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Volumn 22, Issue 19, 2003, Pages 5137-5146

Zinc fingers can act as Zn2+ sensors to regulate transcriptional activation domain function

Author keywords

Gene expression; Homeostasis; Regulation; Transcriptional activation; Zinc fingers

Indexed keywords

CYSTEINE; HISTIDINE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR ZAP1; UNCLASSIFIED DRUG; ZINC; ZINC FINGER 1 PROTEIN; ZINC FINGER 2 PROTEIN; ZINC FINGER PROTEIN;

EID: 0141864674     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdg484     Document Type: Article
Times cited : (100)

References (45)
  • 1
    • 0035696187 scopus 로고    scopus 로고
    • Cellular zinc sensors: MTF-1 regulation of gene expression
    • Andrews, G.K. (2001) Cellular zinc sensors: MTF-1 regulation of gene expression. Biometals, 14, 223-237.
    • (2001) Biometals , vol.14 , pp. 223-237
    • Andrews, G.K.1
  • 2
    • 0028860021 scopus 로고
    • Excitation-transcription coupling mediated by zinc influx through voltage-dependent calcium channels
    • Atar, D., Backx, P.H., Appel, M.M., Gao, W.D. and Marban, E. (1995) Excitation-transcription coupling mediated by zinc influx through voltage-dependent calcium channels. J. Biol. Chem., 270, 2473-2477.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2473-2477
    • Atar, D.1    Backx, P.H.2    Appel, M.M.3    Gao, W.D.4    Marban, E.5
  • 4
    • 0034717152 scopus 로고    scopus 로고
    • Mapping the DNA binding domain of the Zap1 zinc-responsive transcriptional activator
    • Bird, A.J., Evans-Galea, M., Blankman, E., Zhao, H., Luo, H., Winge, D.R. and Eide, D.J. (2000a) Mapping the DNA binding domain of the Zap1 zinc-responsive transcriptional activator. J. Biol. Chem., 275, 16160-16166.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16160-16166
    • Bird, A.J.1    Evans-Galea, M.2    Blankman, E.3    Zhao, H.4    Luo, H.5    Winge, D.R.6    Eide, D.J.7
  • 5
    • 0034679822 scopus 로고    scopus 로고
    • A dual role for zinc fingers in both DNA binding and zinc sensing by the Zap1 transcriptional activator
    • Bird, A.J., Zhui, H., Luo, H., Jensen, L.T., Srinivasan, C., Evans-Galea, M., Winge, D.R. and Eide, D.J. (2000b) A dual role for zinc fingers in both DNA binding and zinc sensing by the Zap1 transcriptional activator. EMBO J., 19, 3704-3713.
    • (2000) EMBO J. , vol.19 , pp. 3704-3713
    • Bird, A.J.1    Zhui, H.2    Luo, H.3    Jensen, L.T.4    Srinivasan, C.5    Evans-Galea, M.6    Winge, D.R.7    Eide, D.J.8
  • 7
    • 0033796599 scopus 로고    scopus 로고
    • Kinetics of metal binding by a zinc finger peptide
    • Buchsbaum, J.C. and Berg, J.M. (2000) Kinetics of metal binding by a zinc finger peptide. Inorg. Chim., 297, 217-219.
    • (2000) Inorg. Chim. , vol.297 , pp. 217-219
    • Buchsbaum, J.C.1    Berg, J.M.2
  • 8
    • 0032508398 scopus 로고    scopus 로고
    • Structural and functional heterogeneity among the zinc fingers of human MRE-binding transcription factor-1
    • Chen, X., Agarwal, A. and Giedroc, D.P. (1998) Structural and functional heterogeneity among the zinc fingers of human MRE-binding transcription factor-1. Biochemistry, 37, 11152-11161.
    • (1998) Biochemistry , vol.37 , pp. 11152-11161
    • Chen, X.1    Agarwal, A.2    Giedroc, D.P.3
  • 9
    • 0033613267 scopus 로고    scopus 로고
    • MRE-binding transcription factor-1: Weak zinc-binding finger domains 5 and 6 modulate the structure, affinity and specificity of the metal response element complex
    • Chen, X., Chua, M. and Giedroc, D.P. (1999) MRE-binding transcription factor-1: Weak zinc-binding finger domains 5 and 6 modulate the structure, affinity and specificity of the metal response element complex. Biochemistry, 38, 12915-12925.
    • (1999) Biochemistry , vol.38 , pp. 12915-12925
    • Chen, X.1    Chua, M.2    Giedroc, D.P.3
  • 10
    • 0031770844 scopus 로고    scopus 로고
    • Calcium-sensitive fluorescent dyes can report increases in intracellular free zinc concentration in cultured forebrain neurons
