메뉴 건너뛰기




Volumn 180, Issue 22, 1998, Pages 5932-5946

Identification and characterization of the fis operon in enteric bacteria

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL DNA; BETA GALACTOSIDASE; DNA BINDING PROTEIN; INTEGRATION HOST FACTOR; RECOMBINASE;

EID: 0031733414     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.22.5932-5946.1998     Document Type: Article
Times cited : (39)

References (57)
  • 2
    • 0031893742 scopus 로고    scopus 로고
    • Activation of Escherichia coli rRNA transcription by FIS during a growth cycle
    • Appleman, J. A., W. Ross, J. Salomon, and R. L. Gourse. 1998. Activation of Escherichia coli rRNA transcription by FIS during a growth cycle. J. Bacteriol. 180:1525-1532.
    • (1998) J. Bacteriol. , vol.180 , pp. 1525-1532
    • Appleman, J.A.1    Ross, W.2    Salomon, J.3    Gourse, R.L.4
  • 3
    • 0025766646 scopus 로고
    • Efficient excision of phage lambda from the Escherichia coli chromosome requires the Fis protein
    • Ball, C. A., and R. C. Johnson. 1991. Efficient excision of phage lambda from the Escherichia coli chromosome requires the Fis protein. J. Bacteriol. 173: 4027-4031.
    • (1991) J. Bacteriol. , vol.173 , pp. 4027-4031
    • Ball, C.A.1    Johnson, R.C.2
  • 4
    • 0025740394 scopus 로고
    • Multiple effects of Fis on integration and the control of lysogeny in phage λ
    • Ball, C. A., and R. C. Johnson. 1991. Multiple effects of Fis on integration and the control of lysogeny in phage λ. J. Bacteriol. 173:4032-4038.
    • (1991) J. Bacteriol. , vol.173 , pp. 4032-4038
    • Ball, C.A.1    Johnson, R.C.2
  • 5
    • 0026620949 scopus 로고
    • Dramatic changes in Fis levels upon nutrient upshift in Escherichia coli
    • Ball, C. A., R. Osuna, K. C. Ferguson, and R. C. Johnson. 1992. Dramatic changes in Fis levels upon nutrient upshift in Escherichia coli. J. Bacteriol. 174:8043-8056.
    • (1992) J. Bacteriol. , vol.174 , pp. 8043-8056
    • Ball, C.A.1    Osuna, R.2    Ferguson, K.C.3    Johnson, R.C.4
  • 6
    • 0023427154 scopus 로고
    • Fis binding to the recombinational enhancer of the Hin DNA inversion system
    • Bruist, M. F., A. C. Glasgow, R. C. Johnson, and M. I. Simon. 1987. Fis binding to the recombinational enhancer of the Hin DNA inversion system. Genes Dev. 1:762-772.
    • (1987) Genes Dev. , vol.1 , pp. 762-772
    • Bruist, M.F.1    Glasgow, A.C.2    Johnson, R.C.3    Simon, M.I.4
  • 7
    • 0021258949 scopus 로고
    • Phase variation and the Hin protein: In vivo activity measurements, protein overproduction and purification
    • Bruist, M. F., and M. I. Simon. 1984. Phase variation and the Hin protein: in vivo activity measurements, protein overproduction and purification. J. Bacteriol. 159:71-79.
    • (1984) J. Bacteriol. , vol.159 , pp. 71-79
    • Bruist, M.F.1    Simon, M.I.2
  • 8
    • 0024213092 scopus 로고
    • Analysis of the promoters and transcripts involved in IS10 anti-sense transcriptional RNA control
    • Case, C. C., S. M. Roels, J. E. Gonzalez, E. Simons, and R. Simons. 1988. Analysis of the promoters and transcripts involved in IS10 anti-sense transcriptional RNA control. Gene 72:219-236.
