolithiasis, and acute pyelonephritis in a mouse model of ascending urinary tract infection. Infect Immun 61, 2748-2754.
    • (1993) Infect. Immun. , vol.61 , pp. 2748-2754
    • Johnson, D.E.1    Russell, R.G.2    Lockatell, C.V.3    Zulty, J.C.4    Warren, J.W.5    Mobley, H.L.6
  • 15
    • 0023261608 scopus 로고
    • Genetic and biochemical diversity of ureases of Proteus, Providencia, and Morganella species isolated from urinary tract infection
    • Jones, B. D. & Mobley, H. L. (1987). Genetic and biochemical diversity of ureases of Proteus, Providencia, and Morganella species isolated from urinary tract infection. Infect Immun 55, 2198-2203.
    • (1987) Infect. Immun. , vol.55 , pp. 2198-2203
    • Jones, B.D.1    Mobley, H.L.2
  • 16
    • 0023740010 scopus 로고
    • Proteus mirabilis urease: Genetic organization, regulation, and expression of structural genes
    • Jones, B. D. & Mobley, H. L. (1988). Proteus mirabilis urease: genetic organization, regulation, and expression of structural genes. J Bacteriol 170, 3342-3349.
    • (1988) J. Bacteriol. , vol.170 , pp. 3342-3349
    • Jones, B.D.1    Mobley, H.L.2
  • 17
    • 0025220411 scopus 로고
    • Construction of a urease-negative mutant of Proteus mirabilis: Analysis of virulence in a mouse model of ascending urinary tract infection
    • Jones, B. D., Lockatell, C. V., Johnson, D. E., Warren, J. W. & Mobley, H. L. (1990). Construction of a urease-negative mutant of Proteus mirabilis: analysis of virulence in a mouse model of ascending urinary tract infection. Infect Immun 58, 1120-1123.
    • (1990) Infect. Immun. , vol.58 , pp. 1120-1123
    • Jones, B.D.1    Lockatell, C.V.2    Johnson, D.E.3    Warren, J.W.4    Mobley, H.L.5
  • 18
    • 0022477409 scopus 로고
    • DNA bending at adenine thymine tracts
    • Koo, H. S., Wu, H. M. & Crothers, D. M. (1986). DNA bending at adenine thymine tracts. Nature 320, 501-506.
    • (1986) Nature , vol.320 , pp. 501-506
    • Koo, H.S.1    Wu, H.M.2    Crothers, D.M.3
  • 19
    • 0036137177 scopus 로고    scopus 로고
    • Visualization of Proteus mirabilis within the matrix of urease-induced bladder stones during experimental urinary tract infection
    • Li, X., Zhao, H., Lockatell, C. V., Drachenberg, C. B., Johnson, D. E. & Mobley, H. L. (2002). Visualization of Proteus mirabilis within the matrix of urease-induced bladder stones during experimental urinary tract infection. Infect Immun 70, 389-394.
    • (2002) Infect. Immun. , vol.70 , pp. 389-394
    • Li, X.1    Zhao, H.2    Lockatell, C.V.3    Drachenberg, C.B.4    Johnson, D.E.5    Mobley, H.L.6
  • 20
    • 0028285269 scopus 로고
    • Interactions of the nucleoid-associated DNA-binding protein H-NS with the regulatory region of the osmotically controlled proU operon of Escherichia coli
    • Lucht, J. M., Dersch, P., Kempf, B. & Bremer, E. (1994). Interactions of the nucleoid-associated DNA-binding protein H-NS with the regulatory region of the osmotically controlled proU operon of Escherichia coli. J Biol Chem 269, 6578-6586.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6578-6586
    • Lucht, J.M.1    Dersch, P.2    Kempf, B.3    Bremer, E.4
  • 21
    • 0023991534 scopus 로고
    • Identification of a chromosomal gene controlling temperature-regulated expression of Shigella virulence
    • Maurelli, A. T. & Sansonetti, P. J. (1988). Identification of a chromosomal gene controlling temperature-regulated expression of Shigella virulence. Proc Natl Acad Sci U S A 85, 2820-2824.
    • (1988) Proc. Natl. Acad. Sci. U S A , vol.85 , pp. 2820-2824
    • Maurelli, A.T.1    Sansonetti, P.J.2
  • 22
    • 0032906759 scopus 로고    scopus 로고
    • Isolation of Helicobacter pylori genes that modulate urease activity
    • McGee, D. J., May, C. A., Garner, R. M., Himpsl, J. M. & Mobley, H. L. (1999). Isolation of Helicobacter pylori genes that modulate urease activity. J Bacteriol 181, 2477-2484.