    • Cheng, C. and Reynolds, I.J. (1998) Calcium-sensitive fluorescent dyes can report increases in intracellular free zinc concentration in cultured forebrain neurons. J. Neurochem., 71, 2401-2410.
    • (1998) J. Neurochem. , vol.71 , pp. 2401-2410
    • Cheng, C.1    Reynolds, I.J.2
  • 11
    • 0026576605 scopus 로고
    • Parallel pathways of gene regulation: Homologous regulators SWI5 and ACE2 differentially control transcription of HO and chitinase
    • Dohrmann, P.R., Butler, G., Tamai, K., Dorland, S., Greene, J.R., Thiele, D.J. and Stillman, D.J. (1992) Parallel pathways of gene regulation: homologous regulators SWI5 and ACE2 differentially control transcription of HO and chitinase. Genes Dev., 6, 93-104.
    • (1992) Genes Dev. , vol.6 , pp. 93-104
    • Dohrmann, P.R.1    Butler, G.2    Tamai, K.3    Dorland, S.4    Greene, J.R.5    Thiele, D.J.6    Stillman, D.J.7
  • 12
    • 0037417769 scopus 로고    scopus 로고
    • Two of the five zinc fingers in the Zap1 transcription factor DNA binding domain dominate site-specific DNA binding
    • Evans-Galea, M.V., Blankman, E., Myszka, D.G., Bird, A.J., Eide, D.J. and Winge, D.R. (2003) Two of the five zinc fingers in the Zap1 transcription factor DNA binding domain dominate site-specific DNA binding. Biochemistry, 42, 1053-1061.
    • (2003) Biochemistry , vol.42 , pp. 1053-1061
    • Evans-Galea, M.V.1    Blankman, E.2    Myszka, D.G.3    Bird, A.J.4    Eide, D.J.5    Winge, D.R.6
  • 13
    • 0040143460 scopus 로고    scopus 로고
    • Subsets of the zinc finger motifs in dsRBP-ZFa can bind double-stranded RNA
    • Finerty, P.J., Jr and Bass, B.L. (1999) Subsets of the zinc finger motifs in dsRBP-ZFa can bind double-stranded RNA. Biochemistry, 38, 4001-4007.
    • (1999) Biochemistry , vol.38 , pp. 4001-4007
    • Finerty P.J., Jr.1    Bass, B.L.2
  • 14
    • 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. USA, 84, 4841-4845.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 4841-4845
    • Frankel, A.D.1    Berg, J.M.2    Pabo, C.O.3
  • 16
    • 0032582814 scopus 로고    scopus 로고
    • Zinc-induced inactivation of the yeast ZRT1 zinc transporter occurs through endocytosis and vacuolar degradation
    • Gitan, R.S., Luo, H., Rodgers, J., Broderius, M. and Eide, D. (1998) Zinc-induced inactivation of the yeast ZRT1 zinc transporter occurs through endocytosis and vacuolar degradation. J. Biol. Chem., 273, 28617-28624.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28617-28624
    • Gitan, R.S.1    Luo, H.2    Rodgers, J.3    Broderius, M.4    Eide, D.5
  • 17
    • 0032915204 scopus 로고    scopus 로고
    • Heterologous URA3MX cassettes for gene replacement in Saccharomyces cerevisiae
    • Goldstein, A.L., Pan, X. and McCusker, J.H. (1999) Heterologous URA3MX cassettes for gene replacement in Saccharomyces cerevisiae. Yeast, 15, 507-511.
    • (1999) Yeast , vol.15 , pp. 507-511
    • Goldstein, A.L.1    Pan, X.2    McCusker, J.H.3
  • 18
    • 0014060675 scopus 로고
    • Determination of sulfhydryl groups with 2, 2′- or 4, 4′-dithiodipyridine
    • Grassetti, D.R. and Murray, J.F., Jr (1967) Determination of sulfhydryl groups with 2, 2′- or 4, 4′-dithiodipyridine. Arch. Biochem. Biophys., 119, 41-49.
    • (1967) Arch. Biochem. Biophys. , vol.119 , pp. 41-49
    • Grassetti, D.R.1    Murray J.F., Jr.2
  • 19
    • 0020645052 scopus 로고
    • Yeast promoters and lacZ fusions designed to study expression of cloned genes in yeast
    • Guarente, L. (1983) Yeast promoters and lacZ fusions designed to study expression of cloned genes in yeast. Methods Enzymol., 101, 181-191.
    • (1983) Methods Enzymol. , vol.101 , pp. 181-191
    • Guarente, L.1
  • 20
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S.N., Hunt, H.D., Horton, R.M., Pullen, J.K. and Pease, L.R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene, 77, 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 21
    • 0029902679 scopus 로고    scopus 로고
    • Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase
    • Kuzmic, P. (1996) Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase. Anal. Biochem., 237, 260-273.
    • (1996) Anal. Biochem. , vol.237 , pp. 260-273
    • Kuzmic, P.1
  • 22
    • 2042437650 scopus 로고    scopus 로고
    • Initial sequencing and analysis of the human genome
    • Landers, E. et al. (2001) Initial sequencing and analysis of the human genome. Nature, 409, 860-921.
    • (2001) Nature , vol.409 , pp. 860-921
    • Landers, E.1
  • 23
    • 0034703040 scopus 로고    scopus 로고
    • Local structural elements in the mostly unstructured transcriptional activation domain of human p53
    • Lee, H. et al. (2000) Local structural elements in the mostly unstructured transcriptional activation domain of human p53. J. Biol. Chem., 275, 29426-29432.
    • (2000) J. Biol. Chem. , vol.275 , pp. 29426-29432
    • Lee, H.1
  • 25
    • 0023615620 scopus 로고
    • Plasmid construction by homologous recombination in yeast
    • Ma, H., Kunes, S., Schatz, P.J. and Botstein, D. (1987) Plasmid construction by homologous recombination in yeast. Gene, 58, 201-216.
    • (1987) Gene , vol.58 , pp. 201-216
    • Ma, H.1    Kunes, S.2    Schatz, P.J.3    Botstein, D.4
  • 26
    • 0023652389 scopus 로고
    • Deletion analysis of GAL4 defines two transcriptional activating segments
    • Ma, J. and Ptashne, M. (1987) Deletion analysis of GAL4 defines two transcriptional activating segments. Cell, 48, 847-853.
    • (1987) Cell , vol.48 , pp. 847-853
    • Ma, J.1    Ptashne, M.2
  • 27
    • 0034660257 scopus 로고    scopus 로고
    • Zinc transporters that regulate vacuolar zinc storage in Saccharomyces cerevisiae
    • MacDiarmid, C.W., Gaither, L.A. and Eide, D. (2000) Zinc transporters that regulate vacuolar zinc storage in Saccharomyces cerevisiae. EMBO J., 19, 2845-2855.
    • (2000) EMBO J. , vol.19 , pp. 2845-2855
    • MacDiarmid, C.W.1    Gaither, L.A.2    Eide, D.3
  • 28
  • 30
    • 0040215628 scopus 로고
    • Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes
    • Miller, J., McLachlan, A.D. and Klug, A. (1985) Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes. EMBO J., 4, 1609-1614.
    • (1985) EMBO J. , vol.4 , pp. 1609-1614
    • Miller, J.1    McLachlan, A.D.2    Klug, A.3
  • 31
    • 0034811137 scopus 로고    scopus 로고
    • Zrc1 is involved in zinc transport system between vacuole and cytosol in Saccharomyces cerevisiae
    • Miyabe, S., Izawa, S. and Inoue, Y. (2001) Zrc1 is involved in zinc transport system between vacuole and cytosol in Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun., 282, 79-83.
    • (2001) Biochem. Biophys. Res. Commun. , vol.282 , pp. 79-83
    • Miyabe, S.1    Izawa, S.2    Inoue, Y.3
  • 32
    • 0023034916 scopus 로고
    • Yeast shuttle and integrative vectors with multiple cloning sites suitable for construction of lacZ fusions
    • Myers, A.M., Tzagoloff, A., Kinney, D.M. and Lusty, C.J. (1986) Yeast shuttle and integrative vectors with multiple cloning sites suitable for construction of lacZ fusions. Gene, 45, 299-310.
    • (1986) Gene , vol.45 , pp. 299-310
    • Myers, A.M.1    Tzagoloff, A.2    Kinney, D.M.3    Lusty, C.J.4
  • 33
    • 0027183546 scopus 로고
    • Transition metals in control of gene expression
    • O'Halloran, T.V. (1993) Transition metals in control of gene expression. Science, 261, 715-725.
    • (1993) Science , vol.261 , pp. 715-725
    • O'Halloran, T.V.1
  • 34
    • 0035968001 scopus 로고    scopus 로고
    • Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis
    • Outten, C.E. and O'Halloran, T.V. (2001) Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis. Science, 292, 2488-2492.
    • (2001) Science , vol.292 , pp. 2488-2492
    • Outten, C.E.1    O'Halloran, T.V.2
  • 35
    • 0031798662 scopus 로고    scopus 로고
    • The ZnuABC high affinity zinc uptake system and its regulator Zur in Escherichia coli
    • Patzer, S.I. and Hantke, K. (1998) The ZnuABC high affinity zinc uptake system and its regulator Zur in Escherichia coli. Mol. Microbiol., 28, 1199-1210.
