메뉴 건너뛰기




Volumn 75, Issue 3, 2010, Pages 637-657

Induction of the ferritin gene (ftnA) of Escherichia coli by Fe 2+-Fur is mediated by reversal of H-NS silencing and is RyhB independent

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; FERRIC UPTAKE REGULATOR; FERRITIN; FERROUS ION; HISTONE LIKE NUCLEOID ASSOCIATED PROTEIN; RNA; RNA POLYMERASE; RNA RYHB; UNCLASSIFIED DRUG;

EID: 75149173382     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2009.06977.x     Document Type: Article
Times cited : (78)

References (119)
  • 1
    • 0033025239 scopus 로고    scopus 로고
    • Ferritin mutants of Escherichia coli are iron deficient and growth impaired; Fur mutants are iron deficient
    • Abdul-Tehrani, H., Hudson, A.J., Chang, Y.S., Timms, A.R., Hawkins, C., Williams, J.M., et al. (1999) Ferritin mutants of Escherichia coli are iron deficient and growth impaired; fur mutants are iron deficient. J Bacteriol 181 : 1415 1428.
    • (1999) J Bacteriol , vol.181 , pp. 1415-1428
    • Abdul-Tehrani, H.1    Hudson, A.J.2    Chang, Y.S.3    Timms, A.R.4    Hawkins, C.5    Williams, J.M.6
  • 2
    • 3142764130 scopus 로고    scopus 로고
    • Cell-to-cell signalling in Escherichia coli and Salmonella enterica
    • Ahmer, B.M.M. (2004) Cell-to-cell signalling in Escherichia coli and Salmonella enterica. Mol Microbiol 52 : 933 945.
    • (2004) Mol Microbiol , vol.52 , pp. 933-945
    • Ahmer, B.M.M.1
  • 3
    • 33745901282 scopus 로고    scopus 로고
    • Regulation of the Helicobacter pylori Fe-S cluster synthesis protein NifS by iron, oxidative stress conditions, and fur
    • Alamuri, P., Mehta, N., Burk, A. Maier, R.J. (2006) Regulation of the Helicobacter pylori Fe-S cluster synthesis protein NifS by iron, oxidative stress conditions, and Fur. J Bacteriol 188 : 5325 5330.
    • (2006) J Bacteriol , vol.188 , pp. 5325-5330
    • Alamuri, P.1    Mehta, N.2    Burk, A.3    Maier, R.J.4
  • 4
    • 0031763106 scopus 로고    scopus 로고
    • Iron storage in bacteria
    • Andrews, S.C. (1998) Iron storage in bacteria. Adv Microb Physiol 40 : 281 351.
    • (1998) Adv Microb Physiol , vol.40 , pp. 281-351
    • Andrews, S.C.1
  • 5
    • 0024384958 scopus 로고
    • Cloning, sequencing, and mapping of the bacterioferritin gene (bfr) of Escherichia coli K-12
    • Andrews, S.C., Harrison, P.M. Guest, J.R. (1989) Cloning, sequencing, and mapping of the bacterioferritin gene (bfr) of Escherichia coli K-12. J Bacteriol 171 : 3940 3947.
    • (1989) J Bacteriol , vol.171 , pp. 3940-3947
    • Andrews, S.C.1    Harrison, P.M.2    Guest, J.R.3
  • 6
    • 0027405142 scopus 로고
    • Overproduction, purification and characterization of bacterioferritin (BFR) from Escherichia coli and a C-terminally extended variant
    • Andrews, S.C., Smith, J.M., Hawkins, C., Williams, J.M., Harrison, P.M. Guest, J.R. (1993) Overproduction, purification and characterization of bacterioferritin (BFR) from Escherichia coli and a C-terminally extended variant. Eur J Biochem 213 : 329 338.
    • (1993) Eur J Biochem , vol.213 , pp. 329-338
    • Andrews, S.C.1    Smith, J.M.2    Hawkins, C.3    Williams, J.M.4    Harrison, P.M.5    Guest, J.R.6
  • 8
    • 0020640059 scopus 로고
    • Oxygen radicals, oxygen toxicity and the life of microorganisms
    • Archibald, F.S. Fridovich, I. (1983) Oxygen radicals, oxygen toxicity and the life of microorganisms. Acta Med Port 4 : 101 112.
    • (1983) Acta Med Port , vol.4 , pp. 101-112
    • Archibald, F.S.1    Fridovich, I.2
  • 9
    • 0029945236 scopus 로고    scopus 로고
    • Translation of the adhE transcript to produce ethanol dehydrogenase requires RNase III cleavage in Escherichia coli
    • Aristarkhov, A., Milkulskis, A., Belasco, J.G. Lin, E.C. (1996) Translation of the adhE transcript to produce ethanol dehydrogenase requires RNase III cleavage in Escherichia coli. J Bacteriol 178 : 4327 4332.
    • (1996) J Bacteriol , vol.178 , pp. 4327-4332
    • Aristarkhov, A.1    Milkulskis, A.2    Belasco, J.G.3    Lin, E.C.4
  • 10
    • 0027980255 scopus 로고
    • Anaerobic regulation of the hydrogenase 1 (hya) operon of Escherichia coli
    • Atlung, T. Brøndsted, L. (1994) Anaerobic regulation of the hydrogenase 1 (hya) operon of Escherichia coli. J Bacteriol 176 : 5414 5422.
    • (1994) J Bacteriol , vol.176 , pp. 5414-5422
    • Atlung, T.1    Brøndsted, L.2
  • 11
    • 0030972952 scopus 로고    scopus 로고
    • H-NS: A modulator of environmentally regulated gene expression
    • Atlung, T. Ingmer, H. (1997) H-NS: a modulator of environmentally regulated gene expression. Mol Microbiol 24 : 7 17.
    • (1997) Mol Microbiol , vol.24 , pp. 7-17
    • Atlung, T.1    Ingmer, H.2
  • 12
    • 0036829677 scopus 로고    scopus 로고
    • The degree of oligomerization of the H-NS nucleoid structuring protein is related to specific binding to DNA
    • Badaut, C., Williams, R., Arluison, V., Bouffartigues, E., Robert, B., Buc, H. Rimsky, S. (2002) The degree of oligomerization of the H-NS nucleoid structuring protein is related to specific binding to DNA. J Biol Chem 277 : 41657 41666.
    • (2002) J Biol Chem , vol.277 , pp. 41657-41666
    • Badaut, C.1    Williams, R.2    Arluison, V.3    Bouffartigues, E.4    Robert, B.5    Buc, H.6    Rimsky, S.7
  • 13
    • 0025778670 scopus 로고
    • Construction and properties of a family of pACYC184-derived cloning vectors compatible with pBR322 and its derivatives
    • Bartolome, B., Jubete, Y., Martinez, E. de la Cruz, F. (1991) Construction and properties of a family of pACYC184-derived cloning vectors compatible with pBR322 and its derivatives. Gene 102 : 75 78.
