메뉴 건너뛰기




Volumn 244, Issue 3, 1997, Pages 767-773

Role of Escherichia coli histone-like nucleoid-structuring protein in bacterial metabolism and stress response - Identification of targets by two-dimensional electrophoresis

Author keywords

Histone like nucleoid structuring protein; Metabolism regulator; Molecular chaperone; Stress response; Two dimensional electrophoresis

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN; HISTONE;

EID: 0030983671     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00767.x     Document Type: Article
Times cited : (61)

References (55)
  • 2
    • 0029983427 scopus 로고    scopus 로고
    • Federated two-dimensional electrophoresis database: A simple means of publishing two-dimensional electrophoresis data
    • Appel, R. D., Bairoch, A., Sanchez, J. C., Vargas, J. R., Golaz, O., Pasquali, C. & Hochstrasser, D. F. (1996) Federated two-dimensional electrophoresis database: a simple means of publishing two-dimensional electrophoresis data, Electrophoresis 17, 540-546.
    • (1996) Electrophoresis , vol.17 , pp. 540-546
    • Appel, R.D.1    Bairoch, A.2    Sanchez, J.C.3    Vargas, J.R.4    Golaz, O.5    Pasquali, C.6    Hochstrasser, D.F.7
  • 3
    • 0022465774 scopus 로고
    • Regulation of envelope protein composition during adaptation to osmotic stress in Escherichia coli
    • Barron, A., May, G., Bremer, E. & Villarejo, M. (1986) Regulation of envelope protein composition during adaptation to osmotic stress in Escherichia coli, J. Bacteriol. 167, 433-438.
    • (1986) J. Bacteriol. , vol.167 , pp. 433-438
    • Barron, A.1    May, G.2    Bremer, E.3    Villarejo, M.4
  • 4
    • 0023664892 scopus 로고
    • Purification and characterization of a glycine betaine binding protein from Escherichia coli
    • Barron, A., Jung, J. U. & Villarejo, M. (1987) Purification and characterization of a glycine betaine binding protein from Escherichia coli, J. Biol. Chem. 262, 11841-11846.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11841-11846
    • Barron, A.1    Jung, J.U.2    Villarejo, M.3
  • 6
    • 0025672667 scopus 로고
    • Mutations in bglY, the structural gene for the DNA-binding protein H1, affect expression of several Escherichia coli genes
    • Bertin, P., Lejeune, P., Laurent-Winter, C. & Danchin, A. (1990) Mutations in bglY, the structural gene for the DNA-binding protein H1, affect expression of several Escherichia coli genes, Biochimie (Paris) 72, 889-891.
    • (1990) Biochimie (Paris) , vol.72 , pp. 889-891
    • Bertin, P.1    Lejeune, P.2    Laurent-Winter, C.3    Danchin, A.4
  • 8
    • 0030271687 scopus 로고    scopus 로고
    • In vivo positive effects of exogenous pyrophosphate on Escherichia coli cell growth and stationary phase survival
    • Biville, F., Laurent-Winter, C. & Danchin, A. (1996) In vivo positive effects of exogenous pyrophosphate on Escherichia coli cell growth and stationary phase survival, Res. Microbiol. 147, 597-608.
    • (1996) Res. Microbiol. , vol.147 , pp. 597-608
    • Biville, F.1    Laurent-Winter, C.2    Danchin, A.3
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 10
    • 0017387646 scopus 로고
    • Biochemical and regulatory properties of Escherichia coli K-12 HisT mutants
    • Bruni, C. B., Colantuoni, V., Sbordone, L., Cortese, R. & Blasi, F. (1977) Biochemical and regulatory properties of Escherichia coli K-12 HisT mutants, J. Bacteriol. 130, 4-10.
