메뉴 건너뛰기




Volumn 182, Issue 4, 2000, Pages 961-966

The TorR high-affinity binding site plays a key role in both torR autoregulation and torCAD operon expression in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

TRIMETHYLAMINE OXIDE;

EID: 0033956361     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.182.4.961-966.2000     Document Type: Article
Times cited : (46)

References (38)
  • 1
    • 0032993401 scopus 로고    scopus 로고
    • TorC apocytochrome negatively autoregulates the trimethylamine N-oxide (TMAO) reductase operon in Escherichia coli
    • Ansaldi, M., C. Bordi, M. Lepelletier, and V. Méjean. 1999. TorC apocytochrome negatively autoregulates the trimethylamine N-oxide (TMAO) reductase operon in Escherichia coli. Mol. Microbiol. 33:284-295.
    • (1999) Mol. Microbiol. , vol.33 , pp. 284-295
    • Ansaldi, M.1    Bordi, C.2    Lepelletier, M.3    Méjean, V.4
  • 2
    • 0021778428 scopus 로고
    • Bacterial reduction of trimethylamine oxide
    • Barrett, E. L., and H. S. Kwan. 1985. Bacterial reduction of trimethylamine oxide. Annu. Rev. Microbiol. 39:131-149.
    • (1985) Annu. Rev. Microbiol. , vol.39 , pp. 131-149
    • Barrett, E.L.1    Kwan, H.S.2
  • 3
    • 0032573575 scopus 로고    scopus 로고
    • Molecular analysis of the trimethylamine N-oxide (TMAO) reductase respiratory system from a Shewanella species
    • Dos Santos, J. P., C. Iobbi-Nivol, C. Couillault, G. Giordano, and V. Méjean. 1998. Molecular analysis of the trimethylamine N-oxide (TMAO) reductase respiratory system from a Shewanella species. J. Mol. Biol. 284:421-433.
    • (1998) J. Mol. Biol. , vol.284 , pp. 421-433
    • Dos Santos, J.P.1    Iobbi-Nivol, C.2    Couillault, C.3    Giordano, G.4    Méjean, V.5
  • 4
    • 0032911194 scopus 로고    scopus 로고
    • Mutational analysis of the phoD promoter in Bacillus subtilis: Implications for PhoP binding and promoter activation of Pho regulon promoters
    • Eder, S., W. Liu, and F. M. Hulett. 1999. Mutational analysis of the phoD promoter in Bacillus subtilis: implications for PhoP binding and promoter activation of Pho regulon promoters. J. Bacteriol. 181:2017-2025.
    • (1999) J. Bacteriol. , vol.181 , pp. 2017-2025
    • Eder, S.1    Liu, W.2    Hulett, F.M.3
  • 5
    • 0032433253 scopus 로고    scopus 로고
    • Electroporation of freshly plated Escherichia coli and Pseudomonas aeruginosa cells
    • Enderle, P. J., and M. A. Farwell. 1998. Electroporation of freshly plated Escherichia coli and Pseudomonas aeruginosa cells. BioTechniques 25:954-958.
    • (1998) BioTechniques , vol.25 , pp. 954-958
    • Enderle, P.J.1    Farwell, M.A.2
  • 6
    • 0026648033 scopus 로고
    • Anaerobic control of colicin E1 production
    • Eraso, J. M., and G. M. Weinstock. 1992. Anaerobic control of colicin E1 production. J. Bacteriol. 174:5101-5109.
    • (1992) J. Bacteriol. , vol.174 , pp. 5101-5109
    • Eraso, J.M.1    Weinstock, G.M.2
  • 7
    • 0032034821 scopus 로고    scopus 로고
    • Signal tranduction in bacteria: Molecular mechanisms of stimulus-response coupling
    • Goudreau, P. N., and A. M. Stock. 1998. Signal tranduction in bacteria: molecular mechanisms of stimulus-response coupling. Curr. Opin. Microbiol. 2:160-169.
    • (1998) Curr. Opin. Microbiol. , vol.2 , pp. 160-169
    • Goudreau, P.N.1    Stock, A.M.2
  • 8
    • 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
  • 10
    • 0032483501 scopus 로고    scopus 로고
    • Relative binding affinities of OmpR and OmpR-phosphate at the ompF and ompC regulatory sites
    • Head, C. G., A. Tardy, and L. J. Kenney. 1998. Relative binding affinities of OmpR and OmpR-phosphate at the ompF and ompC regulatory sites. J. Mol. Biol. 281:857-870.