    • (1988) Gene , vol.72 , pp. 219-236
    • Case, C.C.1    Roels, S.M.2    Gonzalez, J.E.3    Simons, E.4    Simons, R.5
  • 9
    • 0031576352 scopus 로고    scopus 로고
    • Variation in HU composition during growth of Escherichia coli: The heterodimer is required for long term survival
    • Claret, L., and J. Rouviere-Yaniv. 1997. Variation in HU composition during growth of Escherichia coli: the heterodimer is required for long term survival. J. Mol. Biol. 273:93-104.
    • (1997) J. Mol. Biol. , vol.273 , pp. 93-104
    • Claret, L.1    Rouviere-Yaniv, J.2
  • 10
    • 0021710080 scopus 로고
    • E. coli integration host factor binds to specific sites in DNA
    • Craig, N. L., and H. A. Nash. 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
  • 11
    • 0028307609 scopus 로고
    • Growth phase variation of integration host factor level in Escherichia coli
    • Ditto, M. D., D. Roberts, and R. A. Weisberg. 1994. Growth phase variation of integration host factor level in Escherichia coli. J. Bacteriol. 176:3738-3748.
    • (1994) J. Bacteriol. , vol.176 , pp. 3738-3748
    • Ditto, M.D.1    Roberts, D.2    Weisberg, R.A.3
  • 12
    • 0023413620 scopus 로고
    • Histonelike proteins of bacteria
    • Drlica, K., and J. Rouviere-Yaniv. 1987. Histonelike proteins of bacteria. Microbiol. Rev. 51:301-319.
    • (1987) Microbiol. Rev. , vol.51 , pp. 301-319
    • Drlica, K.1    Rouviere-Yaniv, J.2
  • 13
    • 0029880342 scopus 로고    scopus 로고
    • Antagonistic involvement of FIS and H-NS proteins in the transcriptional control of hns expression
    • Falconi, M., A. Brandi, A. L. Teana, C. O. Gualerzi, and C. L. Pon. 1996. Antagonistic involvement of FIS and H-NS proteins in the transcriptional control of hns expression. Mol. Microbiol. 19:965-975.
    • (1996) Mol. Microbiol. , vol.19 , pp. 965-975
    • Falconi, M.1    Brandi, A.2    Teana, A.L.3    Gualerzi, C.O.4    Pon, C.L.5
  • 14
    • 9544231340 scopus 로고
    • The interaction of Fis protein with its DNA-binding sequences
    • R. H. Sarma, and M. H. Sarma (ed.), Proteins. Adenine Press, Schenectady, N.Y.
    • Feng, J.-A., H. S. Yuan, S. E. Finkel, R. C. Johnson, M. Kaczor-Grzeskowiac, and R. E. Dickerson. 1992. The interaction of Fis protein with its DNA-binding sequences, p. 1-9. In R. H. Sarma, and M. H. Sarma (ed.), Structure and function, vol. 2. Proteins. Adenine Press, Schenectady, N.Y.
    • (1992) Structure and Function , vol.2 , pp. 1-9
    • Feng, J.-A.1    Yuan, H.S.2    Finkel, S.E.3    Johnson, R.C.4    Kaczor-Grzeskowiac, M.5    Dickerson, R.E.6
  • 15
    • 0026527078 scopus 로고
    • Involvement of Fis protein in replication of the Escherichia coli chromosome
    • Filutowicz, M., W. Ross, J. Wild, and R. L. Gourse. 1992. Involvement of Fis protein in replication of the Escherichia coli chromosome. J. Bacteriol. 174: 398-407.
    • (1992) J. Bacteriol. , vol.174 , pp. 398-407
    • Filutowicz, M.1    Ross, W.2    Wild, J.3    Gourse, R.L.4
  • 16
    • 0026470852 scopus 로고
    • The Fis protein: It's not just for DNA inversion anymore
    • Finkel, S. E., and R. C. Johnson. 1992. The Fis protein: it's not just for DNA inversion anymore. Mol. Microbiol. 6:3257-3265.