    • (1977) J. Bacteriol. , vol.130 , pp. 4-10
    • Bruni, C.B.1    Colantuoni, V.2    Sbordone, L.3    Cortese, R.4    Blasi, F.5
  • 11
    • 0028111825 scopus 로고
    • The leucine-responsive regulatory protein, a global regulator of metabolism in Escherichia coli
    • Calvo, J. M. & Matthews, R. (1994) The leucine-responsive regulatory protein, a global regulator of metabolism in Escherichia coli, Microbiol. Rev. 58, 466-490.
    • (1994) Microbiol. Rev. , vol.58 , pp. 466-490
    • Calvo, J.M.1    Matthews, R.2
  • 12
    • 0029084928 scopus 로고
    • H-NS regulation of virulence gene expression in enteroinvasive Escherichia coli harboring the virulence plasmid integrated into the host chromosome
    • Colonna, B., Casalino, M., Fradiani, P. A., Zagaglia, C., Naitza, S., Leoni, L., Prosseda, G., Coppo, A., Ghelardini, P. & Nicoletti, M. (1995) H-NS regulation of virulence gene expression in enteroinvasive Escherichia coli harboring the virulence plasmid integrated into the host chromosome, J. Bacteriol. 177, 4703-4712.
    • (1995) J. Bacteriol. , vol.177 , pp. 4703-4712
    • Colonna, B.1    Casalino, M.2    Fradiani, P.A.3    Zagaglia, C.4    Naitza, S.5    Leoni, L.6    Prosseda, G.7    Coppo, A.8    Ghelardini, P.9    Nicoletti, M.10
  • 13
    • 0028882958 scopus 로고
    • Mycobacterium tuberculosis is a natural mutant with an inactivated oxydative-stress regulatory gene: Implications for sensitivity to isoniazid
    • Deretic, V., Philipp, W., Dhandayuthapani, S., Mudd, M. H., Curcic, R., Garbe, T., Heym, B., Via, L. E. & Cole, S. T. (1995) Mycobacterium tuberculosis is a natural mutant with an inactivated oxydative-stress regulatory gene: implications for sensitivity to isoniazid, Mol. Microbiol. 17, 889-900.
    • (1995) Mol. Microbiol. , vol.17 , pp. 889-900
    • Deretic, V.1    Philipp, W.2    Dhandayuthapani, S.3    Mudd, M.H.4    Curcic, R.5    Garbe, T.6    Heym, B.7    Via, L.E.8    Cole, S.T.9
  • 14
    • 0025342874 scopus 로고
    • DNA supercoiling and environmental regulation of virulence gene expression in Shigella flexneri
    • Dorman, C. J., Ni Bhriain, N. & Higgins, C. F. (1990) DNA supercoiling and environmental regulation of virulence gene expression in Shigella flexneri, Nature 344, 789-792.
    • (1990) Nature , vol.344 , pp. 789-792
    • Dorman, C.J.1    Ni Bhriain, N.2    Higgins, C.F.3
  • 15
    • 0026505534 scopus 로고
    • Characterization of the regulon controlled by the leucine-responsive regulatory protein in Escherichia coli
    • Ernsting, B. R., Atkinson, M. R., Ninfa, A. J. & Matthews, R. G. (1992) Characterization of the regulon controlled by the leucine-responsive regulatory protein in Escherichia coli, J. Bacteriol. 174, 1109-1118.
    • (1992) J. Bacteriol. , vol.174 , pp. 1109-1118
    • Ernsting, B.R.1    Atkinson, M.R.2    Ninfa, A.J.3    Matthews, R.G.4
  • 16
    • 0020971322 scopus 로고
    • Qantitative two-dimensional gel electrophoresis of proteins
    • Garrels, J. I. (1983) Qantitative two-dimensional gel electrophoresis of proteins, Methods Enzymol. 100, 411-423.
