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Volumn 60, Issue 2, 2003, Pages 413-421

Microtubule associated protein tau binds to double-stranded but not single-stranded DNA

Author keywords

DNA; DNA binding protein; Double stranded DNA; Electrophoretic mobility shift assay; Human neuronal tau; Nuclear tau

Indexed keywords

CELLULOSE; DITHIOTHREITOL; DOUBLE STRANDED DNA; HISTONE; POLYNUCLEOTIDE; RECOMBINANT PROTEIN; SINGLE STRANDED DNA; SODIUM CHLORIDE; TAU PROTEIN;

EID: 0037299017     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180300034     Document Type: Article
Times cited : (67)

References (38)
  • 2
    • 0027058857 scopus 로고
    • Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau
    • Drechsel D. N., Hyman A. A., Cobb M. H. and Kirschner M. W. (1992) Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau. Mol. Biol. Cell 3: 1141-1154
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1141-1154
    • Drechsel, D.N.1    Hyman, A.A.2    Cobb, M.H.3    Kirschner, M.W.4
  • 3
    • 0022365608 scopus 로고
    • The distribution of tau in the mammalian central nervous system
    • Binder L. I., Frankfurter A. and Rebhun L. I. (1985) The distribution of tau in the mammalian central nervous system. J. Cell Biol. 101: 1371-1378
    • (1985) J. Cell Biol. , vol.101 , pp. 1371-1378
    • Binder, L.I.1    Frankfurter, A.2    Rebhun, L.I.3
  • 4
    • 0023505501 scopus 로고
    • Phosphorylation determines two distinct species of Tau in the central nervous system
    • Papasozomenos S. C. and Binder L. I. (1987) Phosphorylation determines two distinct species of Tau in the central nervous system. Cell Motil. Cytoskel. 8: 210-226
    • (1987) Cell Motil. Cytoskel. , vol.8 , pp. 210-226
    • Papasozomenos, S.C.1    Binder, L.I.2
  • 5
    • 0028095224 scopus 로고
    • Levels of normal and abnormally phosphorylated tau in different cellular and regional compartments of Alzheimer disease and control brains
    • Khatoon S., Grundke-Iqbal I. and Iqbal K (1994) Levels of normal and abnormally phosphorylated tau in different cellular and regional compartments of Alzheimer disease and control brains. FEBS Lett. 351: 80-84
    • (1994) FEBS Lett. , vol.351 , pp. 80-84
    • Khatoon, S.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 6
    • 0021338217 scopus 로고
    • Phosphorylation affects the ability of tau protein to promote microtubule assembly
    • Lindwall G. and Cole R. D. (1984) Phosphorylation affects the ability of tau protein to promote microtubule assembly. J. Biol. Chem. 259: 5301-5305
    • (1984) J. Biol. Chem. , vol.259 , pp. 5301-5305
    • Lindwall, G.1    Cole, R.D.2
  • 10
    • 0027361281 scopus 로고
    • Microtubule-associated protein tau: Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease
    • Köpke E., Tung Y. C., Shaikh S., Alonso A. del C., Iqbal K. et al. (1993) Microtubule-associated protein tau: abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease. J. Biol. Chem. 268: 24374-24384
    • (1993) J. Biol. Chem. , vol.268 , pp. 24374-24384
    • Köpke, E.1    Tung, Y.C.2    Shaikh, S.3    Del Alonso, A.C.4    Iqbal, K.5
  • 12
    • 0033554182 scopus 로고    scopus 로고
    • Regulation of expression, phosphorylation and biological activity of tau during differentiation in SY5Y cells
    • Haque N., Tanaka T., Iqbal K. and Grundke-Iqbal I. (1999) Regulation of expression, phosphorylation and biological activity of tau during differentiation in SY5Y cells. Brain Res. 838: 69-77
    • (1999) Brain Res. , vol.838 , pp. 69-77
    • Haque, N.1    Tanaka, T.2    Iqbal, K.3    Grundke-Iqbal, I.4
  • 13
    • 0033544963 scopus 로고    scopus 로고
    • The microtubule binding of Tau and high molecular weight Tau in apoptotic PC12 cells is impaired because of altered phosphorylation
    • Davis P. K. and Johnson G. V. W. (1999) The microtubule binding of Tau and high molecular weight Tau in apoptotic PC12 cells is impaired because of altered phosphorylation. J. Biol. Chem. 274: 35686-35692
    • (1999) J. Biol. Chem. , vol.274 , pp. 35686-35692
