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Volumn 53, Issue 1, 2007, Pages 195-200

Expression, purification and biochemical characterization of a single-stranded DNA binding protein from Herbaspirillum seropedicae

Author keywords

DNA binding; Herbaspirillum; Overexpression; SSB

Indexed keywords

BACTERIAL PROTEIN; DNA BINDING PROTEIN; PROTEIN SUBUNIT; RECOMBINANT PROTEIN; TRYPSIN;

EID: 33847109693     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2006.11.018     Document Type: Article
Times cited : (1)

References (27)
  • 1
    • 15044347420 scopus 로고    scopus 로고
    • Single-stranded DNA-binding protein of Deinococcus radiodurans: a biophysical characterization
    • Witte G., Urbanke C., and Curth U. Single-stranded DNA-binding protein of Deinococcus radiodurans: a biophysical characterization. Nucleic Acids Res. 33 (2005) 1662-1670
    • (2005) Nucleic Acids Res. , vol.33 , pp. 1662-1670
    • Witte, G.1    Urbanke, C.2    Curth, U.3
  • 2
    • 0002474824 scopus 로고
    • The single-stranded DNA binding protein of Escherichia coli. Physicochemical properties and biological functions
    • Saenger W., and Heinemann U. (Eds), Macmillan, London
    • Greipel J., Urbanke C., and Maass G. The single-stranded DNA binding protein of Escherichia coli. Physicochemical properties and biological functions. In: Saenger W., and Heinemann U. (Eds). Protein-Nucleic Acid Interaction (1989), Macmillan, London 61-86
    • (1989) Protein-Nucleic Acid Interaction , pp. 61-86
    • Greipel, J.1    Urbanke, C.2    Maass, G.3
  • 3
    • 0027479161 scopus 로고
    • OB (oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences
    • Murzin A.G. OB (oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences. EMBO J. 12 (1993) 861-867
    • (1993) EMBO J. , vol.12 , pp. 861-867
    • Murzin, A.G.1
  • 4
    • 0031090688 scopus 로고    scopus 로고
    • Common fold, common function, common origin?
    • Suck D. Common fold, common function, common origin?. Nature Struct. Biol. 4 (1997) 161-165
    • (1997) Nature Struct. Biol. , vol.4 , pp. 161-165
    • Suck, D.1
  • 5
    • 0031009811 scopus 로고    scopus 로고
    • Crystal structure of the homo-tetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength X-ray diffraction on the selenomethionyl protein at 2.9-A resolution
    • Raghunathan S., Ricard C.S., Lohman T.M., and Waksman G. Crystal structure of the homo-tetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength X-ray diffraction on the selenomethionyl protein at 2.9-A resolution. Proc. Natl. Acad. Sci. USA 94 (1997) 6652-6657
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6652-6657
    • Raghunathan, S.1    Ricard, C.S.2    Lohman, T.M.3    Waksman, G.4
  • 6
    • 0031567573 scopus 로고    scopus 로고
    • A common core for binding single-stranded DNA: structural comparison of the single-stranded DNA-binding proteins (SSB) from Escherichia coli and human mitochondria
    • Webster .G., Genschel J., Curth U., Urbanke C., Kang C.H., and Hilgenfeld R. A common core for binding single-stranded DNA: structural comparison of the single-stranded DNA-binding proteins (SSB) from Escherichia coli and human mitochondria. FEBS Lett. 411 (1997) 313-316
    • (1997) FEBS Lett. , vol.411 , pp. 313-316
    • Webster, .G.1    Genschel, J.2    Curth, U.3    Urbanke, C.4    Kang, C.H.5    Hilgenfeld, R.6
  • 7
    • 0031023811 scopus 로고    scopus 로고
    • Crystal structure of human mitochondrial single-stranded DNA binding protein at 2.4 Å resolution
    • Yang C., Curth U., Urbanke C., and Kang C. Crystal structure of human mitochondrial single-stranded DNA binding protein at 2.4 Å resolution. Nature Struct. Biol. 4 (1997) 153-157
    • (1997) Nature Struct. Biol. , vol.4 , pp. 153-157
    • Yang, C.1    Curth, U.2    Urbanke, C.3    Kang, C.4
  • 8
    • 0020580529 scopus 로고
    • Limited proteolysis studies on the Escherichia coli single-stranded DNA binding protein. Evidence for a functionally homologous domain in both the Escherichia coli and T4 DNA binding proteins