    • (1991) Gene , vol.102 , pp. 75-78
    • Bartolome, B.1    Jubete, Y.2    Martinez, E.3    De La Cruz, F.4
  • 15
    • 0031944364 scopus 로고    scopus 로고
    • Characterization of the cvaA and cvi promoters of the colicin v export system: Iron-dependent transcription of cvaA is modulated by downstream sequences
    • Boyer, A.E. Tai, P.C. (1998) Characterization of the cvaA and cvi promoters of the colicin V export system: iron-dependent transcription of cvaA is modulated by downstream sequences. J Bacteriol 180 : 1662 1672.
    • (1998) J Bacteriol , vol.180 , pp. 1662-1672
    • Boyer, A.E.1    Tai, P.C.2
  • 16
    • 0029866860 scopus 로고    scopus 로고
    • Effect of growth conditions on expression of the acid phosphatase (cyx-appA) operon and the appY gene, which encodes a transcriptional activator of Escherichia coli
    • Brøndsted, L. Atlung, T. (1996) Effect of growth conditions on expression of the acid phosphatase (cyx-appA) operon and the appY gene, which encodes a transcriptional activator of Escherichia coli. J Bacteriol 178 : 1556 1564.
    • (1996) J Bacteriol , vol.178 , pp. 1556-1564
    • Brøndsted, L.1    Atlung, T.2
  • 17
    • 0035136207 scopus 로고    scopus 로고
    • Transcriptional regulation of type III secretion genes in enteropathogenic Escherichia coli (EPEC): Ler antagonizes H-NS-dependent repression
    • Bustamante, V.H., Santana, F.J., Calva, E. Puente, J.L. (2001) Transcriptional regulation of type III secretion genes in enteropathogenic Escherichia coli (EPEC): Ler antagonizes H-NS-dependent repression. Mol Microbiol 39 : 664 678.
    • (2001) Mol Microbiol , vol.39 , pp. 664-678
    • Bustamante, V.H.1    Santana, F.J.2    Calva, E.3    Puente, J.L.4
  • 18
    • 0028113847 scopus 로고
    • Observation of binding and polymerization of fur repressor onto operator-containing DNA with electron and atomic force microscopes
    • le Cam, E., Frechon, D., Barray, M., Fourcade, A. Delain, E. (1994) Observation of binding and polymerization of Fur repressor onto operator-containing DNA with electron and atomic force microscopes. Proc Natl Acad Sci USA 91 : 11816 11820.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11816-11820
    • Le Cam, E.1    Frechon, D.2    Barray, M.3    Fourcade, A.4    Delain, E.5
  • 20
    • 0032509098 scopus 로고    scopus 로고
    • Lac and Lambda repressor relieve silencing of the Escherichia coli bgl promoter: Activation by alteration of a repressing nucleoprotein complex
    • Caramel, A. Schnetz, K. (2000) Lac and Lambda repressor relieve silencing of the Escherichia coli bgl promoter: activation by alteration of a repressing nucleoprotein complex. J Mol Biol 284 : 875 883.
    • (2000) J Mol Biol , vol.284 , pp. 875-883
    • Caramel, A.1    Schnetz, K.2
  • 21
    • 67650094768 scopus 로고    scopus 로고
    • This is not your mother's repressor: The complex role of fur in pathogenesis
    • Carpenter, B.M., Whitmire, J.M. Merrell, D.S. (2009) This is not your mother's repressor: the complex role of Fur in pathogenesis. Infect Immun 77 : 2590 2601.
    • (2009) Infect Immun , vol.77 , pp. 2590-2601
    • Carpenter, B.M.1    Whitmire, J.M.2    Merrell, D.S.3
  • 22
    • 0038219647 scopus 로고    scopus 로고
    • Ferritins, iron uptake and storage from the bacterioferritin viewpoint
    • Carrondo, M.A. (2003) Ferritins, iron uptake and storage from the bacterioferritin viewpoint. EMBO J 22 : 1959 1968.
    • (2003) EMBO J , vol.22 , pp. 1959-1968
    • Carrondo, M.A.1
  • 23
    • 34548674949 scopus 로고    scopus 로고
    • The RovA regulons of Yersinia enterocolitica and Yersinia pestis are distinct: Evidence that many RovA-regulated genes were acquired more recently than the core genome
    • Cathelyn, J.S., Ellison, D.W., Hinchliffe, S.J., Wren, B.W. Miller, V.L. (2007) The RovA regulons of Yersinia enterocolitica and Yersinia pestis are distinct: evidence that many RovA-regulated genes were acquired more recently than the core genome. Mol Microbiol 66 : 189 205.
    • (2007) Mol Microbiol , vol.66 , pp. 189-205
    • Cathelyn, J.S.1    Ellison, D.W.2    Hinchliffe, S.J.3    Wren, B.W.4    Miller, V.L.5
  • 24
    • 0029155913 scopus 로고
    • The interaction of the ferric uptake regulation protein with DNA
    • Coy, M. (1995) The interaction of the ferric uptake regulation protein with DNA. Biochem Biophys Res Commun 212 : 784 792.
    • (1995) Biochem Biophys Res Commun , vol.212 , pp. 784-792
    • Coy, M.1
  • 26
    • 69949162821 scopus 로고    scopus 로고
    • The DNA static curvature has a role in the regulation of the ompS1 porin gene in Salmonella enterica serovar Typhi
    • de la Cruz, M.A., Merino, E., Oropeza, R., Telléz, J. Calva, E. (2009) The DNA static curvature has a role in the regulation of the ompS1 porin gene in Salmonella enterica serovar Typhi. Microbiology 155 : 2127 2136.
    • (2009) Microbiology , vol.155 , pp. 2127-2136
    • De La Cruz, M.A.1    Merino, E.2    Oropeza, R.3    Telléz, J.4    Calva, E.5
  • 27
    • 18444369954 scopus 로고    scopus 로고
    • The role of nucleoid-associated proteins in the organization and compaction of bacterial chromatin
    • Dame, R.T. (2005) The role of nucleoid-associated proteins in the organization and compaction of bacterial chromatin. Mol Microbiol 56 : 858 870.
    • (2005) Mol Microbiol , vol.56 , pp. 858-870
    • Dame, R.T.1
  • 28
    • 0034666271 scopus 로고    scopus 로고
    • H-NS mediated compaction of DNA visualised by atomic force microscopy
    • Dame, R.T., Wyman, C. Goosen, N. (2000) H-NS mediated compaction of DNA visualised by atomic force microscopy. Nucleic Acids Res 28 : 3504 3510.