    • Davis, P.K.1    Johnson, G.V.W.2
  • 14
    • 0027469909 scopus 로고
    • A novel tau transcript in cultured human neuroblastoma cells expressing nuclear tau
    • Wang Y., Loomis P. A., Zinkowski R. P. and Binder L. I. (1993) A novel tau transcript in cultured human neuroblastoma cells expressing nuclear tau. J. Cell Biol. 121: 257-267
    • (1993) J. Cell Biol. , vol.121 , pp. 257-267
    • Wang, Y.1    Loomis, P.A.2    Zinkowski, R.P.3    Binder, L.I.4
  • 16
    • 0029161154 scopus 로고
    • Localization and in situ phosphorylation state of nuclear tau
    • Greenwood J. A. and Johnson G. V. W. (1995) Localization and in situ phosphorylation state of nuclear tau. Exp. Cell Res. 220: 332-337
    • (1995) Exp. Cell Res. , vol.220 , pp. 332-337
    • Greenwood, J.A.1    Johnson, G.V.W.2
  • 17
    • 0034483176 scopus 로고    scopus 로고
    • Human neuronal tau promoting the melting temperature of DNA
    • Hua Q. and He R. Q. (2000) Human neuronal tau promoting the melting temperature of DNA. Chin. Sci. Bull. 45: 999-1001
    • (2000) Chin. Sci. Bull. , vol.45 , pp. 999-1001
    • Hua, Q.1    He, R.Q.2
  • 18
    • 0036067745 scopus 로고    scopus 로고
    • Effect of phosphorylation and aggregation on tau binding to DNA
    • Hua Q. and He R. Q. (2002) Effect of phosphorylation and aggregation on tau binding to DNA. Protein Pept. Lett. 9: 249-357
    • (2002) Protein Pept. Lett. , vol.9 , pp. 249-357
    • Hua, Q.1    He, R.Q.2
  • 19
    • 0031043386 scopus 로고    scopus 로고
    • Xrx1, a novel Xenopus homeobox gene expressed during eye and pineal gland development
    • Casarosa S., Andreazzoli M., Simeone A. and Barsacchi G. (1997) Xrx1, a novel Xenopus homeobox gene expressed during eye and pineal gland development. Mech. Dev. 61: 187-198
    • (1997) Mech. Dev. , vol.61 , pp. 187-198
    • Casarosa, S.1    Andreazzoli, M.2    Simeone, A.3    Barsacchi, G.4
  • 21
    • 0028967378 scopus 로고
    • Rapid Alzheimer-like phosphorylation of tau by the synergistic actions of non-proline-dependent protein kinases and GSK-3
    • Singh T. J., Haque N., Grundke-Iqbal I. and Iqbal K. (1995) Rapid Alzheimer-like phosphorylation of tau by the synergistic actions of non-proline-dependent protein kinases and GSK-3. FEBS Lett. 358: 267-272
    • (1995) FEBS Lett. , vol.358 , pp. 267-272
    • Singh, T.J.1    Haque, N.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 22
    • 0030614508 scopus 로고    scopus 로고
    • The regulatory Ser262 of microtubule-associated protein tau is phosphorylated by phosphorylase kinase
    • Paudel H. K. (1997) The regulatory Ser262 of microtubule-associated protein tau is phosphorylated by phosphorylase kinase. J. Biol. Chem. 272: 1777-1785
    • (1997) J. Biol. Chem. , vol.272 , pp. 1777-1785
    • Paudel, H.K.1
  • 23
    • 0030692829 scopus 로고    scopus 로고
    • Phosphorylation by neuronal cdc2-like protein kinase promotes dimerization of Tau protein in vitro
    • Paudel H. K. (1997) Phosphorylation by neuronal cdc2-like protein kinase promotes dimerization of Tau protein in vitro. J. Biol. Chem. 272: 28328-28334
    • (1997) J. Biol. Chem. , vol.272 , pp. 28328-28334
    • Paudel, H.K.1
  • 24
    • 0344627489 scopus 로고    scopus 로고
    • McGraw-Hill New York
    • Rob W. (1999) Molecular biology, pp. 34-36, McGraw-Hill New York
    • (1999) Molecular Biology , pp. 34-36
    • Rob, W.1
  • 25
    • 0027739734 scopus 로고
    • Spacing and orientation of bipartite DNA-binding motifs as potential functional determinants for POU domain factors
    • Li P., He X., Gerrero M. R., Mok M., Aggarwal A. and Rosenfeld M G. (1993) Spacing and orientation of bipartite DNA-binding motifs as potential functional determinants for POU domain factors. Gene Dev. 7: 2483-2496
    • (1993) Gene Dev. , vol.7 , pp. 2483-2496
    • Li, P.1    He, X.2    Gerrero, M.R.3    Mok, M.4    Aggarwal, A.5    Rosenfeld, M.G.6
  • 26
    • 77956988666 scopus 로고
    • DNA-cellulose chromatography