    • (1992) Mol. Microbiol. , vol.6 , pp. 3257-3265
    • Finkel, S.E.1    Johnson, R.C.2
  • 17
    • 0027281171 scopus 로고
    • Sequence, genetic, and lacZ fusion analyses of a nifR3-ntrB-ntrC operon in Rhodobacter capsulatus
    • Foster-Hartnett, D., K. K. Gabbert, P. J. Cullen, and R. G. Kranz. 1993. Sequence, genetic, and lacZ fusion analyses of a nifR3-ntrB-ntrC operon in Rhodobacter capsulatus. Mol. Microbiol. 8:903-914.
    • (1993) Mol. Microbiol. , vol.8 , pp. 903-914
    • Foster-Hartnett, D.1    Gabbert, K.K.2    Cullen, P.J.3    Kranz, R.G.4
  • 18
    • 0028825080 scopus 로고
    • Coupling of Escherichia coli hns mRNA levels to DNA synthesis by autoregulation: Implications for growth phase control
    • Free, A., and C. J. Dorman. 1995. Coupling of Escherichia coli hns mRNA levels to DNA synthesis by autoregulation: implications for growth phase control. Mol. Microbiol. 18:101-113.
    • (1995) Mol. Microbiol. , vol.18 , pp. 101-113
    • Free, A.1    Dorman, C.J.2
  • 19
    • 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
  • 20
    • 0025180835 scopus 로고
    • Searching for and predicting the activity of sites for DNA binding proteins: Compilation and analysis of the binding sites for Escherichia coli integration host factor (IHF)
    • Goodrich, J. A., M. L. Schwartz, and W. R. McClure. 1990. Searching for and predicting the activity of sites for DNA binding proteins: compilation and analysis of the binding sites for Escherichia coli integration host factor (IHF). Nucleic Acids Res. 18:4993-5000.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 4993-5000
    • Goodrich, J.A.1    Schwartz, M.L.2    McClure, W.R.3
  • 21
    • 0028922082 scopus 로고
    • The regulation of transcriptional initiation by integration host factor
    • Goosen, N., and P. Van de Putte. 1995. The regulation of transcriptional initiation by integration host factor. Mol. Microbiol. 16:1-7.
    • (1995) Mol. Microbiol. , vol.16 , pp. 1-7
    • Goosen, N.1    Van De Putte, P.2
  • 22
    • 0029813128 scopus 로고    scopus 로고
    • A positive control mutant of the transcription activator protein FIS
    • Gosink, K. K., T. Gaal, A. J. Bokal IV, and R. L. Gourse. 1996. A positive control mutant of the transcription activator protein FIS. J. Bacteriol. 178: 5181-5187.
    • (1996) J. Bacteriol. , vol.178 , pp. 5181-5187
    • Gosink, K.K.1    Gaal, T.2    Bokal IV, A.J.3    Gourse, R.L.4
  • 23
    • 0027526353 scopus 로고
    • DNA binding and bending are necessary but not sufficient for Fis-dependent activation of rrnB P1
    • Gosink, K. K., W. Ross, S. Leirmo, R. Osuna, S. E. Finkel, R. C. Johnson, and R. L. Gourse. 1993. DNA binding and bending are necessary but not sufficient for Fis-dependent activation of rrnB P1. J. Bacteriol. 175:1580-1589.
    • (1993) J. Bacteriol. , vol.175 , pp. 1580-1589
    • Gosink, K.K.1    Ross, W.2    Leirmo, S.3    Osuna, R.4    Finkel, S.E.5    Johnson, R.C.6    Gourse, R.L.7
  • 24
    • 0024252185 scopus 로고
    • Extension inhibition analysis of translation initiation complexes
    • Hartz, D., D. S. McPheeters, R. Traut, and L. Gold. 1988. Extension inhibition analysis of translation initiation complexes. Methods Enzymol. 164: 419-425.