    • (1983) Methods Enzymol. , vol.100 , pp. 411-423
    • Garrels, J.I.1
  • 17
    • 0000757557 scopus 로고
    • Properties of the heat shock proteins of Escherichia coli and the autoregulation of the heat shock response
    • Morimoto, R. I., Tissières, A. & Georgopoulos, C., eds Cold Spring Harbor Laboratory Press, Cold Spring Harbor NY
    • Georgopoulos, C., Liberek, K., Zylicz, M. & Ang, D. (1994) Properties of the heat shock proteins of Escherichia coli and the autoregulation of the heat shock response, in The biology of heat shock proteins and molecular chaperones (Morimoto, R. I., Tissières, A. & Georgopoulos, C., eds) pp. 209-250, Cold Spring Harbor Laboratory Press, Cold Spring Harbor NY.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 209-250
    • Georgopoulos, C.1    Liberek, K.2    Zylicz, M.3    Ang, D.4
  • 18
    • 0029844676 scopus 로고    scopus 로고
    • FIS is a regulator of metabolism in Escherichia coli
    • Gonzalez-Gil, G., Bringmann, P. & Kahmann, R. (1996) FIS is a regulator of metabolism in Escherichia coli, Mol. Microbiol. 22, 21-29.
    • (1996) Mol. Microbiol. , vol.22 , pp. 21-29
    • Gonzalez-Gil, G.1    Bringmann, P.2    Kahmann, R.3
  • 19
    • 0024726275 scopus 로고
    • Osmotic regulation of porin expression: A role for DNA supercoiling
    • Graeme-Cook, K. A., May, G., Bremer, E. & Higgins, C. F. (1989) Osmotic regulation of porin expression: a role for DNA supercoiling, Mol. Microbiol. 3, 1287-1294.
    • (1989) Mol. Microbiol. , vol.3 , pp. 1287-1294
    • Graeme-Cook, K.A.1    May, G.2    Bremer, E.3    Higgins, C.F.4
  • 21
    • 0030034307 scopus 로고    scopus 로고
    • Heat-shock and general stress response in Bacillus subtilis
    • Hecker, M., Schumann, W. & Völker, U. (1996) Heat-shock and general stress response in Bacillus subtilis, Mol. Microbiol. 19, 417-428.
    • (1996) Mol. Microbiol. , vol.19 , pp. 417-428
    • Hecker, M.1    Schumann, W.2    Völker, U.3
  • 22
    • 0023833060 scopus 로고
    • A physiological role for DNA supercoiling in the osmotic regulation of gene expression in S. typhimurium and E. coli
    • Higgins, C. F., Dorman, C. J., Stirling, D. A., Waddell, L., Booth, I. R., May, G. & Bremer, E. (1988) A physiological role for DNA supercoiling in the osmotic regulation of gene expression in S. typhimurium and E. coli, Cell 52, 569-584.
    • (1988) Cell , vol.52 , pp. 569-584
    • Higgins, C.F.1    Dorman, C.J.2    Stirling, D.A.3    Waddell, L.4    Booth, I.R.5    May, G.6    Bremer, E.7
  • 23
    • 0026661849 scopus 로고
    • Expression and mutational analysis of the nucleoid-associated protein H-NS of Salmonella typhimurium
    • Hinton, J. C. D., Santos, D. S., Seirafi, A., Hulton, C. S. J., Pavitt, G. D. & Higgins, C. F. (1992) Expression and mutational analysis of the nucleoid-associated protein H-NS of Salmonella typhimurium, Mol. Microbiol. 6, 2327-2337.
    • (1992) Mol. Microbiol. , vol.6 , pp. 2327-2337
    • Hinton, J.C.D.1    Santos, D.S.2    Seirafi, A.3    Hulton, C.S.J.4    Pavitt, G.D.5    Higgins, C.F.6
  • 24
    • 0027158766 scopus 로고
    • Pilus and nonpilus bacterial adhesins: Assembly and function in cell recognition
    • Hultgren, S. J., Abraham, S., Caparon, M., Falk, P., Geme, J. W. St III & Normark, S. (1993) Pilus and nonpilus bacterial adhesins: assembly and function in cell recognition, Cell 73, 887-901.