    • (1998) Mol. Microbiol. , vol.28 , pp. 1199-1210
    • Patzer, S.I.1    Hantke, K.2
  • 36
    • 0027423758 scopus 로고
    • Crystal structure of a five-finger GLI-DNA complex: New perspectives on zinc fingers
    • Pavletich, N.P. and Pabo, C.O. (1993) Crystal structure of a five-finger GLI-DNA complex: new perspectives on zinc fingers. Science, 261, 1701-1707.
    • (1993) Science , vol.261 , pp. 1701-1707
    • Pavletich, N.P.1    Pabo, C.O.2
  • 37
    • 0027547987 scopus 로고
    • Zinc fingers
    • Rhodes, D. and Klug, A. (1993) Zinc fingers. Sci. Am., 268, 56-65.
    • (1993) Sci. Am. , vol.268 , pp. 56-65
    • Rhodes, D.1    Klug, A.2
  • 39
    • 0030756675 scopus 로고    scopus 로고
    • Induced alpha helix in the VP16 activation domain upon binding to a human TAF
    • Uesugi, M., Nyanguile, O., Lu, H., Levine, A.J. and Verdine, G.L. (1997) Induced alpha helix in the VP16 activation domain upon binding to a human TAF. Science, 277, 1310-1313.
    • (1997) Science , vol.277 , pp. 1310-1313
    • Uesugi, M.1    Nyanguile, O.2    Lu, H.3    Levine, A.J.4    Verdine, G.L.5
  • 40
    • 0034718523 scopus 로고    scopus 로고
    • The zinc metalloregulatory protein Synechococcus PCC7942 SmtB binds a single zinc ion per monomer with high affinity in a tetrahedral coordination geometry
    • VanZile, M.L., Cosper, N.J., Scott, R.A. and Giedroc, D.P. (2000) The zinc metalloregulatory protein Synechococcus PCC7942 SmtB binds a single zinc ion per monomer with high affinity in a tetrahedral coordination geometry. Biochemistry, 39, 11818-11829.
    • (2000) Biochemistry , vol.39 , pp. 11818-11829
    • VanZile, M.L.1    Cosper, N.J.2    Scott, R.A.3    Giedroc, D.P.4
  • 41
    • 0037072773 scopus 로고    scopus 로고
    • Combinatorial control of yeast FET4 gene expression in response to iron, zinc and oxygen
    • Waters, B.M. and Eide, D.J. (2002) Combinatorial control of yeast FET4 gene expression in response to iron, zinc and oxygen. J. Biol. Chem., 277, 33749-33757.
    • (2002) J. Biol. Chem. , vol.277 , pp. 33749-33757
    • Waters, B.M.1    Eide, D.J.2
  • 42
    • 0029911793 scopus 로고    scopus 로고
    • The yeast ZRT1 gene encodes the zinc transporter of a high affinity uptake system induced by zinc limitation
    • Zhao, H. and Eide, D. (1996a) The yeast ZRT1 gene encodes the zinc transporter of a high affinity uptake system induced by zinc limitation. Proc. Natl Acad. Sci. USA, 93, 2454-2458.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2454-2458
    • Zhao, H.1    Eide, D.2
  • 43
    • 0029841951 scopus 로고    scopus 로고
    • The ZRT2 gene encodes the low affinity zinc transporter in Saccharomyces cerevisiae
    • Zhao, H. and Eide, D. (1996b) The ZRT2 gene encodes the low affinity zinc transporter in Saccharomyces cerevisiae. J. Biol. Chem., 271, 23203-23210.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23203-23210
    • Zhao, H.1    Eide, D.2
  • 44
    • 0030794279 scopus 로고    scopus 로고
    • Zap1p, a metalloregulatory protein involved in zinc-responsive transcriptional regulation in Saccharomyces cerevisiae
    • Zhao, H. and Eide, D.J. (1997) Zap1p, a metalloregulatory protein involved in zinc-responsive transcriptional regulation in Saccharomyces cerevisiae. Mol. Cell. Biol., 17, 5044-5052.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5044-5052
    • Zhao, H.1    Eide, D.J.2
  • 45
    • 0032582651 scopus 로고    scopus 로고
    • Regulation of zinc homeostasis in yeast by binding of the ZAP1 transcriptional activator to zinc-responsive promoter elements
    • Zhao, H., Butler, E., Rodgers, J., Spizzo, T. and Duesterhoeft, S. (1998) Regulation of zinc homeostasis in yeast by binding of the ZAP1 transcriptional activator to zinc-responsive promoter elements. J. Biol. Chem., 273, 28713-28720.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28713-28720
    • Zhao, H.1    Butler, E.2    Rodgers, J.3    Spizzo, T.4    Duesterhoeft, S.5


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