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Volumn 51, Issue 16, 2012, Pages 3342-3348

Zn(II) binding and DNA binding properties of ligand-substituted CXHH-type zinc finger proteins

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID RESIDUES; ASPARTIC ACIDS; BINDING AFFINITIES; CONFORMATIONAL CHANGE; CYSTEINE RESIDUES; DIVERSE RANGE; DNA BINDING; DNA BINDING ABILITY; DNA BINDING AFFINITY; DNA BINDING SEQUENCE; DNA-BINDING DOMAIN; DNA-BINDING PROPERTIES; GEL MOBILITY SHIFT ASSAY; GLUTAMIC ACID; LIGAND SUBSTITUTION; METAL COORDINATION; SECOND LIGAND; WILD TYPES; ZINC FINGER; ZINC FINGER PEPTIDES; ZINC FINGER PROTEIN;

EID: 84860147811     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300236m     Document Type: Article
Times cited : (20)

References (30)
  • 1
    • 77953633943 scopus 로고    scopus 로고
    • The discovery of zinc fingers and their applications in gene regulation and genome manipulation
    • Klug, A. (2010) The discovery of zinc fingers and their applications in gene regulation and genome manipulation Annu. Rev. Biochem. 79, 213-231
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 213-231
    • Klug, A.1
  • 2
    • 0025773296 scopus 로고
    • Zinc finger-DNA recognition: Crystal structure of a Zif268-DNA complex at 2.1 Å
    • Pavletich, N. P. and Pabo, C. O. (1991) Zinc finger-DNA recognition: Crystal structure of a Zif268-DNA complex at 2.1 Å Science 252, 809-817
    • (1991) Science , vol.252 , pp. 809-817
    • Pavletich, N.P.1    Pabo, C.O.2
  • 3
    • 0023375317 scopus 로고
    • Metal-dependent folding of a single zinc finger from transcription factor IIIA
    • Frankel, A. D., Berg, J. M., and Pabo, C. O. (1987) Metal-dependent folding of a single zinc finger from transcription factor IIIA Proc. Natl. Acad. Sci. U.S.A. 84, 4841-4845
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 4841-4845
    • Frankel, A.D.1    Berg, J.M.2    Pabo, C.O.3
  • 4
    • 77955634459 scopus 로고    scopus 로고
    • Metal-stimulated regulation of transcription by an artificial zinc-finger protein
    • Imanishi, M., Nakaya, T., Morisaki, T., Noshiro, D., Futaki, S., and Sugiura, Y. (2010) Metal-stimulated regulation of transcription by an artificial zinc-finger protein ChemBioChem 11, 1653-1655
    • (2010) ChemBioChem , vol.11 , pp. 1653-1655
    • Imanishi, M.1    Nakaya, T.2    Morisaki, T.3    Noshiro, D.4    Futaki, S.5    Sugiura, Y.6
  • 5
    • 0028328872 scopus 로고
    • Zinc finger phage: Affinity selection of fingers with new DNA-binding specificities
    • Rebar, E. J. and Pabo, C. O. (1994) Zinc finger phage: Affinity selection of fingers with new DNA-binding specificities Science 263, 671-673
    • (1994) Science , vol.263 , pp. 671-673
    • Rebar, E.J.1    Pabo, C.O.2
  • 6
    • 0032437591 scopus 로고    scopus 로고
    • Toward controlling gene expression at will: Specific regulation of the erbB-2/HER-2 promoter by using polydactyl zinc finger proteins constructed from modular building blocks
    • Beerli, R. R., Segal, D. J., Dreier, B., and Barbas, C. F., III (1998) Toward controlling gene expression at will: Specific regulation of the erbB-2/HER-2 promoter by using polydactyl zinc finger proteins constructed from modular building blocks Proc. Natl. Acad. Sci. U.S.A. 95, 14628-14633
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 14628-14633
