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Volumn 328, Issue 12, 2005, Pages 1033-1040

Monitoring the interaction between DNA and a transcription factor (MEF2A) using fluorescence correlation spectroscopy

Author keywords

DNA binding; Fluorescence correlation spectroscopy; MADS box; MEF2

Indexed keywords

DNA; MYOCYTE ENHANCER FACTOR 2; MYOCYTE ENHANCER FACTOR 2A; UNCLASSIFIED DRUG;

EID: 29244488764     PISSN: 16310691     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.crvi.2005.07.007     Document Type: Article
Times cited : (9)

References (33)
  • 1
    • 0034755570 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy measures molecular transport in cells
    • E.L. Elson Fluorescence correlation spectroscopy measures molecular transport in cells Traffic 2 2001 789-796
    • (2001) Traffic , vol.2 , pp. 789-796
    • Elson, E.L.1
  • 2
    • 0037154114 scopus 로고    scopus 로고
    • Biological and chemical applications of fluorescence correlation spectroscopy: A review
    • S.T. Hess S. Huang A.A. Heikal W.W. Webb Biological and chemical applications of fluorescence correlation spectroscopy: A review Biochemistry 41 2002 697-705
    • (2002) Biochemistry , vol.41 , pp. 697-705
    • Hess, S.T.1    Huang, S.2    Heikal, A.A.3    Webb, W.W.4
  • 3
    • 0037331059 scopus 로고    scopus 로고
    • Ultrasensitive investigations of biological systems by fluorescence correlation spectroscopy
    • E. Haustein P. Schwille Ultrasensitive investigations of biological systems by fluorescence correlation spectroscopy Methods 29 2003 153-166
    • (2003) Methods , vol.29 , pp. 153-166
    • Haustein, E.1    Schwille, P.2
  • 4
    • 7044237136 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy of molecular motions and kinetics
    • M. Gosch R. Rigler Fluorescence correlation spectroscopy of molecular motions and kinetics Adv. Drug Deliv. Rev. 57 2005 169-190
    • (2005) Adv. Drug Deliv. Rev. , vol.57 , pp. 169-190
    • Gosch, M.1    Rigler, R.2
  • 5
    • 0024366273 scopus 로고
    • A new myocyte-specific enhancer-binding factor that recognizes a conserved element associated with multiple muscle-specific genes
    • L.A. Gossett D.J. Kelvin E.A. Sternberg E.N. Olson A new myocyte-specific enhancer-binding factor that recognizes a conserved element associated with multiple muscle-specific genes Mol. Cell. Biol. 9 1989 5022-5033
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 5022-5033
    • Gossett, L.A.1    Kelvin, D.J.2    Sternberg, E.A.3    Olson, E.N.4
  • 6
    • 9644265333 scopus 로고    scopus 로고
    • Mechanism of recruitment of class II histone deacetylases by myocyte enhancer factor-2
    • A. Han J. He Y. Wu J.O. Liu L. Chen Mechanism of recruitment of class II histone deacetylases by myocyte enhancer factor-2 J. Mol. Biol. 345 2005 91-102
    • (2005) J. Mol. Biol. , vol.345 , pp. 91-102
    • Han, A.1    He, J.2    Wu, Y.3    Liu, J.O.4    Chen, L.5
  • 7
    • 0036165434 scopus 로고    scopus 로고
    • MEF2: A calcium-dependent regulator of cell division, differentiation and death
    • T.A. McKinsey C.L. Zhang E.N. Olson MEF2: A calcium-dependent regulator of cell division, differentiation and death Trends Biochem. Sci. 27 2002 40-47
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 40-47
    • McKinsey, T.A.1    Zhang, C.L.2    Olson, E.N.3
  • 8
    • 0141991995 scopus 로고    scopus 로고
    • Role of MADS box proteins and their cofactors in combinatorial control of gene expression and cell development
    • F. Messenguy E. Dubois Role of MADS box proteins and their cofactors in combinatorial control of gene expression and cell development Gene 316 2003 1-21
    • (2003) Gene , vol.316 , pp. 1-21
    • Messenguy, F.1    Dubois, E.2
  • 9
