메뉴 건너뛰기




Volumn 142, Issue 9, 1996, Pages 2471-2479

Isolation of Borvelia burgdorferi genes encoding homologues of DNA-binding protein HU and ribosomal protein S20

Author keywords

Borrelia burgdorferi; HU protein; Integration host factor (IHF); Lyme disease

Indexed keywords

DNA BINDING PROTEIN; RHO FACTOR; RIBOSOME PROTEIN;

EID: 0029784913     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/00221287-142-9-2471     Document Type: Article
Times cited : (25)

References (65)
  • 1
    • 0026027218 scopus 로고
    • A consensus motif common to all Rho-dependent prokaryotic transcription terminators
    • Alifano, P., Rivellini, F., Limauro, D., Bruni, C. B. & Carlomagno, M. S. (1991). A consensus motif common to all Rho-dependent prokaryotic transcription terminators. Cell 64, 553-563.
    • (1991) Cell , vol.64 , pp. 553-563
    • Alifano, P.1    Rivellini, F.2    Limauro, D.3    Bruni, C.B.4    Carlomagno, M.S.5
  • 4
    • 0023663587 scopus 로고
    • Linear plasmids of the bacterium Borrelia burgdorferi have covalently closed ends
    • Barbour, A. G. & Garon, C. F. (1987). Linear plasmids of the bacterium Borrelia burgdorferi have covalently closed ends. Science 237, 409-411.
    • (1987) Science , vol.237 , pp. 409-411
    • Barbour, A.G.1    Garon, C.F.2
  • 5
    • 0023013908 scopus 로고
    • Biology of Borrelia species
    • Barbour, A. G. & Hayes, S. F. (1986). Biology of Borrelia species. Microbiol Rev 50, 381-400.
    • (1986) Microbiol Rev , vol.50 , pp. 381-400
    • Barbour, A.G.1    Hayes, S.F.2
  • 7
    • 0028136642 scopus 로고
    • DNA-binding parameters of the HU protein of Escherichia coli to cruciform DNA
    • Bonnefoy, E., Takahashi, M. & Yaniv, J. R. (1994). DNA-binding parameters of the HU protein of Escherichia coli to cruciform DNA. J Mol Biol 242, 116-129.
    • (1994) J Mol Biol , vol.242 , pp. 116-129
    • Bonnefoy, E.1    Takahashi, M.2    Yaniv, J.R.3
  • 8
    • 0027281173 scopus 로고
    • Linear chromosomal physical and genetic map of Borrelia burgdorferi, the Lyme disease agent
    • Casjens, S. & Huang, W. M. (1993). Linear chromosomal physical and genetic map of Borrelia burgdorferi, the Lyme disease agent. Mol Microbiol 8, 967-980.
    • (1993) Mol Microbiol , vol.8 , pp. 967-980
    • Casjens, S.1    Huang, W.M.2
  • 9
    • 0019497401 scopus 로고
    • A histone-like protein (HTa) from Thermoplasma acidophilum. II. Complete amino acid sequence
    • DeLange, R. J., Williams, L. C. & Searcy, D. G. (1981). A histone-like protein (HTa) from Thermoplasma acidophilum. II. Complete amino acid sequence. J Biol Chem 256, 905-911.
    • (1981) J Biol Chem , vol.256 , pp. 905-911
    • DeLange, R.J.1    Williams, L.C.2    Searcy, D.G.3
  • 10
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., Haeberli, P. & Smithies, O. (1984). A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res 12, 387-395.