    • (2000) Nucleic Acids Res , vol.28 , pp. 3504-3510
    • Dame, R.T.1    Wyman, C.2    Goosen, N.3
  • 29
    • 0035083490 scopus 로고    scopus 로고
    • Structural basis for preferential binding of H-NS to curved DNA
    • Dame, R.T., Wyman, C. Goosen, N. (2001) Structural basis for preferential binding of H-NS to curved DNA. Biochimie 83 : 231 234.
    • (2001) Biochimie , vol.83 , pp. 231-234
    • Dame, R.T.1    Wyman, C.2    Goosen, N.3
  • 30
    • 0037127209 scopus 로고    scopus 로고
    • Structural basis for H-NS-mediated trapping of RNA polymerase in the open initiation complex at the rrnB P1
    • Dame, R.T., Wyman, C., Wurm, R., Wagner, R. Goosen, N. (2002) Structural basis for H-NS-mediated trapping of RNA polymerase in the open initiation complex at the rrnB P1. J Biol Chem 277 : 2146 2150.
    • (2002) J Biol Chem , vol.277 , pp. 2146-2150
    • Dame, R.T.1    Wyman, C.2    Wurm, R.3    Wagner, R.4    Goosen, N.5
  • 32
    • 33745460953 scopus 로고    scopus 로고
    • In vivo dissection of the Helicobacter pylori fur regulatory circuit by genome-wide location analysis
    • Danielli, A., Roncarati, D., Delany, I., Chiarini, V., Rappuoli, R. Scarlato, V. (2006) In vivo dissection of the Helicobacter pylori Fur regulatory circuit by genome-wide location analysis. J Bacteriol 188 : 4654 4662.
    • (2006) J Bacteriol , vol.188 , pp. 4654-4662
    • Danielli, A.1    Roncarati, D.2    Delany, I.3    Chiarini, V.4    Rappuoli, R.5    Scarlato, V.6
  • 33
    • 0019932517 scopus 로고
    • The metabolism of beta-glucosides in Escherichia coli K12
    • Defez, R. De Felice, M. (1982) The metabolism of beta-glucosides in Escherichia coli K12. Ann Microbiol (Paris) 133 : 347 350.
    • (1982) Ann Microbiol (Paris) , vol.133 , pp. 347-350
    • Defez, R.1    De Felice, M.2
  • 34
    • 0035724513 scopus 로고    scopus 로고
    • The Fur repressor controls transcription of iron-activated and -repressed genes in Helicobacter pylori
    • DOI 10.1046/j.1365-2958.2001.02696.x
    • Delany, I., Spohn, G., Rappuoli, R. Scarlato, V. (2001) The Fur repressor controls transcription of iron-activated and -repressed genes in Helicobacter pylori. Mol Microbiol 42 : 1297 1309. (Pubitemid 34209090)
    • (2001) Molecular Microbiology , vol.42 , Issue.5 , pp. 1297-1309
    • Delany, I.1    Spohn, G.2    Rappuoli, R.3    Scarlato, V.4
  • 35
    • 3042816068 scopus 로고    scopus 로고
    • Fur functions as an activator and as a repressor of putative virulence genes in Neisseria meningitidis
    • Delany, I., Rappuoli, R. Scarlato, V. (2004) Fur functions as an activator and as a repressor of putative virulence genes in Neisseria meningitidis. Mol Microbiol 52 : 1081 1090.
    • (2004) Mol Microbiol , vol.52 , pp. 1081-1090
    • Delany, I.1    Rappuoli, R.2    Scarlato, V.3
  • 36
    • 0027404359 scopus 로고
    • The Helicobacter pylori 19.6-kilodalton protein is an iron-containing protein resembling ferritin
    • Doig, P.J., Austin, W. Trust, T. (1993) The Helicobacter pylori 19.6-kilodalton protein is an iron-containing protein resembling ferritin. J Bacteriol 175 : 557 560.
    • (1993) J Bacteriol , vol.175 , pp. 557-560
    • Doig, P.J.1    Austin, W.2    Trust, T.3
  • 37
    • 0033104294 scopus 로고    scopus 로고
    • Domain organization and oligomerization among H-NS-like nucleoid-associated proteins in bacteria
    • Dorman, C.J., Hinton, J.C.D. Free, A. (1999) Domain organization and oligomerization among H-NS-like nucleoid-associated proteins in bacteria. Trends Microbiol 7 : 124 128.
    • (1999) Trends Microbiol , vol.7 , pp. 124-128
    • Dorman, C.J.1    Hinton, J.C.D.2    Free, A.3
  • 38
    • 0034046748 scopus 로고    scopus 로고
    • Fur positive regulation of iron superoxide dismutase in Escherichia coli: Functional analysis of the sodB promoter
    • Dubrac, S. Touati, D. (2000) Fur positive regulation of iron superoxide dismutase in Escherichia coli: functional analysis of the sodB promoter. J Bacteriol 182 : 3802 3808.
    • (2000) J Bacteriol , vol.182 , pp. 3802-3808
    • Dubrac, S.1    Touati, D.2
  • 39
    • 0036148389 scopus 로고    scopus 로고
    • Fur-mediated transcriptional and post-transcriptional regulation of FeSOD expression in Escherichia coli
    • Dubrac, S. Touati, D. (2002) Fur-mediated transcriptional and post-transcriptional regulation of FeSOD expression in Escherichia coli. Microbiology 148 : 147 156.
    • (2002) Microbiology , vol.148 , pp. 147-156
    • Dubrac, S.1    Touati, D.2
  • 40
    • 21044458727 scopus 로고    scopus 로고
    • Iron-responsive regulation of the Helicobacter pylori iron-cofactored superoxide dismutase SodB is mediated by fur
    • Ernst, F.D., Homuth, G., Stoof, J., Mäder, U., Waidner, B., Kuipers, E.J., et al. (2005) Iron-responsive regulation of the Helicobacter pylori iron-cofactored superoxide dismutase SodB is mediated by Fur. J Bacteriol 187 : 3687 3692.
    • (2005) J Bacteriol , vol.187 , pp. 3687-3692
    • Ernst, F.D.1    Homuth, G.2    Stoof, J.3    Mäder, U.4    Waidner, B.5    Kuipers, E.J.6
  • 41
    • 0030663311 scopus 로고    scopus 로고
    • Metalloregulation in vitro of the aerobactin promoter of Escherichia coli by the fur (ferric uptake regulation) protein
    • Escolar, L., de Lorenzo, V. Pérez-Martin, J. (1997) Metalloregulation in vitro of the aerobactin promoter of Escherichia coli by the Fur (ferric uptake regulation) protein. Mol Microbiol 26 : 799 808.
