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Volumn 45, Issue 2, 2010, Pages 292-296

High-recovery one-step purification of the DNA-binding protein Fur by mild guanidinium chloride treatment

Author keywords

DNA binding proteins; Ferric uptake regulator; Guanidinium chloride; High yield recovery

Indexed keywords

CHAOTROPIC AGENTS; CRUDE EXTRACT; CYANOBACTERIUM ANABAENA; DEEP KNOWLEDGE; DNA-BINDING DOMAIN; DNA-BINDING PROTEIN; FERRIC UPTAKE REGULATOR; GENERAL APPLICATIONS; GUANIDINIUM CHLORIDES; HYDROPHOBIC INTERACTIONS; IMINODIACETATE; NMR SPECTROSCOPY; ONE-STEP PURIFICATION; PROTEIN-DNA INTERACTIONS; REGULATORY PROTEIN; STRUCTURAL DATA; TERTIARY STRUCTURES;

EID: 71249129868     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2009.09.019     Document Type: Article
Times cited : (11)

References (26)
  • 1
    • 0036912846 scopus 로고    scopus 로고
    • Induction of angiogenesis in a mouse model using engineered transcription factors
    • Rebar E.J., Huang Y., Hickey R., Nath A.K., Meoli D., Nath S., et al. Induction of angiogenesis in a mouse model using engineered transcription factors. Nat Med 8 (2002) 1427-1432
    • (2002) Nat Med , vol.8 , pp. 1427-1432
    • Rebar, E.J.1    Huang, Y.2    Hickey, R.3    Nath, A.K.4    Meoli, D.5    Nath, S.6
  • 2
    • 58049195169 scopus 로고    scopus 로고
    • Targeting artificial transcription factors of utrophin A promoter. Effects on dystrophic pathology and muscle function
    • Lu Y., Tian C., Danialou G., Gilbert R., Petrof B.J., Karpati G., et al. Targeting artificial transcription factors of utrophin A promoter. Effects on dystrophic pathology and muscle function. J Biol Chem 283 (2008) 34720-34727
    • (2008) J Biol Chem , vol.283 , pp. 34720-34727
    • Lu, Y.1    Tian, C.2    Danialou, G.3    Gilbert, R.4    Petrof, B.J.5    Karpati, G.6
  • 3
    • 0036792099 scopus 로고    scopus 로고
    • Heritable endogenous gene regulation in plants with designed polydactyl zinc finger transcription factors
    • Guan X., Stege J., Kim M., Dahmani Z., Fan N., Heifetz P., et al. Heritable endogenous gene regulation in plants with designed polydactyl zinc finger transcription factors. Proc Natl Acad Sci USA 99 (2002) 13296-13301
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 13296-13301
    • Guan, X.1    Stege, J.2    Kim, M.3    Dahmani, Z.4    Fan, N.5    Heifetz, P.6
  • 4
    • 52649115929 scopus 로고    scopus 로고
    • Phenotypic engineering by reprogramming gene transcription using novel artificial transcription factors in Escherichia coli
    • Lee J.Y., Sung B.H., Yu B.J., Lee J.H., Lee S.H., Kim M.S., et al. Phenotypic engineering by reprogramming gene transcription using novel artificial transcription factors in Escherichia coli. Nucl Acids Res 36 (2008) 1-10
    • (2008) Nucl Acids Res , vol.36 , pp. 1-10
    • Lee, J.Y.1    Sung, B.H.2    Yu, B.J.3    Lee, J.H.4    Lee, S.H.5    Kim, M.S.6
  • 5
    • 33846706457 scopus 로고    scopus 로고
    • Artificial regulation of ospC expression in Borrelia burgdorferi
    • Gilbert M.A., Morton E.A., Bundle S.F., and Samuels D.S. Artificial regulation of ospC expression in Borrelia burgdorferi. Mol Microbiol 63 (2007) 1259-1273
    • (2007) Mol Microbiol , vol.63 , pp. 1259-1273
    • Gilbert, M.A.1    Morton, E.A.2    Bundle, S.F.3    Samuels, D.S.4
  • 6
    • 34248669001 scopus 로고    scopus 로고
    • Functional specialization within the Fur family of metallo-regulators
    • Lee J.W., and Helmann J.D. Functional specialization within the Fur family of metallo-regulators. Biometals 20 (2007) 485-499
    • (2007) Biometals , vol.20 , pp. 485-499
    • Lee, J.W.1    Helmann, J.D.2
  • 7
    • 0033764027 scopus 로고    scopus 로고
    • The DNA-binding characteristics of the Streptomyces reticuli regulator FurS depend on the redox state of its cysteine residues
    • Ortiz de Orué Lucana D., and Schrempf H. The DNA-binding characteristics of the Streptomyces reticuli regulator FurS depend on the redox state of its cysteine residues. Mol Gen Genet 264 (2000) 341-353