    • 0030973867 scopus 로고    scopus 로고
    • DNA binding by MADS-box transcription factors: A molecular mechanism for differential DNA binding
    • A.G. West P. Shore A.D. Sharrocks DNA binding by MADS-box transcription factors: A molecular mechanism for differential DNA binding Mol. Cell. Biol. 17 1997 2876-2887
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2876-2887
    • West, A.G.1    Shore, P.2    Sharrocks, A.D.3
  • 10
    • 0026782992 scopus 로고
    • Human myocyte-specific enhancer factor 2 comprises a group of tissue-restricted MADS box transcription factors
    • Y.T. Yu R.E. Breitbart L.B. Smoot Y. Lee V. Mahdavi B. Nadal-Ginard Human myocyte-specific enhancer factor 2 comprises a group of tissue-restricted MADS box transcription factors Genes Dev. 6 1992 1783-1798
    • (1992) Genes Dev. , vol.6 , pp. 1783-1798
    • Yu, Y.T.1    Breitbart, R.E.2    Smoot, L.B.3    Lee, Y.4    Mahdavi, V.5    Nadal-Ginard, B.6
  • 11
    • 0028934434 scopus 로고
    • The MADS-box family of transcription factors
    • P. Shore A.D. Sharrocks The MADS-box family of transcription factors Eur. J. Biochem. 229 1995 1-13
    • (1995) Eur. J. Biochem. , vol.229 , pp. 1-13
    • Shore, P.1    Sharrocks, A.D.2
  • 12
    • 0029994419 scopus 로고    scopus 로고
    • Mutational analysis of the DNA binding, dimerization, and transcriptional activation domains of MEF2C
    • J.D. Molkentin B.L. Black J.F. Martin E.N. Olson Mutational analysis of the DNA binding, dimerization, and transcriptional activation domains of MEF2C Mol. Cell. Biol. 16 1996 2627-2636
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2627-2636
    • Molkentin, J.D.1    Black, B.L.2    Martin, J.F.3    Olson, E.N.4
  • 13
    • 0028838391 scopus 로고
    • Determination of the consensus binding site for MEF2 expressed in muscle and brain reveals tissue-specific sequence constraints
    • V. Andres M. Cervera V. Mahdavi Determination of the consensus binding site for MEF2 expressed in muscle and brain reveals tissue-specific sequence constraints J. Biol. Chem. 270 1995 23246-23249
    • (1995) J. Biol. Chem. , vol.270 , pp. 23246-23249
    • Andres, V.1    Cervera, M.2    Mahdavi, V.3
  • 14
    • 0034213458 scopus 로고    scopus 로고
    • Solution structure of the MEF2A-DNA complex: Structural basis for the modulation of DNA binding and specificity by MADS-box transcription factors
    • K. Huang J.M. Louis L. Donaldson F.L. Lim A.D. Sharrocks G.M. Clore Solution structure of the MEF2A-DNA complex: Structural basis for the modulation of DNA binding and specificity by MADS-box transcription factors EMBO J. 19 2000 2615-2628
    • (2000) EMBO J. , vol.19 , pp. 2615-2628
    • Huang, K.1    Louis, J.M.2    Donaldson, L.3    Lim, F.L.4    Sharrocks, A.D.5    Clore, G.M.6
  • 15
    • 0034708333 scopus 로고    scopus 로고
    • Crystal structure of MEF2A core bound to DNA at 1.5-Å resolution
    • E. Santelli T.J. Richmond Crystal structure of MEF2A core bound to DNA at 1.5-Å resolution J. Mol. Biol. 297 2000 437-449
    • (2000) J. Mol. Biol. , vol.297 , pp. 437-449
    • Santelli, E.1    Richmond, T.J.2
  • 17
    • 4243642135 scopus 로고
    • Comparison of theories for the translational and rotational diffusion coefficients of rod-like macromolecules. Application to short DNA fragments
    • M. Tirado C. Martinez J. Garcia de la Torre Comparison of theories for the translational and rotational diffusion coefficients of rod-like macromolecules. Application to short DNA fragments J. Chem. Phys. 81 1984 2047-2052
    • (1984) J. Chem. Phys. , vol.81 , pp. 2047-2052
    • Tirado, M.1    Martinez, C.2    Garcia de la Torre, J.3
  • 18
    • 0032475848 scopus 로고    scopus 로고
    • The N-terminal methionine is a major determinant of the DNA binding specificity of MEF-2C