    • (1997) Mol Microbiol , vol.26 , pp. 799-808
    • Escolar, L.1    De Lorenzo, V.2    Pérez-Martin, J.3
  • 42
    • 2642654228 scopus 로고    scopus 로고
    • Coordinated repression in vitro of the divergent fepA-fes promoters of Escherichia coli by the iron uptake regulation (Fur) protein
    • Escolar, L., Pérez-Martin, J. de Lorenzo, V. (1998) Coordinated repression in vitro of the divergent fepA-fes promoters of Escherichia coli by the iron uptake regulation (Fur) protein. J Bacteriol 180 : 2579 2582.
    • (1998) J Bacteriol , vol.180 , pp. 2579-2582
    • Escolar, L.1    Pérez-Martin, J.2    De Lorenzo, V.3
  • 43
    • 0344172832 scopus 로고    scopus 로고
    • Opening the iron box: Transcriptional metalloregulation by the fur protein
    • Escolar, L., Pérez-Martin, J. de Lorenzo, V. (1999) Opening the iron box: transcriptional metalloregulation by the Fur protein. J Bacteriol 181 : 6223 6229.
    • (1999) J Bacteriol , vol.181 , pp. 6223-6229
    • Escolar, L.1    Pérez-Martin, J.2    De Lorenzo, V.3
  • 44
    • 0034637480 scopus 로고    scopus 로고
    • Evidence of an unusually long operator for the fur repressor in the aerobactin promoter of Escherichia coli
    • Escolar, L., Pérez-Martin, J. de Lorenzo, V. (2000) Evidence of an unusually long operator for the fur repressor in the aerobactin promoter of Escherichia coli. J Biol Chem 275 : 24709 24714.
    • (2000) J Biol Chem , vol.275 , pp. 24709-24714
    • Escolar, L.1    Pérez-Martin, J.2    De Lorenzo, V.3
  • 45
    • 61349145675 scopus 로고    scopus 로고
    • Siderophore-controlled iron assimilation in the enterobacterium Erwinia chrysanthemi: Evidence for the involvement of bacterioferritins and the Suf iron-sulfur cluster assembly machinery
    • Expert, D., Boughammoura, A. Franza, T. (2008) Siderophore-controlled iron assimilation in the enterobacterium Erwinia chrysanthemi: evidence for the involvement of bacterioferritins and the Suf iron-sulfur cluster assembly machinery. J Biol Chem 283 : 36564 36572.
    • (2008) J Biol Chem , vol.283 , pp. 36564-36572
    • Expert, D.1    Boughammoura, A.2    Franza, T.3
  • 46
    • 0027429067 scopus 로고
    • Expression of the gene encoding the major bacterial nucleotide protein H-NS is subject to transcriptional auto-repression
    • Falconi, M., Higgins, N.P., Spurio, R., Pon, C.L. Gualerzi, C.O. (1993) Expression of the gene encoding the major bacterial nucleotide protein H-NS is subject to transcriptional auto-repression. Mol Microbiol 10 : 273 282.
    • (1993) Mol Microbiol , vol.10 , pp. 273-282
    • Falconi, M.1    Higgins, N.P.2    Spurio, R.3    Pon, C.L.4    Gualerzi, C.O.5
  • 47
    • 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
  • 48
    • 0037214415 scopus 로고    scopus 로고
    • Function of oxygen resistance proteins in the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough
    • Fournier, M., Zhang, Y., Wildschut, J.D., Dolla, A., Voordouw, J.K., Schriemer, D.C. Voordouw, G. (2003) Function of oxygen resistance proteins in the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough. J Bacteriol 185 : 71 79.
    • (2003) J Bacteriol , vol.185 , pp. 71-79
    • Fournier, M.1    Zhang, Y.2    Wildschut, J.D.3    Dolla, A.4    Voordouw, J.K.5    Schriemer, D.C.6    Voordouw, G.7
  • 49
    • 0021325030 scopus 로고
    • Mutations in the DNA gyrB gene that are temperature sensitive for lambda site-specific recombination, Mu growth, and plasmid maintenance
    • Friedman, D.I., Plantefaber, L.C., Olson, E.J., Carver, D., O'Dea, M.H. Gellert, M. (1984) Mutations in the DNA gyrB gene that are temperature sensitive for lambda site-specific recombination, Mu growth, and plasmid maintenance. J Bacteriol 157 : 490 497.
    • (1984) J Bacteriol , vol.157 , pp. 490-497
    • Friedman, D.I.1    Plantefaber, L.C.2    Olson, E.J.3    Carver, D.4    O'Dea, M.H.5    Gellert, M.6
  • 52
    • 33750000118 scopus 로고    scopus 로고
    • Association of nucleoid proteins with coding and non-coding segments of the Escherichia coli genome
    • Grainger, D.C., Hurd, D., Goldberg, M.D. Busby, S.J. (2006) Association of nucleoid proteins with coding and non-coding segments of the Escherichia coli genome. Nucleic Acids Res 34 : 4642 4652.
    • (2006) Nucleic Acids Res , vol.34 , pp. 4642-4652
    • Grainger, D.C.1    Hurd, D.2    Goldberg, M.D.3    Busby, S.J.4
  • 53
    • 14544287732 scopus 로고    scopus 로고
    • Escherichia coli ribosomal RNA transcription: Regulatory roles for ppGpp, NTPs, architectural proteins and a polymerase-binding protein
    • Gralla, J.D. (2005) Escherichia coli ribosomal RNA transcription: regulatory roles for ppGpp, NTPs, architectural proteins and a polymerase-binding protein. Mol Microbiol 55 : 973 977.
    • (2005) Mol Microbiol , vol.55 , pp. 973-977
    • Gralla, J.D.1
  • 54
    • 0024618846 scopus 로고
    • Mechanism for iron-regulated transcription of the Escherichia coli cir gene: Metal-dependent binding of fur protein to the promoters
    • Griggs, D.W. Konisky, J. (1989) Mechanism for iron-regulated transcription of the Escherichia coli cir gene: metal-dependent binding of fur protein to the promoters. J Bacteriol 171 : 1048 1054.
    • (1989) J Bacteriol , vol.171 , pp. 1048-1054
    • Griggs, D.W.1    Konisky, J.2
  • 55
    • 33748670718 scopus 로고    scopus 로고
    • A new ferrous iron-uptake transporter, EfeU (YcdN), from Escherichia coli
    • Grosse, C., Scherer, J., Koch, D., Otto, M., Taudte, N. Grass, G. (2006) A new ferrous iron-uptake transporter, EfeU (YcdN), from Escherichia coli. Mol Microbiol 62 : 120 131.