    • Williams K.R., Spicer E.K., LoPresti M.B., Guggenheimer R.A., and Chase J.W. Limited proteolysis studies on the Escherichia coli single-stranded DNA binding protein. Evidence for a functionally homologous domain in both the Escherichia coli and T4 DNA binding proteins. J. Biol. Chem. 258 (1983) 3346-3355
    • (1983) J. Biol. Chem. , vol.258 , pp. 3346-3355
    • Williams, K.R.1    Spicer, E.K.2    LoPresti, M.B.3    Guggenheimer, R.A.4    Chase, J.W.5
  • 9
    • 0026064009 scopus 로고
    • Amino acid 55 plays a central role in tetramerization and function of Escherichia coli single-stranded DNA binding protein
    • Curth U., Bayer I., Greipel J., Mayer F., Urbanke C., and Maas G. Amino acid 55 plays a central role in tetramerization and function of Escherichia coli single-stranded DNA binding protein. Eur. J. Biochem. 196 (1991) 87-93
    • (1991) Eur. J. Biochem. , vol.196 , pp. 87-93
    • Curth, U.1    Bayer, I.2    Greipel, J.3    Mayer, F.4    Urbanke, C.5    Maas, G.6
  • 10
    • 0028246888 scopus 로고
    • Escherichia coli single-stranded DNA binding protein: multiple DNA binding modes and cooperativities
    • Lohman T.M., and Ferrari M.E. Escherichia coli single-stranded DNA binding protein: multiple DNA binding modes and cooperativities. Ann. Rev. Biochem. 63 (1994) 527-570
    • (1994) Ann. Rev. Biochem. , vol.63 , pp. 527-570
    • Lohman, T.M.1    Ferrari, M.E.2
  • 11
    • 0030014904 scopus 로고    scopus 로고
    • In vitro and in vivo function of the C-terminus of Escherichia coli single-stranded DNA binding protein
    • Curth U., Genschel J., Urbanke C., and Greipel J. In vitro and in vivo function of the C-terminus of Escherichia coli single-stranded DNA binding protein. Nucleic Acids Res. 24 (1996) 2706-2711
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2706-2711
    • Curth, U.1    Genschel, J.2    Urbanke, C.3    Greipel, J.4
  • 12
    • 0034074478 scopus 로고    scopus 로고
    • Interaction of E. coli single-stranded DNA binding protein (SSB) with exonuclease I
    • Genschel J., Curth U., and Urbanke C. Interaction of E. coli single-stranded DNA binding protein (SSB) with exonuclease I. Biol. Chem. 381 (2000) 183-192
    • (2000) Biol. Chem. , vol.381 , pp. 183-192
    • Genschel, J.1    Curth, U.2    Urbanke, C.3
  • 13
    • 0028034452 scopus 로고
    • Protein interaction in genetic recombination in Escherichia coli. Interactions involving RecO and RecR overcome the inhibition of RecA by single- stranded DNA-binding protein
    • Umezu K., and Kolodner R.D. Protein interaction in genetic recombination in Escherichia coli. Interactions involving RecO and RecR overcome the inhibition of RecA by single- stranded DNA-binding protein. J. Biol. Chem. 269 (1994) 30005-30013
    • (1994) J. Biol. Chem. , vol.269 , pp. 30005-30013
    • Umezu, K.1    Kolodner, R.D.2
  • 14
    • 0037180443 scopus 로고    scopus 로고
    • Escherichia coli RecO protein anneals ssDNA complexed with its cognate ssDNA-binding protein: a common step in genetic recombination
    • Kantake N., Madiraju M.V.V.M., Sugiyama T., and Kowalczykowski S.C. Escherichia coli RecO protein anneals ssDNA complexed with its cognate ssDNA-binding protein: a common step in genetic recombination. Proc. Natl. Acad. Sci. 99 (2002) 15327-15332
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 15327-15332
    • Kantake, N.1    Madiraju, M.V.V.M.2    Sugiyama, T.3    Kowalczykowski, S.C.4
  • 15
    • 0035907374 scopus 로고    scopus 로고
    • Chimeras between single-stranded DNA-binding proteins from Escherichia coli and Mycobacterium tuberculosis reveal that their C-terminal domains interact with uracil DNA glycosylases
    • Handa P., Acharya N., and Varshney U. Chimeras between single-stranded DNA-binding proteins from Escherichia coli and Mycobacterium tuberculosis reveal that their C-terminal domains interact with uracil DNA glycosylases. J. Biol. Chem. 276 (2001) 16992-16997
    • (2001) J. Biol. Chem. , vol.276 , pp. 16992-16997
    • Handa, P.1    Acharya, N.2    Varshney, U.3
  • 16
    • 0032483511 scopus 로고    scopus 로고
    • The χ ψ subunits of DNA polymerase III holoenzyme bind to single-stranded DNA-binding protein (SSB) and facilitate replication of an SSB-coated template