    • (1984) Nucleic Acids Res , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 11
    • 0023413620 scopus 로고
    • Histonelike proteins of bacteria
    • Drlica, K. & Rouviere-Yaniv, J. (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
  • 12
    • 0024419262 scopus 로고
    • Megabase-sized linear DNA in the bacterium Borrelia burgdorferi, the Lyme disease agent
    • Ferdows, M. S. & Barbour, A. G. (1989). Megabase-sized linear DNA in the bacterium Borrelia burgdorferi, the Lyme disease agent. Proc Natl Acad Sci USA 86, 5969-5973.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 5969-5973
    • Ferdows, M.S.1    Barbour, A.G.2
  • 13
    • 0022204793 scopus 로고
    • Primary structure of the hip gene of Escherichia coli and of its product, the beta subunit of integration host factor
    • Flamm, E. L. & Weisberg, R. A. (1985). Primary structure of the hip gene of Escherichia coli and of its product, the beta subunit of integration host factor. J Mol Biol 183, 117-128.
    • (1985) J Mol Biol , vol.183 , pp. 117-128
    • Flamm, E.L.1    Weisberg, R.A.2
  • 14
    • 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
  • 15
    • 0005403121 scopus 로고
    • Escherichia coli mutants blocked in lambda DNA synthesis
    • Edited by A. D. Hershey. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory
    • Georgopoulos, C. P. & Herskowitz, I. (1971). Escherichia coli mutants blocked in lambda DNA synthesis. In The Bacteriophage Lambda, pp. 553-564. Edited by A. D. Hershey. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory.
    • (1971) The Bacteriophage Lambda , pp. 553-564
    • Georgopoulos, C.P.1    Herskowitz, I.2
  • 16
    • 0026675837 scopus 로고
    • Isolation and characterization of the hup A gene coding for HU of Aeromonas proteolytica
    • Giladi, H., Wang, W.-X. & Oppenheim, A. B. (1992). Isolation and characterization of the hup A gene coding for HU of Aeromonas proteolytica. Nucleic Acids Res 20, 4092.
    • (1992) Nucleic Acids Res , vol.20 , pp. 4092
    • Giladi, H.1    Wang, W.-X.2    Oppenheim, A.B.3
  • 17
    • 0021747911 scopus 로고
    • Sequence of the bacteriophage SP01 gene coding for transcription factor 1, a viral homologue of the bacterial type II DNA-binding proteins
    • Greene, J. R., Brennan, S. M., Andrew, D. J., Thompson, C. C., Richards, S. H., Heinrikson, R. L. & Geiduschek, E. P. (1984). Sequence of the bacteriophage SP01 gene coding for transcription factor 1, a viral homologue of the bacterial type II DNA-binding proteins. Proc Natl Acad Sci USA 81, 7031-7035.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 7031-7035
    • Greene, J.R.1    Brennan, S.M.2    Andrew, D.J.3    Thompson, C.C.4    Richards, S.H.5    Heinrikson, R.L.6    Geiduschek, E.P.7
  • 20
    • 0025746558 scopus 로고
    • Linear plasmids of Borrelia burgdorferi have a telomeric structure and sequence similar to those of a eukaryotic virus
    • Hinnebusch, J. & Barbour, A. G. (1991). Linear plasmids of Borrelia burgdorferi have a telomeric structure and sequence similar to those of a eukaryotic virus. J Bacteriol 173, 7233-7239.
    • (1991) J Bacteriol , vol.173 , pp. 7233-7239
    • Hinnebusch, J.1    Barbour, A.G.2
  • 21
    • 0025375673 scopus 로고
    • Cloning and sequence analysis of linear plasmid telomeres of the bacterium Borrelia burgdorferi
    • Hinnebusch, J., Bergström, S. & Barbour, A. G. (1990). Cloning and sequence analysis of linear plasmid telomeres of the bacterium Borrelia burgdorferi. Mol Microbiol 4, 811-820.
    • (1990) Mol Microbiol , vol.4 , pp. 811-820
    • Hinnebusch, J.1    Bergström, S.2    Barbour, A.G.3
  • 22
    • 0026751258 scopus 로고
    • Heterogeneity of outer membrane proteins in Borrelia burgdorferi: Comparison of osp operons of three isolates of different geographic origins
    • Jonsson, M., Noppa, L., Barbour, A. G. & Bergström, S. (1992). Heterogeneity of outer membrane proteins in Borrelia burgdorferi: comparison of osp operons of three isolates of different geographic origins. Infect Immun 60, 1845-1853.