    • (2006) Mol Microbiol , vol.62 , pp. 120-131
    • Grosse, C.1    Scherer, J.2    Koch, D.3    Otto, M.4    Taudte, N.5    Grass, G.6
  • 56
    • 0023237755 scopus 로고
    • Regulation of the aroH operon of Escherichia coli by the tryptophan repressor
    • Grove, C.L. Gunsalus, R.P. (1987) Regulation of the aroH operon of Escherichia coli by the tryptophan repressor. J Bacteriol 169 : 2158 2164.
    • (1987) J Bacteriol , vol.169 , pp. 2158-2164
    • Grove, C.L.1    Gunsalus, R.P.2
  • 57
    • 0035047678 scopus 로고    scopus 로고
    • Large-scale monitoring of pleiotropic regulation of gene expression by the prokaryotic nucleoid-associated protein, H-NS
    • Hommais, F., Krin, E., Laurent-Winter, C., Soutourina, O., Malpertuy, A., Le Caer, J.P., et al. (2001) Large-scale monitoring of pleiotropic regulation of gene expression by the prokaryotic nucleoid-associated protein, H-NS. Mol Microbiol 40 : 20 36.
    • (2001) Mol Microbiol , vol.40 , pp. 20-36
    • Hommais, F.1    Krin, E.2    Laurent-Winter, C.3    Soutourina, O.4    Malpertuy, A.5    Le Caer, J.P.6
  • 59
    • 0026028046 scopus 로고
    • Cloning and sequencing of an Escherichia coli K12 gene which encodes a polypeptide having similarity to the human ferritin H subunit
    • Izuhara, M., Takamune, K. Takata, R. (1991) Cloning and sequencing of an Escherichia coli K12 gene which encodes a polypeptide having similarity to the human ferritin H subunit. Mol Gen Genet 225 : 510 513.
    • (1991) Mol Gen Genet , vol.225 , pp. 510-513
    • Izuhara, M.1    Takamune, K.2    Takata, R.3
  • 60
    • 0030698856 scopus 로고    scopus 로고
    • CAMP receptor protein-cAMP plays a crucial role in glucose-lactose diauxie by activating the major glucose transporter gene in Escherichia coli
    • Kimata, K., Takahashi, H., Inada, T., Postma, P. Aiba, H. (1997) cAMP receptor protein-cAMP plays a crucial role in glucose-lactose diauxie by activating the major glucose transporter gene in Escherichia coli. Proc Natl Acad Sci USA 94 : 12914 12919.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12914-12919
    • Kimata, K.1    Takahashi, H.2    Inada, T.3    Postma, P.4    Aiba, H.5
  • 62
    • 35549009343 scopus 로고    scopus 로고
    • High-affinity DNA binding sites for H-NS provide a molecular basis for selective silencing within proteobacterial genomes
    • Lang, B., Blot, N., Bouffartigues, E., Buckle, M., Geertz, M., Gualerzi, C.O., et al. (2007) High-affinity DNA binding sites for H-NS provide a molecular basis for selective silencing within proteobacterial genomes. Nucleic Acids Res 35 : 6330 6337.
    • (2007) Nucleic Acids Res , vol.35 , pp. 6330-6337
    • Lang, B.1    Blot, N.2    Bouffartigues, E.3    Buckle, M.4    Geertz, M.5    Gualerzi, C.O.6
  • 63
    • 0037381732 scopus 로고    scopus 로고
    • Architecture of a fur binding site: A comparative analysis
    • Lavrrar, J.L. McIntosh, M.A. (2003) Architecture of a fur binding site: a comparative analysis. J Bacteriol 185 : 2194 2202.
    • (2003) J Bacteriol , vol.185 , pp. 2194-2202
    • Lavrrar, J.L.1    McIntosh, M.A.2
  • 64
    • 0036415664 scopus 로고    scopus 로고
    • Fur-DNA interactions at the bidirectional fepDGC-entS promoter region in Escherichia coli
    • Lavrrar, J.L., Christoffersen, C.A. McIntosh, M.A. (2002) Fur-DNA interactions at the bidirectional fepDGC-entS promoter region in Escherichia coli. J Mol Biol 322 : 983 995.
    • (2002) J Mol Biol , vol.322 , pp. 983-995
    • Lavrrar, J.L.1    Christoffersen, C.A.2    McIntosh, M.A.3
  • 65
    • 34248669001 scopus 로고    scopus 로고
    • Functional specialization within the fur family of metalloregulators
    • Lee, J.W. Helmann, J.D. (2007) Functional specialization within the Fur family of metalloregulators. Biometals 20 : 485 499.
    • (2007) Biometals , vol.20 , pp. 485-499
    • Lee, J.W.1    Helmann, J.D.2
  • 66
    • 35448991375 scopus 로고    scopus 로고
    • Alternate SlyA and H-NS nucleoprotein complexes control hlyE expression in Escherichia coli K-12
    • Lithgow, J.K., Haider, F., Roberts, I.S. Green, J. (2007) Alternate SlyA and H-NS nucleoprotein complexes control hlyE expression in Escherichia coli K-12. Mol Microbiol 66 : 685 698.
    • (2007) Mol Microbiol , vol.66 , pp. 685-698
    • Lithgow, J.K.1    Haider, F.2    Roberts, I.S.3    Green, J.4
  • 67
    • 0023258960 scopus 로고
    • Operator sequences of the aerobactin operon of plasmid ColV-K30 binding the ferric uptake regulation (fur) repressor
    • de Lorenzo, V., Wee, S., Herrero, M. Neilands, J.B. (1987) Operator sequences of the aerobactin operon of plasmid ColV-K30 binding the ferric uptake regulation (fur) repressor. J Bacteriol 169 : 2624 2630.
    • (1987) J Bacteriol , vol.169 , pp. 2624-2630
    • De Lorenzo, V.1    Wee, S.2    Herrero, M.3    Neilands, J.B.4
  • 68
    • 0024276112 scopus 로고
    • Fur (ferric uptake regulation) protein and CAP (catabolite-activator protein) modulate transcription of fur gene in Escherichia coli
    • de Lorenzo, V., Herrero, M., Giovannini, F. Neilands, J.B. (1988) Fur (ferric uptake regulation) protein and CAP (catabolite-activator protein) modulate transcription of fur gene in Escherichia coli. Eur J Biochem 173 : 537 546.