    • (2000) Mol Gen Genet , vol.264 , pp. 341-353
    • Ortiz de Orué Lucana, D.1    Schrempf, H.2
  • 9
    • 33344464022 scopus 로고    scopus 로고
    • Designer zinc finger proteins: tools for creating artificial DNA-binding functional proteins
    • Dhanasekaran M., Negi S., and Sugiura Y. Designer zinc finger proteins: tools for creating artificial DNA-binding functional proteins. Acc Chem Res 39 (2006) 45-52
    • (2006) Acc Chem Res , vol.39 , pp. 45-52
    • Dhanasekaran, M.1    Negi, S.2    Sugiura, Y.3
  • 10
    • 65749115965 scopus 로고    scopus 로고
    • Zinc-finger-based artificial transcription factors and their applications
    • Sera T. Zinc-finger-based artificial transcription factors and their applications. Adv Drug Del Rev 61 (2009) 513-526
    • (2009) Adv Drug Del Rev , vol.61 , pp. 513-526
    • Sera, T.1
  • 11
    • 0344839044 scopus 로고    scopus 로고
    • Evaluation of a modular strategy for the construction of novel polydactyl zinc finger DNA-binding proteins
    • Segal D.J., Beerli R.R., Blancafort P., Dreier B., Effertz K., Huber A., et al. Evaluation of a modular strategy for the construction of novel polydactyl zinc finger DNA-binding proteins. Biochemistry 42 (2003) 2137-2148
    • (2003) Biochemistry , vol.42 , pp. 2137-2148
    • Segal, D.J.1    Beerli, R.R.2    Blancafort, P.3    Dreier, B.4    Effertz, K.5    Huber, A.6
  • 12
    • 9444230573 scopus 로고    scopus 로고
    • Designing transcription factor architectures for drug discovery
    • Blancafort P., Segal D.J., and Barbas III C.F. Designing transcription factor architectures for drug discovery. Mol Pharmacol 66 (2004) 1361-1371
    • (2004) Mol Pharmacol , vol.66 , pp. 1361-1371
    • Blancafort, P.1    Segal, D.J.2    Barbas III, C.F.3
  • 13
    • 35349025902 scopus 로고    scopus 로고
    • Cross-talk between iron and nitrogen regulatory networks in Anabaena (Nostoc) sp. PCC 7120: identification of overlapping genes in FurA and NtcA regulons
    • López-Gomollón S., Hernández J.A., Pellicer S., Espinosa V., Peleato M.L., and Fillat M.F. Cross-talk between iron and nitrogen regulatory networks in Anabaena (Nostoc) sp. PCC 7120: identification of overlapping genes in FurA and NtcA regulons. J Mol Biol 374 (2007) 267-281
    • (2007) J Mol Biol , vol.374 , pp. 267-281
    • López-Gomollón, S.1    Hernández, J.A.2    Pellicer, S.3    Espinosa, V.4    Peleato, M.L.5    Fillat, M.F.6
  • 14
    • 33646061953 scopus 로고    scopus 로고
    • Fur from Microcystis aeruginosa binds in vitro promoter regions of the microcystin biosynthesis gene cluster
    • Martín-Luna B., Sevilla E., Hernández J.A., Bes M.T., Fillat M.F., and Peleato M.L. Fur from Microcystis aeruginosa binds in vitro promoter regions of the microcystin biosynthesis gene cluster. Phytochemistry 67 (2006) 876-881
    • (2006) Phytochemistry , vol.67 , pp. 876-881
    • Martín-Luna, B.1    Sevilla, E.2    Hernández, J.A.3    Bes, M.T.4    Fillat, M.F.5    Peleato, M.L.6
  • 15
    • 0037103830 scopus 로고    scopus 로고
    • Biochemical analysis of the recombinant Fur (ferric uptake regulator) protein from Anabaena PCC 7119: factors affecting its oligomerization state
    • Hernández J.A., Bes M.T., Fillat M.F., Neira J.L., and Peleato M.L. Biochemical analysis of the recombinant Fur (ferric uptake regulator) protein from Anabaena PCC 7119: factors affecting its oligomerization state. Biochem J 366 (2002) 315-322
    • (2002) Biochem J , vol.366 , pp. 315-322
    • Hernández, J.A.1    Bes, M.T.2    Fillat, M.F.3    Neira, J.L.4    Peleato, M.L.5
  • 16
    • 0032855077 scopus 로고    scopus 로고
    • Inhibition of aggregation side reactions during in vitro protein folding
    • Clark E.D.B., Schwartz E., and Rudolph R. Inhibition of aggregation side reactions during in vitro protein folding. Methods Enzymol 309 (1999) 217-236
    • (1999) Methods Enzymol , vol.309 , pp. 217-236
    • Clark, E.D.B.1    Schwartz, E.2    Rudolph, R.3
