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Volumn 215, Issue 2, 1998, Pages 303-310

The ihfmRNA levels decline as Neisseria gonorrhoeae enters the stationary growth phase

Author keywords

Integration host factor; Neisseria; Transcription

Indexed keywords

DNA BINDING PROTEIN; INTEGRATION HOST FACTOR; MESSENGER RNA; POLYPEPTIDE; TRANSCRIPTION FACTOR; BACTERIAL PROTEIN; RECOMBINANT PROTEIN;

EID: 0032581272     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(98)00285-6     Document Type: Article
Times cited : (7)

References (21)
  • 2
    • 0028149835 scopus 로고
    • Expression of the genes coding for the Escherichia coli integration host factor are controlled by growth phase, rpoS, ppGpp and by autoregulation
    • Aviv, M., Giladi, H., Schreiber, G., Oppenheim, A.B., Glaser, G., 1994. Expression of the genes coding for the Escherichia coli integration host factor are controlled by growth phase, rpoS, ppGpp and by autoregulation. Mol. Microbiol. 14, 1021-1031.
    • (1994) Mol. Microbiol. , vol.14 , pp. 1021-1031
    • Aviv, M.1    Giladi, H.2    Schreiber, G.3    Oppenheim, A.B.4    Glaser, G.5
  • 3
    • 0021163783 scopus 로고
    • Mutagenesis of Neiseria gonorrhoeae: Absence of error-prone repair
    • Campbell, L.A., Yasbin, R.E., 1984. Mutagenesis of Neiseria gonorrhoeae: absence of error-prone repair. J. Bacteriol. 160, 288-293.
    • (1984) J. Bacteriol. , vol.160 , pp. 288-293
    • Campbell, L.A.1    Yasbin, R.E.2
  • 4
    • 0021710080 scopus 로고
    • E. coli integration host factor binds to specific sites in DNA
    • Craig, N.L., Nash, H.A., 1984. E. coli integration host factor binds to specific sites in DNA. Cell 39, 707-716.
    • (1984) Cell , vol.39 , pp. 707-716
    • Craig, N.L.1    Nash, H.A.2
  • 5
    • 0028307609 scopus 로고
    • Growth phase variation of integration host factor levels in Escherichia coli
    • Ditto, M.D., Roberts, D., Weisberg, R.A., 1994. Growth phase variation of integration host factor levels in Escherichia coli. J. Bacteriol. 175, 3738-3748.
    • (1994) J. Bacteriol. , vol.175 , pp. 3738-3748
    • Ditto, M.D.1    Roberts, D.2    Weisberg, R.A.3
  • 6
    • 0023413620 scopus 로고
    • Histone-like proteins of bacteria
    • Drlica, K., Rouviere-Yaniv, J., 1987. Histone-like proteins of bacteria. Microbiol. Rev. 51, 301-319.
    • (1987) Microbiol. Rev. , vol.51 , pp. 301-319
    • Drlica, K.1    Rouviere-Yaniv, J.2
  • 7
    • 0022204793 scopus 로고
    • Primary structure of the hip gene of E. coli and of its product, the β subunit of integration host factor
    • Flamm, E.L., Weisberg, R.A., 1985. Primary structure of the hip gene of E. coli and of its product, the β subunit of integration host factor. J. Mol. Biol. 183, 117-128.
    • (1985) J. Mol. Biol. , vol.183 , pp. 117-128
    • Flamm, E.L.1    Weisberg, R.A.2
  • 8
    • 0024291348 scopus 로고
    • Integration host factor: A protein for all reasons
    • Friedman, D.I., 1988. Integration host factor: a protein for all reasons. Cell 55, 545-554.
    • (1988) Cell , vol.55 , pp. 545-554
    • Friedman, D.I.1
  • 11
    • 0001948633 scopus 로고
    • Molecular Cloning
    • Cold Spring Harbor Laboratory, Cold Springer Harbor, NY
    • Maniatis, T., Fritsche, E.F., Sambrook, J., 1982. Molecular Cloning. A Laboratory Manual. Cold Spring Harbor Laboratory, Cold Springer Harbor, NY.
    • (1982) A Laboratory Manual
    • Maniatis, T.1    Fritsche, E.F.2    Sambrook, J.3
  • 12
    • 0023645583 scopus 로고