    • (1993) Cell , vol.73 , pp. 887-901
    • Hultgren, S.J.1    Abraham, S.2    Caparon, M.3    Falk, P.4    Geme III, J.W.St.5    Normark, S.6
  • 26
    • 0026035207 scopus 로고
    • Role of RpoH, a heat shock regulator protein, in Escherichia coli carbon starvation protein synthesis and survival
    • Jenkins, D. E., Auger, E. A. & Matin, A. (1991) Role of RpoH, a heat shock regulator protein, in Escherichia coli carbon starvation protein synthesis and survival, J. Bacteriol. 173, 1992-1996.
    • (1991) J. Bacteriol. , vol.173 , pp. 1992-1996
    • Jenkins, D.E.1    Auger, E.A.2    Matin, A.3
  • 27
    • 0025814531 scopus 로고
    • Sequencing, mutational analysis, and transcriptional regulation of the Escherichia coli htrB gene
    • Karow, M. & Georgopoulos, C. (1991) Sequencing, mutational analysis, and transcriptional regulation of the Escherichia coli htrB gene, Mol. Microbiol. 5, 2285-2292.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2285-2292
    • Karow, M.1    Georgopoulos, C.2
  • 28
    • 0028082094 scopus 로고
    • Mutations in a gene encoding a new hsp70 suppress rapid DNA inversion and bgl activation, but not proU derepression, in hns-1 mutant Escherichia coli
    • Kawula, T. H. & Lelivelt, M. J. (1994) Mutations in a gene encoding a new hsp70 suppress rapid DNA inversion and bgl activation, but not proU derepression, in hns-1 mutant Escherichia coli, J. Bacteriol. 176, 610-619.
    • (1994) J. Bacteriol. , vol.176 , pp. 610-619
    • Kawula, T.H.1    Lelivelt, M.J.2
  • 29
    • 0028888071 scopus 로고
    • The Escherichia coli DNA-binding protein H-NS is one of the first proteins to be synthesized after a nutritional upshift
    • Laurent-Winter, C., Lejeune, P. & Danchin, A. (1995) The Escherichia coli DNA-binding protein H-NS is one of the first proteins to be synthesized after a nutritional upshift, Res. Microbiol. 146, 5-16.
    • (1995) Res. Microbiol. , vol.146 , pp. 5-16
    • Laurent-Winter, C.1    Lejeune, P.2    Danchin, A.3
  • 30
    • 0028288422 scopus 로고
    • The H-NS protein modulates the activation of the ilvIH operon of Escherichia coli K12 by Lrp, the leucine regulatory protein
    • Levinthal, M., Lejeune, P. & Danchin, A. (1994) The H-NS protein modulates the activation of the ilvIH operon of Escherichia coli K12 by Lrp, the leucine regulatory protein, Mol. Gen. Genet. 242, 736-743.
    • (1994) Mol. Gen. Genet. , vol.242 , pp. 736-743
    • Levinthal, M.1    Lejeune, P.2    Danchin, A.3
  • 31
    • 0028075844 scopus 로고
    • Acetyl phosphate and the activation of two-component response regulators
    • McCleary, W. R. & Stock, J. B. (1994) Acetyl phosphate and the activation of two-component response regulators, J. Biol. Chem. 269, 31567-31572.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31567-31572
    • McCleary, W.R.1    Stock, J.B.2
  • 32
    • 0025123398 scopus 로고
    • The osmZ (bglY) gene encodes the DNA-binding protein H-NS (H1a), a component of the Escherichia coli K12 nucleoid
    • May, G., Dersch, P., Haardt, M., Middendorf, A. & Bremer, E. (1990) The osmZ (bglY) gene encodes the DNA-binding protein H-NS (H1a), a component of the Escherichia coli K12 nucleoid, Mol. Gen. Genet. 224, 81-90.
    • (1990) Mol. Gen. Genet. , vol.224 , pp. 81-90
    • May, G.1    Dersch, P.2    Haardt, M.3    Middendorf, A.4    Bremer, E.5
  • 34
    • 0027985236 scopus 로고
    • Role of guanosine tetraphosphate in gene expression and the survival of glucose or seryl-tRNA starved cells of Escherichia coli K12
    • Nyström, T. (1994) Role of guanosine tetraphosphate in gene expression and the survival of glucose or seryl-tRNA starved cells of Escherichia coli K12, Mol. Gen. Genet. 245, 355-362.