    • (1992) Infect Immun , vol.60 , pp. 1845-1853
    • Jonsson, M.1    Noppa, L.2    Barbour, A.G.3    Bergström, S.4
  • 23
    • 0025362475 scopus 로고
    • Requirement of integration host factor (IHF) for growth of Escherichia coli deficient in HU protein
    • Kano, Y. & Imamoto, F. (1990). Requirement of integration host factor (IHF) for growth of Escherichia coli deficient in HU protein. Gene 89, 133-137.
    • (1990) Gene , vol.89 , pp. 133-137
    • Kano, Y.1    Imamoto, F.2
  • 24
    • 0022347597 scopus 로고
    • Molecular cloning and nucleotide sequence of the HU-1 gene of Escherichia coli
    • Kano, Y., Yoshino, S., Wada, M., Yokoyama, K., Nobuhara, M. & Imamoto, F. (1985). Molecular cloning and nucleotide sequence of the HU-1 gene of Escherichia coli. Mol Gen Genet 201, 360-362.
    • (1985) Mol Gen Genet , vol.201 , pp. 360-362
    • Kano, Y.1    Yoshino, S.2    Wada, M.3    Yokoyama, K.4    Nobuhara, M.5    Imamoto, F.6
  • 25
    • 0023413823 scopus 로고
    • Cloning and sequencing of the HU-2 gene of Escherichia coli
    • Kano, Y., Osato, K., Wada, M. & Imamoto, F. (1987). Cloning and sequencing of the HU-2 gene of Escherichia coli. Mol Gen Genet 209, 408-410.
    • (1987) Mol Gen Genet , vol.209 , pp. 408-410
    • Kano, Y.1    Osato, K.2    Wada, M.3    Imamoto, F.4
  • 26
    • 0022036630 scopus 로고
    • Characterization and primary structures of DNA-binding HU-type proteins from Rhizobiaceae
    • Khanaka, H., Laine, B., Sautiere, P. & Guillaume, J. (1985). Characterization and primary structures of DNA-binding HU-type proteins from Rhizobiaceae. Eur J Biochem 147, 343-349.
    • (1985) Eur J Biochem , vol.147 , pp. 343-349
    • Khanaka, H.1    Laine, B.2    Sautiere, P.3    Guillaume, J.4
  • 27
    • 0022432182 scopus 로고
    • An Escherichia coli mutant unable to support site-specific recombination of bacteriophage lambda
    • Kikuchi, A., Flamm, E. & Weisberg, R. A. (1985). An Escherichia coli mutant unable to support site-specific recombination of bacteriophage lambda. J Mol Biol 183, 129-140.
    • (1985) J Mol Biol , vol.183 , pp. 129-140
    • Kikuchi, A.1    Flamm, E.2    Weisberg, R.A.3
  • 28
    • 0026739901 scopus 로고
    • The relapsing fever agent Borrelia hermsii has multiple copies of its chromsome and linear plasmids
    • Kitten, T. & Barbour, A. G. (1992). The relapsing fever agent Borrelia hermsii has multiple copies of its chromsome and linear plasmids. Genetics 132, 311-324.
    • (1992) Genetics , vol.132 , pp. 311-324
    • Kitten, T.1    Barbour, A.G.2
  • 29
    • 0028040517 scopus 로고
    • Cloning and expression of the hup gene encoding a histone-like protein of Campylobacter jejuni
    • Konkel, M. E., Marconi, R. T., Mead, D. J. & Cieplak, W., Jr (1994). Cloning and expression of the hup gene encoding a histone-like protein of Campylobacter jejuni. Gene 146, 83-86.
    • (1994) Gene , vol.146 , pp. 83-86
    • Konkel, M.E.1    Marconi, R.T.2    Mead, D.J.3    Cieplak Jr., W.4
  • 30
    • 0024529497 scopus 로고
    • The interaction of E. coli integration host factor and lambda cos DNA: Multiple complex formation and protein-induced bending
    • Kosturko, L. D., Daub, E. & Murialdo, H. (1989). The interaction of E. coli integration host factor and lambda cos DNA: multiple complex formation and protein-induced bending. Nucleic Acids Res 17, 317-334.