    • Alberts B. and Herrick G. (1971) DNA-cellulose chromatography. Methods Enzymol. 21: 198-217
    • (1971) Methods Enzymol. , vol.21 , pp. 198-217
    • Alberts, B.1    Herrick, G.2
  • 27
    • 0026694783 scopus 로고
    • Brain levels of microtubule-associated protein tau are elevated in Alzheimer's disease: A radioimmuno-slot-blot assay for nanograms of the protein
    • Khatoon S., Grundke-Iqbal I. and Iqbal K. (1992) Brain levels of microtubule-associated protein tau are elevated in Alzheimer's disease: a radioimmuno-slot-blot assay for nanograms of the protein. J. Neurochem. 59: 750-753
    • (1992) J. Neurochem. , vol.59 , pp. 750-753
    • Khatoon, S.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 28
    • 0026490544 scopus 로고
    • Use of gel retardation to analyze protein-nucleic acid interactions
    • Lane D., Prentki P. and Chandler M. (1992) Use of gel retardation to analyze protein-nucleic acid interactions. Microbiol. Rev. 56: 509-528
    • (1992) Microbiol. Rev. , vol.56 , pp. 509-528
    • Lane, D.1    Prentki, P.2    Chandler, M.3
  • 29
    • 0028226799 scopus 로고
    • DNA chaperones: A solution to a persistence problem?
    • Travers A. A., Ner S. S. and 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
  • 30
    • 0013770431 scopus 로고
    • Studies on histones
    • John E. W. (1964) Studies on histones. Biochem. J. 92: 55-59
    • (1964) Biochem. J. , vol.92 , pp. 55-59
    • John, E.W.1
  • 32
    • 0001232758 scopus 로고
    • The nucleolar cycle
    • Jordan E. G. and Cullis C. A. (eds), Cambridge University Press, Cambridge, UK
    • De la Torre C. and Gimenez-Martin G. (1982) The nucleolar cycle. In: The Nucleolus, pp. 153-177, Jordan E. G. and Cullis C. A. (eds), Cambridge University Press, Cambridge, UK
    • (1982) The Nucleolus , pp. 153-177
    • De La Torre, C.1    Gimenez-Martin, G.2
  • 33
    • 0028284569 scopus 로고
    • Harnessing the writhe: A role for DNA chaperones in nucleoprotein-complex formation
    • Ner S. S., Travers A. A. and Churchill M. E. A. (1994) Harnessing the writhe: a role for DNA chaperones in nucleoprotein-complex formation. Trends Biochem. Sci. 19: 185-187
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 185-187
    • Ner, S.S.1    Travers, A.A.2    Churchill, M.E.A.3
  • 34
    • 0027156630 scopus 로고
    • The specific interactions of MG 1 and 2 with negatively supercoiled DNA are modulated by their acidic C-terminal domains and involve cysteine residues in their HMG 1/2 boxes
    • Sheflin L. G., Fucile N. W. and Spaulding S. W. (1993) The specific interactions of MG 1 and 2 with negatively supercoiled DNA are modulated by their acidic C-terminal domains and involve cysteine residues in their HMG 1/2 boxes. Biochemistry 32: 3238-3248
    • (1993) Biochemistry , vol.32 , pp. 3238-3248
    • Sheflin, L.G.1    Fucile, N.W.2    Spaulding, S.W.3
  • 35
    • 0023041804 scopus 로고
    • Interaction of the Escherichia coli HU protein with DNA: Evidence for formation of nucleosome-like structures with altered DNA helical pitch
    • Broyles S. S. and Pettijohn D. E. (1986) Interaction of the Escherichia coli HU protein with DNA: evidence for formation of nucleosome-like structures with altered DNA helical pitch. J. Mol. Biol. 187: 47-60
    • (1986) J. Mol. Biol. , vol.187 , pp. 47-60
    • Broyles, S.S.1    Pettijohn, D.E.2
  • 37
    • 0017758306 scopus 로고
    • Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly
    • Cleveland D. W., Hwo S. Y. and Kirschner M. W. (1977) Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly. J. Mol. Biol. 116: 227-247
    • (1977) J. Mol. Biol. , vol.116 , pp. 227-247
    • Cleveland, D.W.1    Hwo, S.Y.2    Kirschner, M.W.3
  • 38
    • 0012505469 scopus 로고    scopus 로고
    • Tau could protect DNA double helix structure
    • Hua Q. and He R. Q. (2003) Tau could protect DNA double helix structure. Biochim. Biophys. Acta 1645(2): 205-211
    • (2003) Biochim. Biophys. Acta , vol.1645 , Issue.2 , pp. 205-211
    • Hua, Q.1    He, R.Q.2


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