    • (1994) Mol. Gen. Genet. , vol.245 , pp. 355-362
    • Nyström, T.1
  • 35
    • 0029560549 scopus 로고
    • Glucose starvation stimulon of Escherichia coli: Role of integration host factor in starvation survival and growth phase-dependent protein synthesis
    • Nyström, T. (1995) Glucose starvation stimulon of Escherichia coli: role of integration host factor in starvation survival and growth phase-dependent protein synthesis, J. Bacteriol. 177, 5707-5710.
    • (1995) J. Bacteriol. , vol.177 , pp. 5707-5710
    • Nyström, T.1
  • 36
    • 0030066140 scopus 로고    scopus 로고
    • Effects of overproducing the universal stress protein, UspA, in Escherichia coli K-12
    • Nyström, T. & Neidhardt, F. C. (1996) Effects of overproducing the universal stress protein, UspA, in Escherichia coli K-12, J. Bacteriol. 178, 927-930.
    • (1996) J. Bacteriol. , vol.178 , pp. 927-930
    • Nyström, T.1    Neidhardt, F.C.2
  • 37
    • 0028977927 scopus 로고
    • Regulation of lrp gene expression by H-NS and Lrp proteins in Escherichia coli: Dominant negative mutations in lrp
    • Oshima, T., Ito, K., Kabayama, H. & Nakamura, Y. (1995) Regulation of lrp gene expression by H-NS and Lrp proteins in Escherichia coli: dominant negative mutations in lrp, Mol. Gen. Genet. 247, 521-528.
    • (1995) Mol. Gen. Genet. , vol.247 , pp. 521-528
    • Oshima, T.1    Ito, K.2    Kabayama, H.3    Nakamura, Y.4
  • 39
    • 0028340662 scopus 로고
    • Regulation of acetyl phosphate synthesis and degradation, and the control of flagellar expression in Escherichia coli
    • Prüss, B. M. & Wolfe, A. J. (1994) Regulation of acetyl phosphate synthesis and degradation, and the control of flagellar expression in Escherichia coli, Mol. Microbiol. 12, 973-984.
    • (1994) Mol. Microbiol. , vol.12 , pp. 973-984
    • Prüss, B.M.1    Wolfe, A.J.2
  • 40
    • 0029095544 scopus 로고
    • Salmonella typhimurium responses to a bactericidal protein from human neutrophils
    • Qi, S. Y., Li, Y., Szyroki, A., Giles, I. G., Moir, A. & O'Connor, C. D. (1995) Salmonella typhimurium responses to a bactericidal protein from human neutrophils, Mol. Microbiol. 17, 523-531.
    • (1995) Mol. Microbiol. , vol.17 , pp. 523-531
    • Qi, S.Y.1    Li, Y.2    Szyroki, A.3    Giles, I.G.4    Moir, A.5    O'Connor, C.D.6
  • 41
    • 0030003403 scopus 로고    scopus 로고
    • Analysis of global responses by protein and peptide fingerprinting of proteins isolated by two-dimensional gel electrophoresis. Application to the sulfate-starvation response of Escherichia coli
    • Quadroni, M., Staudenmann, W., Kertesz, M. & James, P. (1996) Analysis of global responses by protein and peptide fingerprinting of proteins isolated by two-dimensional gel electrophoresis. Application to the sulfate-starvation response of Escherichia coli, Eur. J. Biochem. 239, 773-781.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 773-781
    • Quadroni, M.1    Staudenmann, W.2    Kertesz, M.3    James, P.4
  • 42
    • 0017802555 scopus 로고
    • Permease-specific mutations in Salmonella typhymurium and Escherichia coli that release the glycerol, maltose, melibiose, and lactose transport systems from regulation by the phosphoenolpyruvate:sugar phosphotransferase system
    • Saier, M. H. Jr, Straud, H., Massman, L. S., Judice, J. J., Newman, M. J. & Feucht, B. U. (1978) Permease-specific mutations in Salmonella typhymurium and Escherichia coli that release the glycerol, maltose, melibiose, and lactose transport systems from regulation by the phosphoenolpyruvate:sugar phosphotransferase system, J. Bacteriol. 133, 1358-1367.