  • 17
    • 0036774673 scopus 로고    scopus 로고
    • Biophysical effect of amino acids on the prevention of protein aggregation
    • Shiraki M., Kudou S., Fujiwara T., and Imanaka M. Biophysical effect of amino acids on the prevention of protein aggregation. J Biochem 132 (2002) 591-595
    • (2002) J Biochem , vol.132 , pp. 591-595
    • Shiraki, M.1    Kudou, S.2    Fujiwara, T.3    Imanaka, M.4
  • 18
    • 0017809275 scopus 로고
    • The renaturation of reduced chymotrypsinogen A in guanidine HCl. Refolding versus aggregation
    • Orsini G., and Goldberg M.E. The renaturation of reduced chymotrypsinogen A in guanidine HCl. Refolding versus aggregation. J Biol Chem 253 (1978) 3453-3458
    • (1978) J Biol Chem , vol.253 , pp. 3453-3458
    • Orsini, G.1    Goldberg, M.E.2
  • 19
    • 0027407353 scopus 로고
    • Guanidine hydrochloride stabilization of a partially unfolded intermediate during the reversible denaturation of protein disulfide isomerase
    • Morjana N.A., McKeone B.J., and Gilbert H.F. Guanidine hydrochloride stabilization of a partially unfolded intermediate during the reversible denaturation of protein disulfide isomerase. Proc Natl Acad Sci USA 90 (1993) 2107-2111
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 2107-2111
    • Morjana, N.A.1    McKeone, B.J.2    Gilbert, H.F.3
  • 20
    • 0035862444 scopus 로고    scopus 로고
    • Cloning, overexpression and interaction of recombinant Fur from the cyanobacterium Anabaena PCC 7119 with isiB and its own promoter
    • Bes M.T., Hernández J.A., Peleato M.L., and Fillat M.F. Cloning, overexpression and interaction of recombinant Fur from the cyanobacterium Anabaena PCC 7119 with isiB and its own promoter. FEMS Microbiol Lett 194 (2001) 187-192
    • (2001) FEMS Microbiol Lett , vol.194 , pp. 187-192
    • Bes, M.T.1    Hernández, J.A.2    Peleato, M.L.3    Fillat, M.F.4
  • 21
    • 28444466626 scopus 로고    scopus 로고
    • The conformational stability and thermodynamics of Fur A (Ferric Uptake Regulator) from Anabaena sp. PCC 7119
    • Hernández J.A., Meier J., Barrera F.N., Ruiz de los Paños O., Hurtado-Gómez E., Bes M.T., et al. The conformational stability and thermodynamics of Fur A (Ferric Uptake Regulator) from Anabaena sp. PCC 7119. Biophys J 89 (2005) 4188-4200
    • (2005) Biophys J , vol.89 , pp. 4188-4200
    • Hernández, J.A.1    Meier, J.2    Barrera, F.N.3    Ruiz de los Paños, O.4    Hurtado-Gómez, E.5    Bes, M.T.6
  • 22
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto M., Saudek V., and Sklenar V. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J Biomol NMR 2 (1993) 661-665
    • (1993) J Biomol NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 23
    • 3142696264 scopus 로고    scopus 로고
    • Three fur homologues from Anabaena sp. PCC 7120: exploring reciprocal protein-promoter recognition
    • Hernández J.A., López-Gomollón S., Bes M.T., Fillat M.F., and Peleato M.L. Three fur homologues from Anabaena sp. PCC 7120: exploring reciprocal protein-promoter recognition. FEMS Microbiol Lett 236 (2004) 275-282
    • (2004) FEMS Microbiol Lett , vol.236 , pp. 275-282
    • Hernández, J.A.1    López-Gomollón, S.2    Bes, M.T.3    Fillat, M.F.4    Peleato, M.L.5
  • 24
    • 7544226457 scopus 로고    scopus 로고
    • Heme binds to and inhibits the DNA-binding activity of the global regulator FurA from Anabaena sp. PCC 7120
    • Hernández J.A., Peleato M.L., Fillat M.F., and Bes M.T. Heme binds to and inhibits the DNA-binding activity of the global regulator FurA from Anabaena sp. PCC 7120. FEBS Lett 577 (2004) 35-41
    • (2004) FEBS Lett , vol.577 , pp. 35-41
    • Hernández, J.A.1    Peleato, M.L.2    Fillat, M.F.3    Bes, M.T.4
  • 25
    • 0028959773 scopus 로고
    • Circular dichroism
    • Woody R.W. Circular dichroism. Methods Enzymol 246 (1995) 34-71
    • (1995) Methods Enzymol , vol.246 , pp. 34-71
    • Woody, R.W.1


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