    • (1988) Methods Enzymol. , vol.164 , pp. 419-425
    • Hartz, D.1    McPheeters, D.S.2    Traut, R.3    Gold, L.4
  • 25
    • 0023693199 scopus 로고
    • Isolation of the gene encoding the Hin recombinational enhancer binding protein
    • Johnson, R. C., C. A. Ball, D. Pfeiffer, and M. I. Simon. 1988. Isolation of the gene encoding the Hin recombinational enhancer binding protein. Proc. Natl. Acad. Sci. USA 85:3484-3488.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3484-3488
    • Johnson, R.C.1    Ball, C.A.2    Pfeiffer, D.3    Simon, M.I.4
  • 26
    • 0022545522 scopus 로고
    • Host protein requirements for in vitro site-specific DNA inversion
    • Johnson, R. C., M. F. Bruist, and M. I. Simon. 1986. Host protein requirements for in vitro site-specific DNA inversion. Cell 46:531-539.
    • (1986) Cell , vol.46 , pp. 531-539
    • Johnson, R.C.1    Bruist, M.F.2    Simon, M.I.3
  • 27
    • 0022006792 scopus 로고
    • Hin-mediated site-specific recombination requires two 26 bp recombination sites and a 60 bp recombinational enhancer
    • Johnson, R. C., and M. I. Simon. 1985. Hin-mediated site-specific recombination requires two 26 bp recombination sites and a 60 bp recombinational enhancer. Cell 41:781-791.
    • (1985) Cell , vol.41 , pp. 781-791
    • Johnson, R.C.1    Simon, M.I.2
  • 28
    • 0020196971 scopus 로고
    • Control of Tn5 transposition in Escherichia coli is mediated by protein from the right repeat
    • Johnson, R. C., J. C. P. Yin, and W. S. Reznikoff. 1982. Control of Tn5 transposition in Escherichia coli is mediated by protein from the right repeat. Cell 30:873-882.
    • (1982) Cell , vol.30 , pp. 873-882
    • Johnson, R.C.1    Yin, J.C.P.2    Reznikoff, W.S.3
  • 29
    • 0025950160 scopus 로고
    • The N-terminal part of the E. coli DNA binding protein Fis is essential for stimulating site-specific DNA inversion but is not required for specific DNA binding
    • Koch, C., O. Ninnemann, H. Fuss, and R. Kahmann. 1991. The N-terminal part of the E. coli DNA binding protein Fis is essential for stimulating site-specific DNA inversion but is not required for specific DNA binding. Nucleic Acids Res. 19:5915-5922.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 5915-5922
    • Koch, C.1    Ninnemann, O.2    Fuss, H.3    Kahmann, R.4
  • 31
    • 0026749182 scopus 로고
    • Crystal structure of the factor for inversion stimulation FIS at 2.0 Å resolution
    • Kostrewa, D., J. Granzin, H. W. Choe, J. Labahn, and W. Saenger. 1992. Crystal structure of the factor for inversion stimulation FIS at 2.0 Å resolution. J. Mol. Biol. 226:209-226.
    • (1992) J. Mol. Biol. , vol.226 , pp. 209-226
    • Kostrewa, D.1    Granzin, J.2    Choe, H.W.3    Labahn, J.4    Saenger, W.5
  • 32
    • 0025067388 scopus 로고
    • Mutations in the bglY gene increase the frequency of spontaneous deletions in Escherichia coli K-12
    • Lejeune, P., and A. Danchin. 1990. Mutations in the bglY gene increase the frequency of spontaneous deletions in Escherichia coli K-12. Proc. Natl. Acad. Sci. USA 87:360-363.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 360-363
    • Lejeune, P.1    Danchin, A.2
  • 33
    • 0028981682 scopus 로고
    • The ntrBC genes of Azospirillum brasilense are part of a nifR3-like-ntrB-ntrC operon and are negatively regulated
    • Machado, H. B., M. B. Yates, S. Funayama, L. U. Rigo, M. B. Steffens, E. M. Souza, and F. O. Pedrosa. 1995. The ntrBC genes of Azospirillum brasilense are part of a nifR3-like-ntrB-ntrC operon and are negatively regulated. Can. J. Microbiol. 41:674-684.