    • (1999) J. Bacteriol. , vol.181 , pp. 2477-2484
    • McGee, D.J.1    May, C.A.2    Garner, R.M.3    Himpsl, J.M.4    Mobley, H.L.5
  • 23
    • 0023892552 scopus 로고
    • A novel suicide vector and its use in construction of insertion mutations: Osmoregulation of outer membrane proteins and virulence determinants in Vibrio cholerae requires toxR
    • Miller, V. L. & Mekalanos, J. J. (1988). A novel suicide vector and its use in construction of insertion mutations: osmoregulation of outer membrane proteins and virulence determinants in Vibrio cholerae requires toxR. J Bacteriol 170, 2575-2583.
    • (1988) J. Bacteriol. , vol.170 , pp. 2575-2583
    • Miller, V.L.1    Mekalanos, J.J.2
  • 24
    • 0023651364 scopus 로고
    • Random cloning of bent DNA segments from Escherichia coli chromosome and primary characterization of their structures
    • Mizuno, T. (1987). Random cloning of bent DNA segments from Escherichia coli chromosome and primary characterization of their structures. Nucleic Acids Res 15, 6827-6841.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 6827-6841
    • Mizuno, T.1
  • 25
    • 0023636563 scopus 로고
    • Urease-positive bacteriuria and obstruction of long-term urinary catheters
    • Mobley, H. L. & Warren, J. W. (1987). Urease-positive bacteriuria and obstruction of long-term urinary catheters. J Clin Microbiol 25, 2216-2217.
    • (1987) J. Clin. Microbiol. , vol.25 , pp. 2216-2217
    • Mobley, H.L.1    Warren, J.W.2
  • 26
    • 0000735263 scopus 로고
    • Virulence determinants of uropathogenic Escherichia coli and Proteus mirabilis
    • Mobley, H. L., Island, M. D. & Massad, G. (1994). Virulence determinants of uropathogenic Escherichia coli and Proteus mirabilis. Kidney Int Suppl 47, S129-S136.
    • (1994) Kidney Int. Suppl. , vol.47
    • Mobley, H.L.1    Island, M.D.2    Massad, G.3
  • 27
    • 0032168436 scopus 로고    scopus 로고
    • Rod models of DNA: Sequence-dependent anisotropic elastic modelling of local bending phenomena
    • Munteanu, M. G., Vlahovicek, K., Parthasarathy, S., Simon, I. & Pongor, S. (1998). Rod models of DNA: sequence-dependent anisotropic elastic modelling of local bending phenomena. Trends Biochem Sci 23, 341-347.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 341-347
    • Munteanu, M.G.1    Vlahovicek, K.2    Parthasarathy, S.3    Simon, I.4    Pongor, S.5
  • 29
    • 0033941006 scopus 로고    scopus 로고
    • Vibrio cholerae H-NS silences virulence gene expression at multiple steps in the ToxR regulatory cascade
    • Nye, M. B., Pfau, J. D., Skorupski, K. & Taylor, R. K. (2000). Vibrio cholerae H-NS silences virulence gene expression at multiple steps in the ToxR regulatory cascade. J Bacteriol 182, 4295-4303.
    • (2000) J. Bacteriol. , vol.182 , pp. 4295-4303
    • Nye, M.B.1    Pfau, J.D.2    Skorupski, K.3    Taylor, R.K.4
  • 30
    • 0026754366 scopus 로고
    • The chromatin-associated protein H-NS interacts with curved DNA to influence DNA topology and gene expression
    • Owen-Hughes, T. A., Pavitt, G. D., Santos, D. S., Sidebotham, J. M., Hulton, C. S., Hinton, J. C. & Higgins, C. F. (1992). The chromatin-associated protein H-NS interacts with curved DNA to influence DNA topology and gene expression. Cell 71, 255-265.
    • (1992) Cell , vol.71 , pp. 255-265
    • Owen-Hughes, T.A.1    Pavitt, G.D.2    Santos, D.S.3    Sidebotham, J.M.4    Hulton, C.S.5    Hinton, J.C.6    Higgins, C.F.7
  • 31
    • 0002972659 scopus 로고
    • Assays of β-galactosidase activity
    • Edited by J. Miller. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory
    • Platt, T., Meuler-Hill, B. & Miller, J. (1972). Assays of β-galactosidase activity. In Experiments in Molecular Genetics. Edited by J. Miller. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory.