    • (1998) J. Mol. Biol. , vol.281 , pp. 857-870
    • Head, C.G.1    Tardy, A.2    Kenney, L.J.3
  • 11
    • 0032489504 scopus 로고    scopus 로고
    • Protein-protein contacts that activate and repress prokaryotic transcription
    • Hochschild, A., and S. L. Dove. 1998. Protein-protein contacts that activate and repress prokaryotic transcription. Cell 92:597-600.
    • (1998) Cell , vol.92 , pp. 597-600
    • Hochschild, A.1    Dove, S.L.2
  • 12
    • 0030580087 scopus 로고    scopus 로고
    • Identification of the bases in the ompF regulatory region, which interact with the transcription factor OmpR
    • Huang, K. J., and M. M. Igo. 1996. Identification of the bases in the ompF regulatory region, which interact with the transcription factor OmpR. J. Mol. Biol. 262:615-628.
    • (1996) J. Mol. Biol. , vol.262 , pp. 615-628
    • Huang, K.J.1    Igo, M.M.2
  • 13
    • 0030940341 scopus 로고    scopus 로고
    • Phosphorylation stimulates the cooperative DNA-binding properties of the transcription factor OmpR
    • Huang, K. J., C. Y. Lan, and M. M. Igo. 1997. Phosphorylation stimulates the cooperative DNA-binding properties of the transcription factor OmpR. Proc. Natl. Acad. Sci. USA 94:2828-2832.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2828-2832
    • Huang, K.J.1    Lan, C.Y.2    Igo, M.M.3
  • 14
    • 0031564650 scopus 로고    scopus 로고
    • Transphosphorylation of the TorR response regulator requires the three phosphorylation sites of the TorS unorthodox sensor in Escherichia coli
    • Jourlin, C., M. Ansaldi, and V. Méjean. 1997. Transphosphorylation of the TorR response regulator requires the three phosphorylation sites of the TorS unorthodox sensor in Escherichia coli. J. Mol. Biol. 267:770-777.
    • (1997) J. Mol. Biol. , vol.267 , pp. 770-777
    • Jourlin, C.1    Ansaldi, M.2    Méjean, V.3
  • 15
    • 0029941952 scopus 로고    scopus 로고
    • An unorthodox sensor protein (TorS) mediates the induction of the tor structural genes in response to trimethylamine N-oxide in Escherichia coli
    • Jourlin, C., A. Bengrine, M. Chippaux, and V. Méjean. 1996. An unorthodox sensor protein (TorS) mediates the induction of the tor structural genes in response to trimethylamine N-oxide in Escherichia coli. Mol. Microbiol. 20:1297-1306.
    • (1996) Mol. Microbiol. , vol.20 , pp. 1297-1306
    • Jourlin, C.1    Bengrine, A.2    Chippaux, M.3    Méjean, V.4
  • 16
    • 0030058278 scopus 로고    scopus 로고
    • The periplasmic TorT protein is required for trimethylamine N-oxide reductase gene induction in Escherichia coli
    • Jourlin, C., G. Simon, J. Pommier, M. Chippaux, and V. Méjean. 1996. The periplasmic TorT protein is required for trimethylamine N-oxide reductase gene induction in Escherichia coli. J. Bacteriol. 178:1219-1223.
    • (1996) J. Bacteriol. , vol.178 , pp. 1219-1223
    • Jourlin, C.1    Simon, G.2    Pommier, J.3    Chippaux, M.4    Méjean, V.5
  • 17
    • 0031027087 scopus 로고    scopus 로고
    • Escherichia coli positive regulator OmpR has a large loop structure at the putative RNA polymerase interaction site
    • Kondo, H., A. Nakagawa, J. Nishihira, Y. Nishimura, T. Mizuno, and I. Tanaka. 1997. Escherichia coli positive regulator OmpR has a large loop structure at the putative RNA polymerase interaction site. Nat. Struct. Biol. 4:28-31.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 28-31
    • Kondo, H.1    Nakagawa, A.2    Nishihira, J.3    Nishimura, Y.4    Mizuno, T.5    Tanaka, I.6
  • 18
    • 0022921901 scopus 로고
    • Mutations in a new chromosomal gene of Escherichia coli K-12, pcnB, reduce plasmid copy number of pBR322 and its derivatives
    • Lopilato, J., S. Bortner, and J. Beckwith. 1986. Mutations in a new chromosomal gene of Escherichia coli K-12, pcnB, reduce plasmid copy number of pBR322 and its derivatives. Mol. Gen. Genet. 205:285-290.