    • (1988) Eur J Biochem , vol.173 , pp. 537-546
    • De Lorenzo, V.1    Herrero, M.2    Giovannini, F.3    Neilands, J.B.4
  • 69
    • 24744459983 scopus 로고    scopus 로고
    • Mode of binding of the fur protein to target DNA: Negative regulation of iron-controlled gene expression
    • Crosa, J.H. Mey, A.R. Payne, S.M. (eds). Washington, DC. ASM Press
    • de Lorenzo, V., Perez-Martin, J., Escolar, L., Pesole, G. Bertoni, G. (2004) Mode of binding of the Fur protein to target DNA: negative regulation of iron-controlled gene expression. In Iron Transport in Bacteria. Crosa, J.H., Mey, A.R. Payne, S.M. (eds). Washington, DC : ASM Press, pp. 185 196.
    • (2004) Iron Transport in Bacteria , pp. 185-196
    • De Lorenzo, V.1    Perez-Martin, J.2    Escolar, L.3    Pesole, G.4    Bertoni, G.5
  • 71
    • 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
  • 73
    • 0037007078 scopus 로고    scopus 로고
    • A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli
    • Massé, E. Gottesman, S. (2002) A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli. Proc Natl Acad Sci USA 99 : 4620 4625.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 4620-4625
    • Massé, E.1    Gottesman, S.2
  • 74
    • 26444505976 scopus 로고    scopus 로고
    • Effect of RyhB small RNA on global iron use in Escherichia coli
    • Massé, E., Vanderpool, C.K. Gottesman, S. (2005) Effect of RyhB small RNA on global iron use in Escherichia coli. J Bacteriol 187 : 6962 6971.
    • (2005) J Bacteriol , vol.187 , pp. 6962-6971
    • Massé, E.1    Vanderpool, C.K.2    Gottesman, S.3
  • 76
    • 34248359838 scopus 로고    scopus 로고
    • A novel fur- and iron-regulated small RNA, NrrF, is required for indirect fur-mediated regulation of the sdhA and sdhC genes in Neisseria meningitidis
    • Mellin, J.R., Goswami, S., Grogan, S., Tjaden, B. Genco, C.A. (2007) A novel fur- and iron-regulated small RNA, NrrF, is required for indirect fur-mediated regulation of the sdhA and sdhC genes in Neisseria meningitidis. J Bacteriol 189 : 3686 3694.
    • (2007) J Bacteriol , vol.189 , pp. 3686-3694
    • Mellin, J.R.1    Goswami, S.2    Grogan, S.3    Tjaden, B.4    Genco, C.A.5
  • 77
    • 0021738991 scopus 로고
    • Improved plasmid vectors for the isolation of translational lac gene fusions
    • Minton, N.P. (1984) Improved plasmid vectors for the isolation of translational lac gene fusions. Gene 31 : 269 273.
    • (1984) Gene , vol.31 , pp. 269-273
    • Minton, N.P.1
  • 78
    • 33746008173 scopus 로고    scopus 로고
    • Selective silencing of foreign DNA with low GC content by the H-NS protein in Salmonella
    • Navarre, W.W., Porwollik, S., Wang, Y., McClelland, M., Rosen, H., Libby, S.J. Fang, F.C. (2006) Selective silencing of foreign DNA with low GC content by the H-NS protein in Salmonella. Science 313 : 236 238.
    • (2006) Science , vol.313 , pp. 236-238
    • Navarre, W.W.1    Porwollik, S.2    Wang, Y.3    McClelland, M.4    Rosen, H.5    Libby, S.J.6    Fang, F.C.7
  • 79
    • 0002215233 scopus 로고
    • Iron and its role in microbial physiology
    • Neilands, J.B. (ed.). New York. Academic Press
    • Neilands, J.B. (1974) Iron and its role in microbial physiology. In Microbial Iron Metabolism. Neilands, J.B. (ed.). New York : Academic Press, pp. 3 34.
    • (1974) Microbial Iron Metabolism. , pp. 3-34
    • Neilands, J.B.1
  • 80
    • 0019348762 scopus 로고
    • Microbial iron compounds
    • Neilands, J.B. (1981) Microbial iron compounds. Annu Rev Biochem 50 : 715 731.
    • (1981) Annu Rev Biochem , vol.50 , pp. 715-731
    • Neilands, J.B.1
  • 81
    • 0033621203 scopus 로고    scopus 로고
    • Isolation and identification of fur binding genes in Escherichia coli
    • Oh, M., Chai, S.H. Wee, S. (1999) Isolation and identification of Fur binding genes in Escherichia coli. Mol Cells 9 : 517 525.
    • (1999) Mol Cells , vol.9 , pp. 517-525
    • Oh, M.1    Chai, S.H.2    Wee, S.3
  • 82
    • 0032693325 scopus 로고    scopus 로고
    • RpoS function is essential for bgl silencing caused by C-terminally truncated H-NS in Escherichia coli
    • Ohta, T., Ueguchi, C. Mizuno, T. (1999) rpoS function is essential for bgl silencing caused by C-terminally truncated H-NS in Escherichia coli. J Bacteriol 181 : 6278 6283.
    • (1999) J Bacteriol , vol.181 , pp. 6278-6283
    • Ohta, T.1    Ueguchi, C.2    Mizuno, T.3
  • 83
    • 34948824379 scopus 로고    scopus 로고
    • Role of nucleoid-associated proteins Hha and H-NS in expression of Salmonella enterica activators HilD, HilC, and RtsA required for cell invasion
    • Olekhnovich, I.N. Kadner, R.J. (2007) Role of nucleoid-associated proteins Hha and H-NS in expression of Salmonella enterica activators HilD, HilC, and RtsA required for cell invasion. J Bacteriol 189 : 6882 6890.
    • (2007) J Bacteriol , vol.189 , pp. 6882-6890
    • Olekhnovich, I.N.1    Kadner, R.J.2
  • 84
    • 33750898424 scopus 로고    scopus 로고
    • Escherichia coli histone-like protein H-NS preferentially binds to horizontally acquired DNA in association with RNA polymerase
    • Oshima, T., Ishikawa, S., Kurokawa, K., Aiba, H. Ogasawara, N. (2006) Escherichia coli histone-like protein H-NS preferentially binds to horizontally acquired DNA in association with RNA polymerase. DNA Res 13 : 141 153.
    • (2006) DNA Res , vol.13 , pp. 141-153
    • Oshima, T.1    Ishikawa, S.2    Kurokawa, K.3    Aiba, H.4    Ogasawara, N.5
  • 85
    • 0346252350 scopus 로고    scopus 로고
    • Differential regulation of the Proteus mirabilis urease gene cluster by UreR and H-NS
    • Poore, C.A. Mobley, H.L. (2003) Differential regulation of the Proteus mirabilis urease gene cluster by UreR and H-NS. Microbiology 149 : 3383 3394.