    • (1989) Nucleic Acids Res , vol.17 , pp. 317-334
    • Kosturko, L.D.1    Daub, E.2    Murialdo, H.3
  • 31
    • 0021103559 scopus 로고
    • Primary structure of the DNA-binding protein HRm from Rhizobium meliloti
    • Laine, B., Belaiche, D., Khanaka, H. & Sautiere, P. (1983). Primary structure of the DNA-binding protein HRm from Rhizobium meliloti. Eur J Biochem 131, 325-331.
    • (1983) Eur J Biochem , vol.131 , pp. 325-331
    • Laine, B.1    Belaiche, D.2    Khanaka, H.3    Sautiere, P.4
  • 32
    • 0026541608 scopus 로고
    • The isolation and characterization of mutants of the integration host factor (IHF) of Escherichia coli with altered, expanded DNA-binding specificities
    • Lee, E. C., Hales, L. M., Gumport, R. I. & Gardner, J. F. (1992). The isolation and characterization of mutants of the integration host factor (IHF) of Escherichia coli with altered, expanded DNA-binding specificities. EMBO J 11, 305-313.
    • (1992) EMBO J , vol.11 , pp. 305-313
    • Lee, E.C.1    Hales, L.M.2    Gumport, R.I.3    Gardner, J.F.4
  • 33
    • 0027310615 scopus 로고
    • Variability of osp genes and gene products among species of Lyme disease spirochetes
    • Marconi, R. T., Konkel, M. E. & Garon, C. F. (1993). Variability of osp genes and gene products among species of Lyme disease spirochetes. Infect Immun 61, 2611-2617.
    • (1993) Infect Immun , vol.61 , pp. 2611-2617
    • Marconi, R.T.1    Konkel, M.E.2    Garon, C.F.3
  • 34
    • 0022637897 scopus 로고
    • Autogenous regulation of the gene for transcription termination factor rho in Escherichia coli: Localization and function of its attenuators
    • Matsumoto, Y., Shigesada, K., Hirano, M. & Imai, M. (1986). Autogenous regulation of the gene for transcription termination factor rho in Escherichia coli: localization and function of its attenuators. J Bacteriol 166, 945-958.
    • (1986) J Bacteriol , vol.166 , pp. 945-958
    • Matsumoto, Y.1    Shigesada, K.2    Hirano, M.3    Imai, M.4
  • 35
    • 0021867663 scopus 로고
    • Sequence of the Escherichia coli pheST operon and identification of the him A gene
    • Mechulam, Y., Fayat, G. & Blanquet, S. (1985). Sequence of the Escherichia coli pheST operon and identification of the him A gene. J Bacteriol 163, 787-791.
    • (1985) J Bacteriol , vol.163 , pp. 787-791
    • Mechulam, Y.1    Fayat, G.2    Blanquet, S.3
  • 36
    • 0026031442 scopus 로고
    • HU and integration host factor function as auxiliary proteins in cleavage of phage lambda cohesive ends by terminase
    • Mendelson, I., Gottesman, M. & Oppenheim, A. B. (1991). HU and integration host factor function as auxiliary proteins in cleavage of phage lambda cohesive ends by terminase. J Bacteriol 173, 1670-1676.
    • (1991) J Bacteriol , vol.173 , pp. 1670-1676
    • Mendelson, I.1    Gottesman, M.2    Oppenheim, A.B.3
  • 37
    • 0027327311 scopus 로고
    • Genetic and biochemical analysis of the integration host factor of Escherichia coli
    • Mengeritsky, G., Goldenberg, D., Mendelson, I., Giladi, H. & Oppenheim, A. B. (1993). Genetic and biochemical analysis of the integration host factor of Escherichia coli. J Mol Biol 231, 646-657.