    • Beerli, R.R.1    Segal, D.J.2    Dreier, B.3    Barbas III, C.F.4
  • 7
    • 0032981699 scopus 로고    scopus 로고
    • Toward controlling gene expression at will: Selection and design of zinc finger domains recognizing each of the 5′-GNN-3′ DNA target sequences
    • Segal, D. J., Dreier, B., Beerli, R. R., and Barbas, C. F., III. (1999) Toward controlling gene expression at will: Selection and design of zinc finger domains recognizing each of the 5′-GNN-3′ DNA target sequences Proc. Natl. Acad. Sci. U.S.A. 96, 2758-2763
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 2758-2763
    • Segal, D.J.1    Dreier, B.2    Beerli, R.R.3    Barbas III, C.F.4
  • 8
    • 70349146995 scopus 로고    scopus 로고
    • Oligomerized pool engineering (OPEN): An 'open-source' protocol for making customized zinc-finger arrays
    • Maeder, M. L., Thibodeau-Beganny, S., Sander, J. D., Voytas, D. F., and Joung, J. K. (2009) Oligomerized pool engineering (OPEN): An 'open-source' protocol for making customized zinc-finger arrays Nat. Protoc. 4, 1471-1501
    • (2009) Nat. Protoc. , vol.4 , pp. 1471-1501
    • Maeder, M.L.1    Thibodeau-Beganny, S.2    Sander, J.D.3    Voytas, D.F.4    Joung, J.K.5
  • 10
    • 9444230573 scopus 로고    scopus 로고
    • Designing transcription factor architectures for drug discovery
    • Blancafort, P., Segal, D. J., and Barbas, C. F., III (2004) Designing transcription factor architectures for drug discovery Mol. Pharmacol. 66, 1361-1371
    • (2004) Mol. Pharmacol. , vol.66 , pp. 1361-1371
    • Blancafort, P.1    Segal, D.J.2    Barbas III, C.F.3
  • 11
    • 34748870747 scopus 로고    scopus 로고
    • Analysis of the structural consensus of the zinc coordination centers of metalloprotein structures
    • Patel, K., Kumar, A., and Durani, S. (2007) Analysis of the structural consensus of the zinc coordination centers of metalloprotein structures Biochim. Biophys. Acta 1774, 1247-1253
    • (2007) Biochim. Biophys. Acta , vol.1774 , pp. 1247-1253
    • Patel, K.1    Kumar, A.2    Durani, S.3
  • 12
    • 70349310441 scopus 로고    scopus 로고
    • The zinc proteome: A tale of stability and functionality
    • Sousa, S. F., Lopes, A. B., Fernandes, P. A., and Ramos, M. J. (2009) The zinc proteome: A tale of stability and functionality Dalton Trans., 38, 7946-7956
    • (2009) Dalton Trans. , vol.38 , pp. 7946-7956
    • Sousa, S.F.1    Lopes, A.B.2    Fernandes, P.A.3    Ramos, M.J.4
  • 13
    • 0032127766 scopus 로고    scopus 로고
    • Alteration of zif268 zinc-finger motifs gives rise to non-native zinc-co-ordination sites but preserves wild-type DNA recognition
    • Green, A. and Sarkar, B. (1998) Alteration of zif268 zinc-finger motifs gives rise to non-native zinc-co-ordination sites but preserves wild-type DNA recognition Biochem. J. 333, 85-90
    • (1998) Biochem. J. , vol.333 , pp. 85-90
    • Green, A.1    Sarkar, B.2
  • 15
    • 0037098864 scopus 로고    scopus 로고
    • Contribution of individual zinc ligands to metal binding and peptide folding of zinc finger peptides
    • Nomura, A. and Sugiura, Y. (2002) Contribution of individual zinc ligands to metal binding and peptide folding of zinc finger peptides Inorg. Chem. 41, 3693-3698
    • (2002) Inorg. Chem. , vol.41 , pp. 3693-3698
    • Nomura, A.1    Sugiura, Y.2
  • 16
    • 0042346328 scopus 로고    scopus 로고