    • (2003) Microbiology , vol.149 , pp. 3383-3394
    • Poore, C.A.1    Mobley, H.L.2
  • 86
    • 0034595617 scopus 로고    scopus 로고
    • Lack of a role for iron in the Lyme disease pathogen
    • Posey, J.E. Gherardini, F.C. (2000) Lack of a role for iron in the Lyme disease pathogen. Science 288 : 1651 1653.
    • (2000) Science , vol.288 , pp. 1651-1653
    • Posey, J.E.1    Gherardini, F.C.2
  • 87
    • 17344383264 scopus 로고    scopus 로고
    • Spectroscopic and voltammetric characterisation of the bacterioferritin-associated ferredoxin of Escherichia coli
    • Quail, M.A., Jordan, P., Grogan, J.M., Butt, J.N., Lutz, M., Thomson, A.J., et al. (1996) Spectroscopic and voltammetric characterisation of the bacterioferritin-associated ferredoxin of Escherichia coli. Biochem Biophys Res Commun 229 : 635 642.
    • (1996) Biochem Biophys Res Commun , vol.229 , pp. 635-642
    • Quail, M.A.1    Jordan, P.2    Grogan, J.M.3    Butt, J.N.4    Lutz, M.5    Thomson, A.J.6
  • 88
    • 0035725521 scopus 로고    scopus 로고
    • A molecular mechanism for the repression of transcription by the H-NS protein
    • Rimsky, S., Zuber, F., Buckle, M. Buc, H. (2001) A molecular mechanism for the repression of transcription by the H-NS protein. Mol Microbiol 42 : 1311 1323.
    • (2001) Mol Microbiol , vol.42 , pp. 1311-1323
    • Rimsky, S.1    Zuber, F.2    Buckle, M.3    Buc, H.4
  • 89
    • 0032573426 scopus 로고    scopus 로고
    • A comprehensive library of DNA-binding site matrices for 55 proteins applied to the complete Escherichia coli K-12 genome
    • Robison, K., McGuire, A.M. Church, G.M. (1998) A comprehensive library of DNA-binding site matrices for 55 proteins applied to the complete Escherichia coli K-12 genome. J Mol Biol 284 : 241 254.
    • (1998) J Mol Biol , vol.284 , pp. 241-254
    • Robison, K.1    McGuire, A.M.2    Church, G.M.3
  • 91
    • 0021840332 scopus 로고
    • Nucleotide sequence of the iron regulatory gene fur
    • Schäffer, S., Hantke, K. Braun, V. (1985) Nucleotide sequence of the iron regulatory gene fur. Mol Gen Genet 200 : 110 113.
    • (1985) Mol Gen Genet , vol.200 , pp. 110-113
    • Schäffer, S.1    Hantke, K.2    Braun, V.3
  • 93
    • 0034685608 scopus 로고    scopus 로고
    • The bacterial DNA-binding protein H-NS represses ribosomal RNA transcription by trapping RNA polymerase in the initiation complex
    • Schröder, O. Wagner, R. (2000) The bacterial DNA-binding protein H-NS represses ribosomal RNA transcription by trapping RNA polymerase in the initiation complex. J Mol Biol 298 : 737 748.
    • (2000) J Mol Biol , vol.298 , pp. 737-748
    • Schröder, O.1    Wagner, R.2
  • 94
    • 0036332716 scopus 로고    scopus 로고
    • The bacterial regulatory protein H-NS - A versatile modulator of nucleic acid structures
    • Schröder, O. Wagner, R. (2002) The bacterial regulatory protein H-NS - a versatile modulator of nucleic acid structures. Biol Chem 383 : 945 960.
    • (2002) Biol Chem , vol.383 , pp. 945-960
    • Schröder, O.1    Wagner, R.2
  • 95
    • 0023255472 scopus 로고
    • Improved single and multicopy lac-based cloning vectors for protein and operon fusions
    • Simons, R.W., Houman, F. Kleckner, N. (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
  • 96
    • 0028957883 scopus 로고
    • A small RNA acts as an antisilencer of the H-NS-silenced rcsA gene of Escherichia coli
    • Sledjeski, D. Gottesman, S. (1995) A small RNA acts as an antisilencer of the H-NS-silenced rcsA gene of Escherichia coli. Proc Natl Acad Sci USA 92 : 2003 2007.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2003-2007
    • Sledjeski, D.1    Gottesman, S.2
  • 97
    • 0032796421 scopus 로고    scopus 로고
    • Multiple control of flagellum biosynthesis in Escherichia coli: Role of H-NS protein and the cyclic AMP-catabolite activator protein complex in transcription of the flhDC master operon
    • Soutourina, O., Kolb, A., Krin, E., Laurent-Winter, C., Rimsky, S., Danchin, A. Bertin, P. (1999) Multiple control of flagellum biosynthesis in Escherichia coli: role of H-NS protein and the cyclic AMP-catabolite activator protein complex in transcription of the flhDC master operon. J Bacteriol 181 : 7500 7508.
    • (1999) J Bacteriol , vol.181 , pp. 7500-7508
    • Soutourina, O.1    Kolb, A.2    Krin, E.3    Laurent-Winter, C.4    Rimsky, S.5    Danchin, A.6    Bertin, P.7
  • 98
    • 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
  • 99
    • 53449102029 scopus 로고    scopus 로고
    • Anti-silencing: Overcoming H-NS mediated repression of transcription in Gram-negative enteric bacteria
    • Stoebel, D.M., Free, A. Dorman, C.J. (2008) Anti-silencing: overcoming H-NS mediated repression of transcription in Gram-negative enteric bacteria. Microbiology 154 : 2533 2545.
    • (2008) Microbiology , vol.154 , pp. 2533-2545
    • Stoebel, D.M.1    Free, A.2    Dorman, C.J.3
  • 100
    • 0027255374 scopus 로고
    • Iron and oxygen regulation of Escherichia coli MnSOD expression: Competition between the global regulators fur and ArcA for binding to DNA
    • Tardat, B. Touati, D. (1993) Iron and oxygen regulation of Escherichia coli MnSOD expression: competition between the global regulators Fur and ArcA for binding to DNA. Mol Microbiol 91 : 53 63.
    • (1993) Mol Microbiol , vol.91 , pp. 53-63
    • Tardat, B.1    Touati, D.2
  • 101
    • 0028306747 scopus 로고
    • Evidence for a regulatory function of the histone-like Escherichia coli protein H-NS in ribosomal RNA synthesis
    • Tippner, D., Afflerbach, H., Bradaczek, C. Wagner, R. (1994) Evidence for a regulatory function of the histone-like Escherichia coli protein H-NS in ribosomal RNA synthesis. Mol Microbiol 11 : 589 604.