    • (1993) J Mol Biol , vol.231 , pp. 646-657
    • Mengeritsky, G.1    Goldenberg, D.2    Mendelson, I.3    Giladi, H.4    Oppenheim, A.B.5
  • 38
    • 0026702673 scopus 로고
    • The DNA-binding protein HBsu is essential for normal growth and development in Bacillus subtilis
    • Micka, B. & Marahiel, M. A. (1992). The DNA-binding protein HBsu is essential for normal growth and development in Bacillus subtilis. Biochimie 74, 641-650.
    • (1992) Biochimie , vol.74 , pp. 641-650
    • Micka, B.1    Marahiel, M.A.2
  • 39
    • 0025897381 scopus 로고
    • Molecular cloning, nucleotide sequence, and characterization of the Bacillus subtilis gene encoding the DNA-binding protein HBsu
    • Micka, B., Grouch, N., Heinemann, U. & Marahiel, M. A. (1991). Molecular cloning, nucleotide sequence, and characterization of the Bacillus subtilis gene encoding the DNA-binding protein HBsu. J Bacteriol 173, 3191-3198.
    • (1991) J Bacteriol , vol.173 , pp. 3191-3198
    • Micka, B.1    Grouch, N.2    Heinemann, U.3    Marahiel, M.A.4
  • 40
    • 0021646254 scopus 로고
    • Primary structure of the himA gene of Escherichia coli: Homology with DNA-binding protein HU and association with the phenylalanyl-tRNA synthetase operon
    • Miller, H. I. (1984). Primary structure of the himA gene of Escherichia coli: homology with DNA-binding protein HU and association with the phenylalanyl-tRNA synthetase operon. Cold Spring Harbor Symp Quant Biol 49, 691-698.
    • (1984) Cold Spring Harbor Symp Quant Biol , vol.49 , pp. 691-698
    • Miller, H.I.1
  • 42
    • 0027297919 scopus 로고
    • An African swine fever virus gene with similarity to bacterial DNA binding proteins, bacterial integration host factors, and the Bacillus phage SPO1 transcription factor, TF1
    • Neilan, J. G., Lu, Z., Kutish, G. F., Sussman, M. D., Roberts, P. C., Yozawa, T. & Rock, D. L. (1993). An African swine fever virus gene with similarity to bacterial DNA binding proteins, bacterial integration host factors, and the Bacillus phage SPO1 transcription factor, TF1. Nucleic Acids Res 21, 1496.
    • (1993) Nucleic Acids Res , vol.21 , pp. 1496
    • Neilan, J.G.1    Lu, Z.2    Kutish, G.F.3    Sussman, M.D.4    Roberts, P.C.5    Yozawa, T.6    Rock, D.L.7
  • 43
    • 0028284569 scopus 로고
    • Harnessing the writhe: A role for DNA chaperones in nucleoprotein-complex formation
    • Ner, S. S., Travers, A. A. & Churchill, M. E. A. (1994). Harnessing the writhe: a role for DNA chaperones in nucleoprotein-complex formation. Treads Biochem Sci 19, 185-187.
    • (1994) Treads Biochem Sci , vol.19 , pp. 185-187
    • Ner, S.S.1    Travers, A.A.2    Churchill, M.E.A.3
  • 44
    • 0030063060 scopus 로고    scopus 로고
    • Serratia marcescens contains a heterodimeric HU protein like Escherichia coli and Salmonella typhimurium
    • Oberto, J. & Rouviere-Yaniv, J. (1996). Serratia marcescens contains a heterodimeric HU protein like Escherichia coli and Salmonella typhimurium. J Bacteriol 178, 293-297.
    • (1996) J Bacteriol , vol.178 , pp. 293-297
    • Oberto, J.1    Rouviere-Yaniv, J.2
  • 45
    • 0026648406 scopus 로고
    • The DNA-binding protein HU from mesophilic and thermophilic bacilli: Gene cloning, overproduction and purification
    • Padas, P. M. (1992). The DNA-binding protein HU from mesophilic and thermophilic bacilli: gene cloning, overproduction and purification. Gene 117, 39-44.