    • (1995) Can. J. Microbiol. , vol.41 , pp. 674-684
    • Machado, H.B.1    Yates, M.B.2    Funayama, S.3    Rigo, L.U.4    Steffens, M.B.5    Souza, E.M.6    Pedrosa, F.O.7
  • 35
    • 0003842951 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Miller, J. H. 1992. A short course in bacterial genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1992) A Short Course in Bacterial Genetics
    • Miller, J.H.1
  • 36
    • 0025069971 scopus 로고
    • The role of Fis in trans activation of stable RNA operons in E. coli
    • Nilsson, L., A. Vanet, E. Vijgenboom, and L. Bosch. 1990. The role of Fis in trans activation of stable RNA operons in E. coli. EMBO J. 9:727-734.
    • (1990) EMBO J. , vol.9 , pp. 727-734
    • Nilsson, L.1    Vanet, A.2    Vijgenboom, E.3    Bosch, L.4
  • 37
    • 0026508913 scopus 로고
    • Fis-dependent trans activation of stable RNA operons of Escherichia coli under various growth conditions
    • Nilsson, L., H. Verbeek, E. Vijgenboom, C. van Drunen, A. Vanet, and L. Bosch. 1992. Fis-dependent trans activation of stable RNA operons of Escherichia coli under various growth conditions. J. Bacteriol. 174:921-929.
    • (1992) J. Bacteriol. , vol.174 , pp. 921-929
    • Nilsson, L.1    Verbeek, H.2    Vijgenboom, E.3    Van Drunen, C.4    Vanet, A.5    Bosch, L.6
  • 38
    • 0026569267 scopus 로고
    • The E. coli fis promoter is subject to stringent control and autoregulation
    • Ninnemann, O., C. Koch, and R. Kahmann. 1992. The E. coli fis promoter is subject to stringent control and autoregulation. EMBO J. 11:1075-1083.
    • (1992) EMBO J. , vol.11 , pp. 1075-1083
    • Ninnemann, O.1    Koch, C.2    Kahmann, R.3
  • 39
    • 0027248437 scopus 로고
    • Prokaryotic enhancer-binding proteins reflect eukaryote-like modularity: The puzzle of nitrogen regulatory protein C.J
    • North, A. K., K. E. Klose, K. M. Stedman, and S. Kustu. 1993. Prokaryotic enhancer-binding proteins reflect eukaryote-like modularity: the puzzle of nitrogen regulatory protein C.J. Bacteriol. 175:4267-4273.
    • (1993) Bacteriol. , vol.175 , pp. 4267-4273
    • North, A.K.1    Klose, K.E.2    Stedman, K.M.3    Kustu, S.4
  • 40
    • 0031033042 scopus 로고    scopus 로고
    • Expression of AbrB, a transition state regulator from Bacillus subtilis, is growth phase dependent in a manner resembling that of Fis, the nucleoid binding protein from Escherichia coli
    • O'Reilly, M., and K. M. Devine. 1997. Expression of AbrB, a transition state regulator from Bacillus subtilis, is growth phase dependent in a manner resembling that of Fis, the nucleoid binding protein from Escherichia coli. J. Bacteriol. 179:522-529.
    • (1997) J. Bacteriol. , vol.179 , pp. 522-529
    • O'Reilly, M.1    Devine, K.M.2
  • 41
    • 0025905172 scopus 로고
    • Identification of two functional regions in Fis: The N-terminus is required to promote Hin-mediated DNA inversion but not λ excision
    • Osuna, R., S. E. Finkel, and R. C. Johnson. 1991. Identification of two functional regions in Fis: the N-terminus is required to promote Hin-mediated DNA inversion but not λ excision. EMBO J. 10:1593-1603.
    • (1991) EMBO J. , vol.10 , pp. 1593-1603
    • Osuna, R.1    Finkel, S.E.2    Johnson, R.C.3
  • 42
    • 0028953095 scopus 로고
    • Sequence, regulation, and functions of fis in Salmonella typhimurium
    • Osuna, R., D. Lienau, K. Hughes, and R. C. Johnson. 1995. Sequence, regulation, and functions of fis in Salmonella typhimurium. J. Bacteriol. 177: 2021-2032.