    • (1978) J. Bacteriol. , vol.133 , pp. 1358-1367
    • Saier Jr., M.H.1    Straud, H.2    Massman, L.S.3    Judice, J.J.4    Newman, M.J.5    Feucht, B.U.6
  • 43
    • 0029130181 scopus 로고
    • Modulation of flagellar expression in Escherichia coli by acetyl phosphate and the osmoregulator OmpR
    • Shin, S. & Park, C. (1995) Modulation of flagellar expression in Escherichia coli by acetyl phosphate and the osmoregulator OmpR, J. Bacteriol. 177, 4696-4702.
    • (1995) J. Bacteriol. , vol.177 , pp. 4696-4702
    • Shin, S.1    Park, C.2
  • 44
    • 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
  • 45
    • 0029116083 scopus 로고
    • Characterisation of the yenI/yenR locus from Yersinia enterocolitica mediating the synthesis of two N-acylhomoserine lactone signal molecules
    • Throup, J. P., Camara, M., Briggs, G. S., Winson, M. K., Chhabra, S. R., Bycroft, B. W., Williams, P. & Stewart, G. S. A. B. (1995) Characterisation of the yenI/yenR locus from Yersinia enterocolitica mediating the synthesis of two N-acylhomoserine lactone signal molecules, Mol. Microbiol. 17, 345-356.
    • (1995) Mol. Microbiol. , vol.17 , pp. 345-356
    • Throup, J.P.1    Camara, M.2    Briggs, G.S.3    Winson, M.K.4    Chhabra, S.R.5    Bycroft, B.W.6    Williams, P.7    Stewart, G.S.A.B.8
  • 46
    • 0030057627 scopus 로고    scopus 로고
    • Global response of Escherichia coli cells to a treatment with 7-metoxy-2-nitronaphto [2, 1b] furan (R7000), an extremely potent mutagen
    • Touati, E., Laurent-Winter, C., Quillardet, P. & Hoffnung, M. (1996) Global response of Escherichia coli cells to a treatment with 7-metoxy-2-nitronaphto [2, 1b] furan (R7000), an extremely potent mutagen, Mutation Res. 349, 193-200.
    • (1996) Mutation Res. , vol.349 , pp. 193-200
    • Touati, E.1    Laurent-Winter, C.2    Quillardet, P.3    Hoffnung, M.4
  • 48
    • 0000087068 scopus 로고    scopus 로고
    • Gene-protein database of Escherichia coli K-12
    • edition 6, Neidhardt, F. C., Curtis, R. III, Ingraham, J. L., Lin, E. C. C., Low, K. B., Magasanik, B., Reznikoff, W. S., Riley, M., Schaechter, M. & Umbarger, H. E., eds 2nd edn, ASM Press, Washington DC
    • Van Bogelen, R. A., Abshire, K. Z., Pertsemlidis, A., Clark, R. L. & Neidhardt, F. C. (1996) Gene-protein database of Escherichia coli K-12, edition 6, in Escherichia coli and Salmonella: cellular and molecular biology (Neidhardt, F. C., Curtis, R. III, Ingraham, J. L., Lin, E. C. C., Low, K. B., Magasanik, B., Reznikoff, W. S., Riley, M., Schaechter, M. & Umbarger, H. E., eds) pp. 2067-2117, 2nd edn, ASM Press, Washington DC.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology , pp. 2067-2117
    • Van Bogelen, R.A.1    Abshire, K.Z.2    Pertsemlidis, A.3    Clark, R.L.4    Neidhardt, F.C.5
  • 49
    • 0024554109 scopus 로고
    • Escherichia coli proteins inducible by oxydative stress mediated by the superoxyde radical
    • Walkup, L. K. B. & Kogoma, T. (1989) Escherichia coli proteins inducible by oxydative stress mediated by the superoxyde radical, J. Bacteriol. 171, 1476-1484.