    • (1992) Gene , vol.117 , pp. 39-44
    • Padas, P.M.1
  • 47
    • 0014771240 scopus 로고
    • Evidence for extrachromosomal location of prophage N15
    • Ravin, V. K. & Shulga, M. G. (1970). Evidence for extrachromosomal location of prophage N15. Virology 40, 800-807.
    • (1970) Virology , vol.40 , pp. 800-807
    • Ravin, V.K.1    Shulga, M.G.2
  • 49
    • 0017681196 scopus 로고
    • DNA sequencing with chain-terminating inhibitors
    • Sanger, F., Nicklen, S. & Coulson, A. R. (1977). DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA 74, 5463-5467.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 5463-5467
    • Sanger, F.1    Nicklen, S.2    Coulson, A.R.3
  • 50
    • 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
  • 51
    • 0026654661 scopus 로고
    • rRNA gene organization in the Lyme disease spirochete, Borrelia burgdorferi
    • Schwartz, J. J., Gazumyan, A. & Schwartz, I. (1992). rRNA gene organization in the Lyme disease spirochete, Borrelia burgdorferi. J Bacteriol 174, 3757-3765.
    • (1992) J Bacteriol , vol.174 , pp. 3757-3765
    • Schwartz, J.J.1    Gazumyan, A.2    Schwartz, I.3
  • 52
    • 0026667410 scopus 로고
    • GCWIND: A microcomputer program for identifying open reading frames according to codon positional G+C
    • Shields, D. C., Higgins, D. G. & Sharp, P. M. (1992). GCWIND: a microcomputer program for identifying open reading frames according to codon positional G+C (communication). CABIOS 8, 521-523.
    • (1992) CABIOS , vol.8 , pp. 521-523
    • Shields, D.C.1    Higgins, D.G.2    Sharp, P.M.3
  • 54
    • 0022974221 scopus 로고
    • Opacity genes in Neisseria gonorrhoeae: Control of phase and antigenic variation
    • Stern, A., Brown, M., Nickel, P. & Meyer, T. F. (1986). Opacity genes in Neisseria gonorrhoeae: control of phase and antigenic variation. Cell 47, 61-71.
    • (1986) Cell , vol.47 , pp. 61-71
    • Stern, A.1    Brown, M.2    Nickel, P.3    Meyer, T.F.4
  • 55
    • 0002112063 scopus 로고
    • Characteristics of plasmid properties of bacteriophage N15
    • in Russian
    • Svarchevsky, A. N. & Rybchin, V. N. (1984). Characteristics of plasmid properties of bacteriophage N15. Mol Genet Mikrobiol Virusol 5, 34-39 (in Russian).
    • (1984) Mol Genet Mikrobiol Virusol , vol.5 , pp. 34-39
    • Svarchevsky, A.N.1    Rybchin, V.N.2
  • 56
    • 0021286693 scopus 로고
    • 3-Å resolution structure of a protein with histone-like properties in prokaryotes
    • Tanaka, I., Appelt, K., Dijk, J., White, S. W. & Wilson, K. S. (1984). 3-Å resolution structure of a protein with histone-like properties in prokaryotes. Nature 310, 376-381.
    • (1984) Nature , vol.310 , pp. 376-381
    • Tanaka, I.1    Appelt, K.2    Dijk, J.3    White, S.W.4    Wilson, K.S.5
  • 57
    • 0023771741 scopus 로고
    • Empirical estimation of protein-induced DNA bending angles: Applications to lambda site-specific recombination complexes
    • Thompson, J. F. & Landy, A. (1988). Empirical estimation of protein-induced DNA bending angles: applications to lambda site-specific recombination complexes. Nucleic Acids Res 16, 9687-9705.
    • (1988) Nucleic Acids Res , vol.16 , pp. 9687-9705
    • Thompson, J.F.1    Landy, A.2
  • 58
    • 0027164312 scopus 로고
    • A Borrelia burgdorferi homolog of the Escherichia coli rho gene
    • Tilly, K. & Campbell, J. (1993). A Borrelia burgdorferi homolog of the Escherichia coli rho gene. Nucleic Acids Res 21, 1040.