    • (1995) J. Bacteriol. , vol.177 , pp. 2021-2032
    • Osuna, R.1    Lienau, D.2    Hughes, K.3    Johnson, R.C.4
  • 43
    • 0027170683 scopus 로고
    • The ntrBC genes of Rhizobium leguminosarum are part of a complex operon subject to negative regulation
    • Patriarca, E. J., A. Riccio, R. Täte, S. Colonna-Romano, M. Iaccarino, and R. Defez. 1993. The ntrBC genes of Rhizobium leguminosarum are part of a complex operon subject to negative regulation. Mol. Microbiol. 9:569-577.
    • (1993) Mol. Microbiol. , vol.9 , pp. 569-577
    • Patriarca, E.J.1    Riccio, A.2    Täte, R.3    Colonna-Romano, S.4    Iaccarino, M.5    Defez, R.6
  • 44
    • 0028557390 scopus 로고
    • HU and functional analogs in eukaryotes promote Hin invertasome assembly
    • Paull, T. T., M. J. Haykinson, and R. C. Johnson. 1994. HU and functional analogs in eukaryotes promote Hin invertasome assembly. Biochimie 76: 992-1004.
    • (1994) Biochimie , vol.76 , pp. 992-1004
    • Paull, T.T.1    Haykinson, M.J.2    Johnson, R.C.3
  • 45
    • 0030795165 scopus 로고    scopus 로고
    • Deletion analysis of the fis promoter region in Escherichia coli: Antagonistic effects of integration host factor and Fis
    • Pratt, T. S., T. Steiner, L. S. Feldman, K. A. Walker, and R. Osuna. 1997. Deletion analysis of the fis promoter region in Escherichia coli: antagonistic effects of integration host factor and Fis. J. Bacteriol. 179:6367-6377.
    • (1997) J. Bacteriol. , vol.179 , pp. 6367-6377
    • Pratt, T.S.1    Steiner, T.2    Feldman, L.S.3    Walker, K.A.4    Osuna, R.5
  • 46
    • 0025163439 scopus 로고
    • E. coli Fis protein activates ribosomal RNA transcription in vitro and in vivo
    • Ross, W. J., J. F. Thompson, J. T. Newlands, and R. L. Gourse. 1990. E. coli Fis protein activates ribosomal RNA transcription in vitro and in vivo. EMBO J. 9:3733-3742.
    • (1990) EMBO J. , vol.9 , pp. 3733-3742
    • Ross, W.J.1    Thompson, J.F.2    Newlands, J.T.3    Gourse, R.L.4
  • 47
    • 0030842186 scopus 로고    scopus 로고
    • The transactivation region of the Fis protein that controls site-specific DNA inversion contains extended mobile β-hairpin arms
    • Safo, M. K., W.-Z. Yang, L. Corselli, S. E. Cramton, H. S. Yuan, and R. C. Johnson. 1998. The transactivation region of the Fis protein that controls site-specific DNA inversion contains extended mobile β-hairpin arms. EMBO J. 16:6860-6873.
    • (1998) EMBO J. , vol.16 , pp. 6860-6873
    • Safo, M.K.1    Yang, W.-Z.2    Corselli, L.3    Cramton, S.E.4    Yuan, H.S.5    Johnson, R.C.6
  • 49
    • 0025153881 scopus 로고
    • More than just "histone-like" proteins
    • Schmid, M. B. 1990. More than just "histone-like" proteins. Cell 63:451-453.
    • (1990) Cell , vol.63 , pp. 451-453
    • Schmid, M.B.1
  • 50
    • 0030668269 scopus 로고    scopus 로고
    • FIS modulates growth phase-dependent topological transitions of DNA in Escherichia coli
    • Schneider, R., A. Travers, and G. Muskhelisvili. 1997. FIS modulates growth phase-dependent topological transitions of DNA in Escherichia coli. Mol. Microbiol. 26:519-530.