    • CCHX zinc finger derivatives retain the ability to bind Zn(II) and mediate protein-DNA interactions
    • Simpson, R. J., Cram, E. D., Czolij, R., Matthews, J. M., Crossley, M., and Mackay, J. P. (2003) CCHX zinc finger derivatives retain the ability to bind Zn(II) and mediate protein-DNA interactions J. Biol. Chem. 278, 28011-28018
    • (2003) J. Biol. Chem. , vol.278 , pp. 28011-28018
    • Simpson, R.J.1    Cram, E.D.2    Czolij, R.3    Matthews, J.M.4    Crossley, M.5    MacKay, J.P.6
  • 17
    • 78650260200 scopus 로고    scopus 로고
    • Coordination properties of zinc finger peptides revisited: Ligand competition studies reveal higher affinities for zinc and cobalt
    • Sénèque, O. and Latour, J. M. (2010) Coordination properties of zinc finger peptides revisited: Ligand competition studies reveal higher affinities for zinc and cobalt J. Am. Chem. Soc. 132, 17760-17774
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 17760-17774
    • Sénèque, O.1    Latour, J.M.2
  • 18
    • 52249093066 scopus 로고    scopus 로고
    • Rapid transcriptional activity in vivo and slow DNA binding in vitro by an artificial multi-zinc finger protein
    • Morisaki, T., Imanishi, M., Futaki, S., and Sugiura, Y. (2008) Rapid transcriptional activity in vivo and slow DNA binding in vitro by an artificial multi-zinc finger protein Biochemistry 47, 10171-10177
    • (2008) Biochemistry , vol.47 , pp. 10171-10177
    • Morisaki, T.1    Imanishi, M.2    Futaki, S.3    Sugiura, Y.4
  • 19
    • 0040483073 scopus 로고
    • Gene 32 protein, the single-stranded DNA binding protein from bacteriophage T4, is a zinc metalloprotein
    • Giedroc, D. P., Keating, K. M., Williams, K. R., Konigsberg, W. H., and Coleman, J. E. (1986) Gene 32 protein, the single-stranded DNA binding protein from bacteriophage T4, is a zinc metalloprotein Proc. Natl. Acad. Sci. U.S.A. 83, 8452-8456
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 8452-8456
    • Giedroc, D.P.1    Keating, K.M.2    Williams, K.R.3    Konigsberg, W.H.4    Coleman, J.E.5
  • 20
    • 0017818322 scopus 로고
    • Preparation and properties of cobalt(II) rubredoxin
    • May, S. W. and Kuo, J. Y. (1978) Preparation and properties of cobalt(II) rubredoxin Biochemistry 17, 3333-3338
    • (1978) Biochemistry , vol.17 , pp. 3333-3338
    • May, S.W.1    Kuo, J.Y.2
  • 21
    • 0019877715 scopus 로고
    • Spectral studies of cobalt(II)- and nickel(II)-metallothionein
    • Vasák, M., Kägi, J. H., Holmquist, B., and Vallee, B. L. (1981) Spectral studies of cobalt(II)- and nickel(II)-metallothionein Biochemistry 20, 6659-6664
    • (1981) Biochemistry , vol.20 , pp. 6659-6664
    • Vasák, M.1    Kägi, J.H.2    Holmquist, B.3    Vallee, B.L.4
  • 22
    • 0021667647 scopus 로고
    • High spin cobalt(II) as a probe for the investigation of metalloproteins
    • Bertini, I. and Luchinat, C. (1984) High spin cobalt(II) as a probe for the investigation of metalloproteins Adv. Inorg. Biochem. 6, 71-111
    • (1984) Adv. Inorg. Biochem. , vol.6 , pp. 71-111
    • Bertini, I.1    Luchinat, C.2
  • 23
    • 79960274555 scopus 로고    scopus 로고
    • An arginine residue instead of a conserved leucine residue in the recognition helix of the finger 3 of Zif268 stabilizes the domain structure and mediates DNA binding