    • (1986) Mol. Gen. Genet. , vol.205 , pp. 285-290
    • Lopilato, J.1    Bortner, S.2    Beckwith, J.3
  • 20
    • 0027500344 scopus 로고
    • Autogenous regulation of gene expression
    • Maloy, S., and V. Stewart. 1993. Autogenous regulation of gene expression. J. Bacteriol. 175:307-316.
    • (1993) J. Bacteriol. , vol.175 , pp. 307-316
    • Maloy, S.1    Stewart, V.2
  • 21
    • 0031566431 scopus 로고    scopus 로고
    • Structural relationships in the OmpR family of winged-helix transcription factors
    • Martinez-Hackert, E., and A. M. Stock. 1997. Structural relationships in the OmpR family of winged-helix transcription factors. J. Mol. Biol. 269:301-312.
    • (1997) J. Mol. Biol. , vol.269 , pp. 301-312
    • Martinez-Hackert, E.1    Stock, A.M.2
  • 23
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • Miller, J. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.1
  • 24
    • 0031589010 scopus 로고    scopus 로고
    • Compilation of all genes encoding two-component phosphotransfer signal transducers in the genome of Escherichia coli
    • Mizuno, T. 1997. Compilation of all genes encoding two-component phosphotransfer signal transducers in the genome of Escherichia coli. DNA Res. 4:161-168.
    • (1997) DNA Res. , vol.4 , pp. 161-168
    • Mizuno, T.1
  • 25
    • 0032454788 scopus 로고    scopus 로고
    • Cascade regulation of dimethyl sulfoxide reductase (dor) gene expression in the facultative phototroph Rhodobacter sphaeroides 2.4.1T
    • Mouncey, N. J., and S. Kaplan. 1998. Cascade regulation of dimethyl sulfoxide reductase (dor) gene expression in the facultative phototroph Rhodobacter sphaeroides 2.4.1T. J. Bacteriol. 180:2924-2930.
    • (1998) J. Bacteriol. , vol.180 , pp. 2924-2930
    • Mouncey, N.J.1    Kaplan, S.2
  • 26
    • 0032034820 scopus 로고    scopus 로고
    • Some repressors of bacterial transcription
    • Müller-Hill, B. 1998. Some repressors of bacterial transcription. Curr. Opin. Microbiol. 1:145-151.
    • (1998) Curr. Opin. Microbiol. , vol.1 , pp. 145-151
    • Müller-Hill, B.1
  • 27
    • 0027056677 scopus 로고
    • Communication modules in bacterial signaling proteins
    • Parkinson, J. S., and E. C. Kofoid. 1992. Communication modules in bacterial signaling proteins. Annu. Rev. Genet. 26:71-112.
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 71-112
    • Parkinson, J.S.1    Kofoid, E.C.2
  • 28
    • 0032568823 scopus 로고    scopus 로고
    • TorD, a cytoplasmic chaperone that interacts with the unfolded trimethylamine N-oxide reductase enzyme (TorA) in Escherichia coli
    • Pommier, J., V. Méjean, G. Giordano, and C. Iobbi-Nivol. 1998. TorD, a cytoplasmic chaperone that interacts with the unfolded trimethylamine N-oxide reductase enzyme (TorA) in Escherichia coli. J. Biol. Chem. 273: 16615-16620.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16615-16620
    • Pommier, J.1    Méjean, V.2    Giordano, G.3    Iobbi-Nivol, C.4
  • 29
    • 0001427734 scopus 로고
    • Porin regulon of Escherichia coli, p. 105-127
    • J. A. Hoch and T. J. Silhavy (ed.), ASM Press, Washington, D.C.
    • Pratt, L. A., and T. J. Silhavy. 1995. Porin regulon of Escherichia coli, p. 105-127. In J. A. Hoch and T. J. Silhavy (ed.), Two-component signal transduction. ASM Press, Washington, D.C.