    • (1997) Mol. Microbiol. , vol.26 , pp. 519-530
    • Schneider, R.1    Travers, A.2    Muskhelisvili, G.3
  • 51
    • 0026002819 scopus 로고
    • Determinants of DNA sequence divergence between Escherichia coli and Salmonella typhimurium: Codon usage, map position, and concerted evolution
    • Sharp, P. M. 1991. Determinants of DNA sequence divergence between Escherichia coli and Salmonella typhimurium: codon usage, map position, and concerted evolution. J. Mol. Evol. 33:23-33.
    • (1991) J. Mol. Evol. , vol.33 , pp. 23-33
    • Sharp, P.M.1
  • 52
    • 0023255472 scopus 로고
    • Improved single and multicopy lac-based cloning vectors for protein and operon fusions
    • Simons, R. W., F. Houman, and N. Kleckner. 1987. Improved single and multicopy lac-based cloning vectors for protein and operon fusions. Gene 53: 85-96.
    • (1987) Gene , vol.53 , pp. 85-96
    • Simons, R.W.1    Houman, F.2    Kleckner, N.3
  • 53
    • 0027506115 scopus 로고
    • Transition state regulators: Sentinels of Bacillus subtilis post-exponential gene expression
    • Strauch, M. A., and J. A. Hoch. 1993. Transition state regulators: sentinels of Bacillus subtilis post-exponential gene expression. Mol. Microbiol. 7:337-342.
    • (1993) Mol. Microbiol. , vol.7 , pp. 337-342
    • Strauch, M.A.1    Hoch, J.A.2
  • 54
    • 0023651267 scopus 로고
    • Cellular factors couple recombination with growth phase: Characterization of a new component in the lambda site-specific recombination pathway
    • Thompson, J. F., L. Moitoso de Vargas, C. Koch, R. Kahmann, and A. Landy. 1987. Cellular factors couple recombination with growth phase: characterization of a new component in the lambda site-specific recombination pathway. Cell 50:901-908.
    • (1987) Cell , vol.50 , pp. 901-908
    • Thompson, J.F.1    Moitoso De Vargas, L.2    Koch, C.3    Kahmann, R.4    Landy, A.5
  • 55
    • 0027378528 scopus 로고
    • Cotranscription of two genes necessary for ribosomal protein L11 methylation (prmA) and pantothenate transport (panF) in Escherichia coli K-12
    • Vanet, A., J. A. Plumbridge, and J. Alix. 1993. Cotranscription of two genes necessary for ribosomal protein L11 methylation (prmA) and pantothenate transport (panF) in Escherichia coli K-12. J. Bacteriol. 175:7178-7188.
    • (1993) J. Bacteriol. , vol.175 , pp. 7178-7188
    • Vanet, A.1    Plumbridge, J.A.2    Alix, J.3
  • 56
    • 0029791749 scopus 로고    scopus 로고
    • The Escherichia coli Fis protein prevents initiation of DNA replication from oriC in vitro
    • Wold, S., E. Crooke, and K. S. Karstad. 1996. The Escherichia coli Fis protein prevents initiation of DNA replication from oriC in vitro. Nucleic Acids Res. 24:3527-3532.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3527-3532
    • Wold, S.1    Crooke, E.2    Karstad, K.S.3
  • 57
    • 0025939520 scopus 로고
    • The molecular structure of wild-type and a mutant Fis protein: Relationship between mutational changes and recombinational enhancer function or DNA binding
    • Yuan, H., S. E. Finkel, J. A. Feng, M. Kaczor-Grzeskowiak, R. C. Johnson, and R. E. Dickerson. 1991. The molecular structure of wild-type and a mutant Fis protein: relationship between mutational changes and recombinational enhancer function or DNA binding. Proc. Natl. Acad. Sci. USA 88: 9559-9562.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9559-9562
    • Yuan, H.1    Finkel, S.E.2    Feng, J.A.3    Kaczor-Grzeskowiak, M.4    Johnson, R.C.5    Dickerson, R.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.