    • (1989) J. Bacteriol. , vol.171 , pp. 1476-1484
    • Walkup, L.K.B.1    Kogoma, T.2
  • 50
    • 0027370350 scopus 로고
    • Stress response of Escherichia coli to elevated hydrostatic pressure
    • Welch, T. J., Farewell, A., Neidhardt, F. C. & Bartlett, D. H. (1993) Stress response of Escherichia coli to elevated hydrostatic pressure, J. Bacteriol. 175, 7170-7177.
    • (1993) J. Bacteriol. , vol.175 , pp. 7170-7177
    • Welch, T.J.1    Farewell, A.2    Neidhardt, F.C.3    Bartlett, D.H.4
  • 51
    • 0025003429 scopus 로고
    • An Escherichia coli protein that preferentially binds to sharply curved DNA
    • Yamada, H., Muramatsu, S. & Mizuno, T. (1990) An Escherichia coli protein that preferentially binds to sharply curved DNA, J. Biochem. (Tokyo) 108, 420-425.
    • (1990) J. Biochem. (Tokyo) , vol.108 , pp. 420-425
    • Yamada, H.1    Muramatsu, S.2    Mizuno, T.3
  • 52
    • 0026250129 scopus 로고
    • Molecular analysis of the Escherichia coli hns gene encoding a DNA-binding protein, which preferentially recognizes curved DNA sequences
    • Yamada, H., Yoshida, T., Tanaka, K., Sasakawa, C. & Mizuno, T. (1991) Molecular analysis of the Escherichia coli hns gene encoding a DNA-binding protein, which preferentially recognizes curved DNA sequences, Mol. Gen. Genet. 230, 332-336.
    • (1991) Mol. Gen. Genet. , vol.230 , pp. 332-336
    • Yamada, H.1    Yoshida, T.2    Tanaka, K.3    Sasakawa, C.4    Mizuno, T.5
  • 53
    • 0028895391 scopus 로고
    • s, in Escherichia coli: Involvement of the nucleoid protein H-NS
    • s, in Escherichia coli: involvement of the nucleoid protein H-NS, EMBO J. 14, 594-602.
    • (1995) EMBO J. , vol.14 , pp. 594-602
    • Yamashino, T.1    Ueguchi, C.2    Mizuno, T.3
  • 54
    • 0027666044 scopus 로고
    • Expression of the Escherichia coli dimorphic glutamic acid decarboxylases is regulated by the nucleoid protein H-NS
    • Yoshida, T., Yamashino, T., Ueguchi, C. & Mizuno, T. (1993) Expression of the Escherichia coli dimorphic glutamic acid decarboxylases is regulated by the nucleoid protein H-NS, Biosci. Biotechnol. Biochem. 57, 1568-1569.
    • (1993) Biosci. Biotechnol. Biochem. , vol.57 , pp. 1568-1569
    • Yoshida, T.1    Yamashino, T.2    Ueguchi, C.3    Mizuno, T.4
  • 55
    • 0029913710 scopus 로고    scopus 로고
    • Escherichia coli protein analogs StpA and H-NS: Regulatory loops, similar and disparate effects on nucleic acid dynamics
    • Zhang, A., Rimsky, S., Reaban, M. E., Buc, H. & Belfort, M. (1996) Escherichia coli protein analogs StpA and H-NS: regulatory loops, similar and disparate effects on nucleic acid dynamics, EMBO J. 15, 1340-1349.
    • (1996) EMBO J. , vol.15 , pp. 1340-1349
    • Zhang, A.1    Rimsky, S.2    Reaban, M.E.3    Buc, H.4    Belfort, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.