    • Glover B.P., and McHenry C.S. The χ ψ subunits of DNA polymerase III holoenzyme bind to single-stranded DNA-binding protein (SSB) and facilitate replication of an SSB-coated template. J. Biol. Chem. 273 (1998) 23476-23484
    • (1998) J. Biol. Chem. , vol.273 , pp. 23476-23484
    • Glover, B.P.1    McHenry, C.S.2
  • 17
    • 0032522760 scopus 로고    scopus 로고
    • Devoted to the lagging strand-the χ subunit of DNA polymerase III holoenzyme contacts SSB to promote processive elongation and sliding clamp assembly
    • Kelman Z., Yuzhakov A., Andjelkovic J., and O'Donnell M. Devoted to the lagging strand-the χ subunit of DNA polymerase III holoenzyme contacts SSB to promote processive elongation and sliding clamp assembly. EMBO J. 17 (1998) 2436-2449
    • (1998) EMBO J. , vol.17 , pp. 2436-2449
    • Kelman, Z.1    Yuzhakov, A.2    Andjelkovic, J.3    O'Donnell, M.4
  • 18
    • 0043163774 scopus 로고    scopus 로고
    • DNA polymerase III χ subunit ties single-stranded DNA binding protein to the bacterial replication machinery
    • Witte G., Urbanke C., and Curth U. DNA polymerase III χ subunit ties single-stranded DNA binding protein to the bacterial replication machinery. Nucleic Acids Res. 31 (2003) 4434-4440
    • (2003) Nucleic Acids Res. , vol.31 , pp. 4434-4440
    • Witte, G.1    Urbanke, C.2    Curth, U.3
  • 19
    • 0021920551 scopus 로고
    • Two binding modes in Escherichia coli single-stranded binding protein-single-stranded DNA complexes
    • Lohman T.M., and Overman L.B. Two binding modes in Escherichia coli single-stranded binding protein-single-stranded DNA complexes. J. Biol. Chem. 260 (1985) 3594-3601
    • (1985) J. Biol. Chem. , vol.260 , pp. 3594-3601
    • Lohman, T.M.1    Overman, L.B.2
  • 20
    • 0028175289 scopus 로고
    • Co-operrative binding of Escherichia coli SSB tetramers to single-stranded DNA in the (SSB) 35 binding mode
    • Ferrari M.E., Bujalowski W., and Lohman T.M. Co-operrative binding of Escherichia coli SSB tetramers to single-stranded DNA in the (SSB) 35 binding mode. J. Mol. Biol. 236 (1994) 106-123
    • (1994) J. Mol. Biol. , vol.236 , pp. 106-123
    • Ferrari, M.E.1    Bujalowski, W.2    Lohman, T.M.3
  • 21
    • 0023655856 scopus 로고
    • Investigation of the role of individual tryptophan residues in the binding of Escherichia coli single-stranded DNA binding protein to single-stranded polynucleotides
    • Khamis M.I., Casas-Finet J.R., Maki A.H., Murphy J.B., and Chase J.W. Investigation of the role of individual tryptophan residues in the binding of Escherichia coli single-stranded DNA binding protein to single-stranded polynucleotides. J. Biol. Chem. 262 (1987) 10938-10945
    • (1987) J. Biol. Chem. , vol.262 , pp. 10938-10945
    • Khamis, M.I.1    Casas-Finet, J.R.2    Maki, A.H.3    Murphy, J.B.4    Chase, J.W.5
  • 22
    • 12644298689 scopus 로고    scopus 로고
    • Emended description of Herbaspirillum; inclusion of [Pseudomonas] rubrisubalbicans, a mild plant pathogen, as Herbaspirillum rubrisubalbicans comb. nov.; and classification of a group of clinical isolates (EF group 1) as Herbaspirillum species 3
    • Baldani J.I., Pot B., Kirchhof G., Falsen E., Baldani V.L., Olivares F.L., Hoste B., Kersters K., Hartmann A., Gillis M., and Dobereiner J. Emended description of Herbaspirillum; inclusion of [Pseudomonas] rubrisubalbicans, a mild plant pathogen, as Herbaspirillum rubrisubalbicans comb. nov.; and classification of a group of clinical isolates (EF group 1) as Herbaspirillum species 3. Int. J. Syst. Bacteriol. 46 (1996) 802-810
    • (1996) Int. J. Syst. Bacteriol. , vol.46 , pp. 802-810
    • Baldani, J.I.1    Pot, B.2    Kirchhof, G.3    Falsen, E.4    Baldani, V.L.5    Olivares, F.L.6    Hoste, B.7    Kersters, K.8    Hartmann, A.9    Gillis, M.10    Dobereiner, J.11
  • 24
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Shägger H., and von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166 (1987) 368-379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Shägger, H.1    von Jagow, G.2
  • 25
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 27
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.