    • (1994) Mol Microbiol , vol.11 , pp. 589-604
    • Tippner, D.1    Afflerbach, H.2    Bradaczek, C.3    Wagner, R.4
  • 103
    • 0033985228 scopus 로고    scopus 로고
    • Iron and oxidative stress in bacteria
    • Touati, D. (2000) Iron and oxidative stress in bacteria. Arch Biochem Biophys 373 : 1 6.
    • (2000) Arch Biochem Biophys , vol.373 , pp. 1-6
    • Touati, D.1
  • 104
    • 0029041226 scopus 로고
    • Lethal oxidative damage and mutagenesis are generated by iron in delta fur mutants of Escherichia coli: Protective role of superoxide dismutase
    • Touati, D., Jacques, M., Tardat, B., Bouchard, L. Despied, S. (1995) Lethal oxidative damage and mutagenesis are generated by iron in delta fur mutants of Escherichia coli: protective role of superoxide dismutase. J Bacteriol 177 : 2305 2314.
    • (1995) J Bacteriol , vol.177 , pp. 2305-2314
    • Touati, D.1    Jacques, M.2    Tardat, B.3    Bouchard, L.4    Despied, S.5
  • 106
    • 34247579743 scopus 로고    scopus 로고
    • H-NS antagonism in Shigella flexneri by VirB, a virulence gene transcription regulator that is closely related to plasmid partition factors
    • Turner, E.C. Dorman, C.J. (2007) H-NS antagonism in Shigella flexneri by VirB, a virulence gene transcription regulator that is closely related to plasmid partition factors. J Bacteriol 189 : 3403 3413.
    • (2007) J Bacteriol , vol.189 , pp. 3403-3413
    • Turner, E.C.1    Dorman, C.J.2
  • 107
    • 0027408394 scopus 로고
    • The Escherichia coli nucleoid protein H-NS functions directly as a transcriptional repressor
    • Ueguchi, C. Mizuno, T. (1993) The Escherichia coli nucleoid protein H-NS functions directly as a transcriptional repressor. EMBO J 12 : 1039 1046.
    • (1993) EMBO J , vol.12 , pp. 1039-1046
    • Ueguchi, C.1    Mizuno, T.2
  • 108
    • 0036311688 scopus 로고    scopus 로고
    • Role of SdiA in Salmonella enterica serovar Typhimurium physiology and virulence
    • Volf, J., Sevcik, M., Havlickova, H., Sisak, F., Damborsky, J. Rychlik, I. (2002) Role of SdiA in Salmonella enterica serovar Typhimurium physiology and virulence. Arch Microbiol 178 : 94 101.
    • (2002) Arch Microbiol , vol.178 , pp. 94-101
    • Volf, J.1    Sevcik, M.2    Havlickova, H.3    Sisak, F.4    Damborsky, J.5    Rychlik, I.6
  • 109
    • 0025941965 scopus 로고
    • A factor that positively regulates cell division by activating transcription of the major cluster of essential cell division genes of Escherichia coli
    • Wang, X.D., de Boer, P.A. Rothfield, L.I. (1991) A factor that positively regulates cell division by activating transcription of the major cluster of essential cell division genes of Escherichia coli. EMBO J 10 : 3363 3372.
    • (1991) EMBO J , vol.10 , pp. 3363-3372
    • Wang, X.D.1    De Boer, P.A.2    Rothfield, L.I.3
  • 110
    • 0031033529 scopus 로고    scopus 로고
    • Purification of Vibrio cholerae fur and estimation of its intracellular abundance by antibody sandwich enzyme-linked immunosorbent assay
    • Watnick, P.I., Eto, T., Takahashi, H. Calderwood, S.B. (1997) Purification of Vibrio cholerae fur and estimation of its intracellular abundance by antibody sandwich enzyme-linked immunosorbent assay. J Bacteriol 179 : 243 247.
    • (1997) J Bacteriol , vol.179 , pp. 243-247
    • Watnick, P.I.1    Eto, T.2    Takahashi, H.3    Calderwood, S.B.4
  • 111
    • 0024152952 scopus 로고
    • Expression, isolation and properties of fur (ferric uptake regulation) protein of Escherichia coli K 12
    • Wee, S., Neilands, J.B., Bittner, M.L., Hemming, B.C., Haymore, B.L. Seetharam, R. (1988) Expression, isolation and properties of Fur (ferric uptake regulation) protein of Escherichia coli K 12. Biol Met 1 : 62 68.
    • (1988) Biol Met , vol.1 , pp. 62-68
    • Wee, S.1    Neilands, J.B.2    Bittner, M.L.3    Hemming, B.C.4    Haymore, B.L.5    Seetharam, R.6
  • 113
  • 115
    • 0034935287 scopus 로고    scopus 로고
    • Nonradiochemical DNase i footprinting by capillary electrophoresis
    • Wilson, D.O., Johnson, P. McCord, B.R. (2001) Nonradiochemical DNase I footprinting by capillary electrophoresis. Electrophoresis 22 : 1979 1986.
    • (2001) Electrophoresis , vol.22 , pp. 1979-1986
    • Wilson, D.O.1    Johnson, P.2    McCord, B.R.3
  • 116
    • 1542286940 scopus 로고    scopus 로고
    • Regulation of Escherichia coli hemolysin e expression by H-NS and Salmonella SlyA
    • Wyborn, N.R., Stapleton, M.R., Norte, V.A., Roberts, R.E., Grafton, J. Green, J. (2004) Regulation of Escherichia coli hemolysin E expression by H-NS and Salmonella SlyA. J Bacteriol 186 : 1620 1628.
    • (2004) J Bacteriol , vol.186 , pp. 1620-1628
    • Wyborn, N.R.1    Stapleton, M.R.2    Norte, V.A.3    Roberts, R.E.4    Grafton, J.5    Green, J.6
  • 117
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., Vieira, J. Messing, J. (1985) Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33 : 103 119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 118
    • 0037008743 scopus 로고    scopus 로고
    • Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells. A ferritin-like DNA-binding protein of Escherichia coli
    • Zhao, G., Ceci, P., Ilari, A., Giangiacomo, L., Laue, T.M., Chiancone, E. Chasteen, N.D. (2002) Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells. A ferritin-like DNA-binding protein of Escherichia coli. J Biol Chem 277 : 27689 27696.
    • (2002) J Biol Chem , vol.277 , pp. 27689-27696
    • Zhao, G.1    Ceci, P.2    Ilari, A.3    Giangiacomo, L.4    Laue, T.M.5    Chiancone, E.6    Chasteen, N.D.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.