    • phe-dependent attenuation and transcriptional operator-repressor control by himA and the SOS network
    • phe-dependent attenuation and transcriptional operator-repressor control by himA and the SOS network. 1987. J. Mol. Biol. 197, 453-470.
    • (1987) J. Mol. Biol. , vol.197 , pp. 453-470
    • Mechulam, Y.1    Blankquet, S.2    Fayat, G.3
  • 13
    • 0021646254 scopus 로고
    • Primary structure of the himA gene of E. coli: Homology with DNA binding protein HU and association with the phenylalanyl tRNA synthetase operon
    • Miller, H.I., 1984. Primary structure of the himA gene of E. coli: homology with DNA binding protein HU and association with the phenylalanyl tRNA synthetase operon. Cold Spring Harbor Symp. Quant. Biol. 49, 691-698.
    • (1984) Cold Spring Harbor Symp. Quant. Biol. , vol.49 , pp. 691-698
    • Miller, H.I.1
  • 14
    • 0019822504 scopus 로고
    • SOS induction and autoregulation of the himA gene for site-specific recombination in Escherichia coli
    • Miller, H.I., Kirk, M., Echols, H., 1981. SOS induction and autoregulation of the himA gene for site-specific recombination in Escherichia coli. Proc. Natl. Acad. Sci. USA 78, 6754-6758.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 6754-6758
    • Miller, H.I.1    Kirk, M.2    Echols, H.3
  • 15
    • 0002480960 scopus 로고    scopus 로고
    • The HU and IHF proteins: Accessory factors for complex protein-DNA assemblies
    • R.G. Landes, Austin, TX
    • Nash, H.A., 1996. The HU and IHF proteins: accessory factors for complex protein-DNA assemblies. Regulation of gene expression in Escherichia coli. R.G. Landes, Austin, TX.
    • (1996) Regulation of Gene Expression in Escherichia Coli
    • Nash, H.A.1
  • 16
    • 0028298256 scopus 로고
    • Promoters responsive to DNA bending: A common theme in prokaryotic gene expression
    • Perez-Martin, J., Rojo, F., de Lorenzo, V., 1994. Promoters responsive to DNA bending: a common theme in prokaryotic gene expression. Microbiol. Rev. 58, 268-290.
    • (1994) Microbiol. Rev. , vol.58 , pp. 268-290
    • Perez-Martin, J.1    Rojo, F.2    De Lorenzo, V.3
  • 17
    • 0023833241 scopus 로고
    • Bending of the bacteriophage λ attachment site by Escherichia coli integration shot factor
    • Robertson, C.A., Nash, H.A., 1988. Bending of the bacteriophage λ attachment site by Escherichia coli integration shot factor. J. Biol. Chem. 263, 3554-3557.
    • (1988) J. Biol. Chem. , vol.263 , pp. 3554-3557
    • Robertson, C.A.1    Nash, H.A.2
  • 19
    • 0019997588 scopus 로고
    • Colony opacity and protein II compositions of gonococci
    • Swanson, J., 1982. Colony opacity and protein II compositions of gonococci. Infect. Immun. 37, 359-368.
    • (1982) Infect. Immun. , vol.37 , pp. 359-368
    • Swanson, J.1
  • 20
    • 0027358806 scopus 로고
    • Purification of the integration host factor homolog of Rhodobacter capsulatus: Cloning and sequencing of the hip gene, which encodes the β subunit
    • Toussaint, B., Delic-Attree, I., de Sury D'Aspremont, R., David, L., Vincon, M., Vignais, P.M., 1993. Purification of the integration host factor homolog of Rhodobacter capsulatus: cloning and sequencing of the hip gene, which encodes the β subunit. J. Bacteriol. 175, 6499-6504.
    • (1993) J. Bacteriol. , vol.175 , pp. 6499-6504
    • Toussaint, B.1    Delic-Attree, I.2    De Sury D'Aspremont, R.3    David, L.4    Vincon, M.5    Vignais, P.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.