    • Negi, S., Imanishi, M., Sasaki, M., Tatsutani, K., Futaki, S., and Sugiura, Y. (2011) An arginine residue instead of a conserved leucine residue in the recognition helix of the finger 3 of Zif268 stabilizes the domain structure and mediates DNA binding Biochemistry 50, 6266-6272
    • (2011) Biochemistry , vol.50 , pp. 6266-6272
    • Negi, S.1    Imanishi, M.2    Sasaki, M.3    Tatsutani, K.4    Futaki, S.5    Sugiura, Y.6
  • 24
    • 55849141927 scopus 로고    scopus 로고
    • Effects of bulkiness and hydrophobicity of an aliphatic amino acid in the recognition helix of the GAGA zinc finger on the stability of the hydrophobic core and DNA binding affinity
    • Dhanasekaran, M., Negi, S., Imanishi, M., Suzuki, M., and Sugiura, Y. (2008) Effects of bulkiness and hydrophobicity of an aliphatic amino acid in the recognition helix of the GAGA zinc finger on the stability of the hydrophobic core and DNA binding affinity Biochemistry 47, 11717-11724
    • (2008) Biochemistry , vol.47 , pp. 11717-11724
    • Dhanasekaran, M.1    Negi, S.2    Imanishi, M.3    Suzuki, M.4    Sugiura, Y.5
  • 25
    • 34250882693 scopus 로고    scopus 로고
    • DNA-binding ability of GAGA zinc finger depends on the nature of amino acids present in the β-hairpin
    • Dhanasekaran, M., Negi, S., Imanishi, M., and Sugiura, Y. (2007) DNA-binding ability of GAGA zinc finger depends on the nature of amino acids present in the β-hairpin Biochemistry 46, 7506-7513
    • (2007) Biochemistry , vol.46 , pp. 7506-7513
    • Dhanasekaran, M.1    Negi, S.2    Imanishi, M.3    Sugiura, Y.4
  • 26
    • 0032522662 scopus 로고    scopus 로고
    • High-resolution structures of variant Zif268-DNA complexes: Implications for understanding zinc finger-DNA recognition
    • Elrod-Erickson, M., Benson, T. E., and Pabo, C. O. (1998) High-resolution structures of variant Zif268-DNA complexes: Implications for understanding zinc finger-DNA recognition Structure 6, 451-464
    • (1998) Structure , vol.6 , pp. 451-464
    • Elrod-Erickson, M.1    Benson, T.E.2    Pabo, C.O.3
  • 27
    • 0033516667 scopus 로고    scopus 로고
    • Binding studies with mutants of Zif268. Contribution of individual side chains to binding affinity and specificity in the Zif268 zinc finger-DNA complex
    • Elrod-Erickson, M. and Pabo, C. O. (1999) Binding studies with mutants of Zif268. Contribution of individual side chains to binding affinity and specificity in the Zif268 zinc finger-DNA complex J. Biol. Chem. 274, 19281-19285
    • (1999) J. Biol. Chem. , vol.274 , pp. 19281-19285
    • Elrod-Erickson, M.1    Pabo, C.O.2
  • 28
    • 0035912721 scopus 로고    scopus 로고
    • Exploring the DNA-binding specificities of zinc fingers with DNA microarrays
    • Bulyk, M. L., Huang, X., Choo, Y., and Church, G. M. (2001) Exploring the DNA-binding specificities of zinc fingers with DNA microarrays Proc. Natl. Acad. Sci. U.S.A. 98, 7158-7163
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 7158-7163
    • Bulyk, M.L.1    Huang, X.2    Choo, Y.3    Church, G.M.4
  • 29
    • 0028900074 scopus 로고
    • DNA-binding specificity of NGFI-A and related zinc finger transcription factors
    • Swirnoff, A. H. and Milbrandt, J. (1995) DNA-binding specificity of NGFI-A and related zinc finger transcription factors Mol. Cell. Biol. 15, 2275-2287
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2275-2287
    • Swirnoff, A.H.1    Milbrandt, J.2


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