    • (1993) Nucleic Acids Res , vol.21 , pp. 1040
    • Tilly, K.1    Campbell, J.2
  • 59
    • 0027415873 scopus 로고
    • Isolation of dnaJ, dnaK, and grpE homologues from Borrelia burgdorferi and complementation of Escherichia coli mutants
    • Tilly, K., Hauser, R., Campbell, J. & Ostheimer, J. (1993). Isolation of dnaJ, dnaK, and grpE homologues from Borrelia burgdorferi and complementation of Escherichia coli mutants. Mol Microbiol 7, 359-369.
    • (1993) Mol Microbiol , vol.7 , pp. 359-369
    • Tilly, K.1    Hauser, R.2    Campbell, J.3    Ostheimer, J.4
  • 60
    • 0025746322 scopus 로고
    • A mutation in a Rhodobacter capsulatus gene encoding an integration host factor-like protein impairs in vivo hydrogenase expression
    • Toussaint, B., Bosc, C., Richaud, P., Colbeau, A. & Vignais, P. M. (1991). A mutation in a Rhodobacter capsulatus gene encoding an integration host factor-like protein impairs in vivo hydrogenase expression. Proc Natl Acad Sci USA 88, 10749-10753.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10749-10753
    • Toussaint, B.1    Bosc, C.2    Richaud, P.3    Colbeau, A.4    Vignais, P.M.5
  • 61
    • 0027358806 scopus 로고
    • Purification of the integration host factor homolog of Rhodobacter capsulatus: Cloning and sequencing of the hip gene, which encodes the beta subunit
    • Toussaint, B., Delic-Attree, I., De Sury D'Aspremont, R., David, L., Vincon, M. & Vignais, P. M. (1993). Purification of the integration host factor homolog of Rhodobacter capsulatus: cloning and sequencing of the hip gene, which encodes the beta subunit. J Bacteriol 175, 6499-6504.
    • (1993) J Bacteriol , vol.175 , pp. 6499-6504
    • Toussaint, B.1    Delic-Attree, I.2    De Sury D'Aspremont, R.3    David, L.4    Vincon, M.5    Vignais, P.M.6
  • 62
    • 0028226799 scopus 로고
    • DNA chaperones: A solution to a persistence problem?
    • Travers, A. A., Ner, S. S. & Churchill, M. E. A. (1994). DNA chaperones: a solution to a persistence problem? Cell 77, 167-169.
    • (1994) Cell , vol.77 , pp. 167-169
    • Travers, A.A.1    Ner, S.S.2    Churchill, M.E.A.3
  • 63
    • 0025831084 scopus 로고
    • The plastid genome of Crytomonas phi encodes an hsp70-like protein, a histone-like protein, and an acyl carrier protein
    • Wang, S. & Liu, X.-Q. (1991). The plastid genome of Crytomonas phi encodes an hsp70-like protein, a histone-like protein, and an acyl carrier protein. Proc Natl Acad Sci USA 88, 10783-10787.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10783-10787
    • Wang, S.1    Liu, X.-Q.2
  • 64
    • 0024340266 scopus 로고
    • The interaction of E. coli IHF protein with its specific binding sites
    • Yang, C.-C. & Nash, H. A. (1989). The interaction of E. coli IHF protein with its specific binding sites. Cell 57, 869-880.
    • (1989) Cell , vol.57 , pp. 869-880
    • Yang, C.-C.1    Nash, H.A.2
  • 65
    • 0025015387 scopus 로고
    • The primary structure of DNA binding protein II from the extreme thermophilic bacterium Thermus thermophilus
    • Zierer, R. & Choli, D. (1990). The primary structure of DNA binding protein II from the extreme thermophilic bacterium Thermus thermophilus. FEBS Lett 273, 59-62.
    • (1990) FEBS Lett , vol.273 , pp. 59-62
    • Zierer, R.1    Choli, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.