    • (1995) Two-component Signal Transduction
    • Pratt, L.A.1    Silhavy, T.J.2
  • 30
    • 0028222516 scopus 로고
    • The OmpR protein of Escherichia coli binds to sites in the ompF promoter region in a hierarchical manner determined by its degree of phosphorylation
    • Rampersaud, A., S. L. Harlocker, and M. Inouye. 1994. The OmpR protein of Escherichia coli binds to sites in the ompF promoter region in a hierarchical manner determined by its degree of phosphorylation. J. Biol. Chem. 269:12559-12566.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12559-12566
    • Rampersaud, A.1    Harlocker, S.L.2    Inouye, M.3
  • 31
    • 0032035329 scopus 로고    scopus 로고
    • Positive activation of gene expression
    • Rhodius, V. A., and S. J. Busby. 1998. Positive activation of gene expression. Curr. Opin. Microbiol. 1:152-159.
    • (1998) Curr. Opin. Microbiol. , vol.1 , pp. 152-159
    • Rhodius, V.A.1    Busby, S.J.2
  • 32
    • 0032955002 scopus 로고    scopus 로고
    • Repression of transcription initiation in bacteria
    • Rojo, F. 1999. Repression of transcription initiation in bacteria. J. Bacteriol. 181:2987-2991.
    • (1999) J. Bacteriol. , vol.181 , pp. 2987-2991
    • Rojo, F.1
  • 34
    • 0028862516 scopus 로고
    • Binding of the TorR regulator to cis-acting direct repeats activates tor operon expression
    • Simon, G., C. Jourlin, M. Ansaldi, M. C. Pascal, M. Chippaux, and V. Méjean. 1995. Binding of the TorR regulator to cis-acting direct repeats activates tor operon expression. Mol. Microbiol. 17:971-980.
    • (1995) Mol. Microbiol. , vol.17 , pp. 971-980
    • Simon, G.1    Jourlin, C.2    Ansaldi, M.3    Pascal, M.C.4    Chippaux, M.5    Méjean, V.6
  • 35
    • 0027959266 scopus 로고
    • The torR gene of Escherichia coli encodes a response regulator protein involved in the expression of the trimethylamine N-oxide reductase
    • Simon, G., V. Méjean, C. Jourlin, M. Chippaux, and M. C. Pascal. 1994. The torR gene of Escherichia coli encodes a response regulator protein involved in the expression of the trimethylamine N-oxide reductase. J. Bacteriol. 176:5601-5606.
    • (1994) J. Bacteriol. , vol.176 , pp. 5601-5606
    • Simon, G.1    Méjean, V.2    Jourlin, C.3    Chippaux, M.4    Pascal, M.C.5
  • 36
    • 0029116605 scopus 로고
    • Transcriptional autoregulation of the Salmonella typhimurium phoPQ operon
    • Soncini, F. C., E. G. Vescovi, and E. A. Groisman. 1995. Transcriptional autoregulation of the Salmonella typhimurium phoPQ operon. J. Bacteriol. 177:4364-4371.
    • (1995) J. Bacteriol. , vol.177 , pp. 4364-4371
    • Soncini, F.C.1    Vescovi, E.G.2    Groisman, E.A.3
  • 37
    • 0030762556 scopus 로고    scopus 로고
    • A naturally occurring protective system in urea-rich cells: Mechanism of osmolyte protection of proteins against urea denaturation
    • Wang, A., and D. W. Bolen. 1997. A naturally occurring protective system in urea-rich cells: mechanism of osmolyte protection of proteins against urea denaturation. Biochemistry 36:9101-9108.
    • (1997) Biochemistry , vol.36 , pp. 9101-9108
    • Wang, A.1    Bolen, D.W.2
  • 38
    • 0030929313 scopus 로고    scopus 로고
    • A novel family of proteins that regulates antibiotic production in streptomycetes appears to contain an OmpR-like DNA-binding fold
    • Wietzorrek, A., and M. Bibb. 1997. A novel family of proteins that regulates antibiotic production in streptomycetes appears to contain an OmpR-like DNA-binding fold. Mol. Microbiol. 25:1181-1184.
    • (1997) Mol. Microbiol. , vol.25 , pp. 1181-1184
    • Wietzorrek, A.1    Bibb, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.