    • (1972) Experiments in Molecular Genetics
    • Platt, T.1    Meuler-Hill, B.2    Miller, J.3
  • 32
    • 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. & Mobley, H. L. T. (2001). Identification of the domains of UreR, an AraC-like transcriptional regulator of the urease gene cluster in Proteus mirabilis. J Bacteriol 183, 4526-4535.
    • (2001) J. Bacteriol. , vol.183 , pp. 4526-4535
    • Poore, C.A.1    Coker, C.2    Dattelbaum, J.D.3    Mobley, H.L.T.4
  • 33
    • 0028095884 scopus 로고
    • A role for H-NS in the thermo-osmotic regulation of virulence gene expression in Shigella flexneri
    • Porter, M. E. & Dorman, C. J. (1994). A role for H-NS in the thermo-osmotic regulation of virulence gene expression in Shigella flexneri. J Bacteriol 176, 4187-4191.
    • (1994) J. Bacteriol. , vol.176 , pp. 4187-4191
    • Porter, M.E.1    Dorman, C.J.2
  • 36
    • 0021760528 scopus 로고
    • H1a, an E. coli DNA-binding protein which accumulates in stationary phase, strongly compacts DNA in vitro
    • Spassky, A., Rimsky, S., Garreau, H. & Buc, H. (1984). H1a, an E. coli DNA-binding protein which accumulates in stationary phase, strongly compacts DNA in vitro. Nucleic Acids Res 12, 5321-5340.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 5321-5340
    • Spassky, A.1    Rimsky, S.2    Garreau, H.3    Buc, H.4
  • 37
    • 0030976054 scopus 로고    scopus 로고
    • The oligomeric structure of nucleoid protein H-NS is necessary for recognition of intrinsically curved DNA and for DNA bending
    • Spurio, R., Falconi, M., Brandi, A., Pon, C. L. & Gualerzi, C. O. (1997). The oligomeric structure of nucleoid protein H-NS is necessary for recognition of intrinsically curved DNA and for DNA bending. EMBO J 16, 1795-1805.
    • (1997) EMBO J. , vol.16 , pp. 1795-1805
    • Spurio, R.1    Falconi, M.2    Brandi, A.3    Pon, C.L.4    Gualerzi, C.O.5
  • 38
    • 0033023573 scopus 로고    scopus 로고
    • Identification of UreR binding sites in the Enterobacteriaceae plasmid-encoded and Proteus mirabilis urease gene operons
    • Thomas, V. J. & Collins, C. M. (1999). Identification of UreR binding sites in the Enterobacteriaceae plasmid-encoded and Proteus mirabilis urease gene operons. Mol Microbiol 31, 1417-1428.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1417-1428
    • Thomas, V.J.1    Collins, C.M.2
  • 39
    • 0023771741 scopus 로고
    • Empirical estimation of protein-induced DNA bending angles: Applications to lambda site-specific recombination complexes
    • Thompson, J. F. & Landy, A. (1988). Empirical estimation of protein-induced DNA bending angles: applications to lambda site-specific recombination complexes. Nucleic Acids Res 16, 9687-9705.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 9687-9705
    • Thompson, J.F.1    Landy, A.2
  • 42
    • 0021268779 scopus 로고
    • The locus of sequence-directed and protein-induced DNA bending
    • Wu, H. M. & Crothers, D. M. (1984). The locus of sequence-directed and protein-induced DNA bending. Nature 308, 509-513.
    • (1984) Nature , vol.308 , pp. 509-513
    • Wu, H.M.1    Crothers, D.M.2
  • 43
    • 0026250129 scopus 로고
    • Molecular analysis of the Escherichia coli hns gene encoding a DNA-binding protein, which preferentially recognizes curved DNA sequences
    • Yamada, H., Yoshida, T., Tanaka, K., Sasakawa, C. & Mizuno, T. (1991). Molecular analysis of the Escherichia coli hns gene encoding a DNA-binding protein, which preferentially recognizes curved DNA sequences. Mol Gen Genet 230, 332-336.
    • (1991) Mol. Gen. Genet. , vol.230 , pp. 332-336
    • Yamada, H.1    Yoshida, T.2    Tanaka, K.3    Sasakawa, C.4    Mizuno, T.5
  • 44
    • 0028186679 scopus 로고
    • Improved plasmid vectors for the analysis of protein-induced DNA bending
    • Zwieb, C. & Adhya, S. (1994). Improved plasmid vectors for the analysis of protein-induced DNA bending. Methods Mol Biol 30, 281-294.
    • (1994) Methods Mol. Biol. , vol.30 , pp. 281-294
    • Zwieb, C.1    Adhya, S.2


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