    • D. Meierhans R.K. Allemann The N-terminal methionine is a major determinant of the DNA binding specificity of MEF-2C J. Biol. Chem. 273 1998 26052-26060
    • (1998) J. Biol. Chem. , vol.273 , pp. 26052-26060
    • Meierhans, D.1    Allemann, R.K.2
  • 19
    • 0030728598 scopus 로고    scopus 로고
    • High affinity binding of MEF-2C correlates with DNA binding
    • D. Meierhans M. Sieber R.K. Allemann High affinity binding of MEF-2C correlates with DNA binding Nucleic Acids Res. 25 1997 4537-4544
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4537-4544
    • Meierhans, D.1    Sieber, M.2    Allemann, R.K.3
  • 21
    • 18744391949 scopus 로고    scopus 로고
    • Two-hybrid fluorescence cross-correlation spectroscopy detects protein-protein interactions in vivo
    • N. Baudendistel G. Muller W. Waldeck P. Angel J. Langowski Two-hybrid fluorescence cross-correlation spectroscopy detects protein-protein interactions in vivo Chem. Phys. Chem. 6 2005 984-990
    • (2005) Chem. Phys. Chem. , vol.6 , pp. 984-990
    • Baudendistel, N.1    Muller, G.2    Waldeck, W.3    Angel, P.4    Langowski, J.5
  • 22
    • 22244464837 scopus 로고    scopus 로고
    • Two-photon cross-correlation analysis of intracellular reactions with variable stoichiometry
    • S.A. Kim K.G. Heinze K. Bacia M.N. Waxham P. Schwille Two-photon cross-correlation analysis of intracellular reactions with variable stoichiometry Biophys. J. 88 2005 4319-4336
    • (2005) Biophys. J. , vol.88 , pp. 4319-4336
    • Kim, S.A.1    Heinze, K.G.2    Bacia, K.3    Waxham, M.N.4    Schwille, P.5
  • 23
    • 0040182980 scopus 로고    scopus 로고
    • Simultaneous binding of two DNA duplexes to the NtrC-enhancer complex studied by two-color fluorescence cross-correlation spectroscopy
    • K. Rippe Simultaneous binding of two DNA duplexes to the NtrC-enhancer complex studied by two-color fluorescence cross-correlation spectroscopy Biochemistry 39 2000 2131-2139
    • (2000) Biochemistry , vol.39 , pp. 2131-2139
    • Rippe, K.1
  • 24
    • 0035912866 scopus 로고    scopus 로고
    • Interaction of fluorescence labeled single-stranded DNA with hexameric DNA-helicase RepA: A photon and fluorescence correlation spectroscopy study
    • H. Xu J. Frank U. Trier S. Hammer W. Schroder J. Behlke M. Schafer-Korting J.F. Holzwarth W. Saenger Interaction of fluorescence labeled single-stranded DNA with hexameric DNA-helicase RepA: A photon and fluorescence correlation spectroscopy study Biochemistry 40 2001 7211-7218
    • (2001) Biochemistry , vol.40 , pp. 7211-7218
    • Xu, H.1    Frank, J.2    Trier, U.3    Hammer, S.4    Schroder, W.5    Behlke, J.6    Schafer-Korting, M.7    Holzwarth, J.F.8    Saenger, W.9
  • 25
    • 0032520644 scopus 로고    scopus 로고
    • DNA binding and oligomerization of NtrC studied by fluorescence anisotropy and fluorescence correlation spectroscopy
    • F.W. Sevenich J. Langowski V. Weiss K. Rippe DNA binding and oligomerization of NtrC studied by fluorescence anisotropy and fluorescence correlation spectroscopy Nucleic Acids Res. 26 1998 1373-1381
    • (1998) Nucleic Acids Res. , vol.26 , pp. 1373-1381
    • Sevenich, F.W.1    Langowski, J.2    Weiss, V.3    Rippe, K.4
  • 26
  • 27
    • 4143147548 scopus 로고    scopus 로고
    • Detection of protein-DNA interactions in crude cellular extracts by fluorescence correlation spectroscopy
    • T. Kobayashi N. Okamoto T. Sawasaki Y. Endo Detection of protein-DNA interactions in crude cellular extracts by fluorescence correlation spectroscopy Anal. Biochem. 332 2004 58-66
    • (2004) Anal. Biochem. , vol.332 , pp. 58-66
    • Kobayashi, T.1    Okamoto, N.2    Sawasaki, T.3    Endo, Y.4
  • 28
    • 0042358627 scopus 로고    scopus 로고
    • Analysis of p53 'latency' and 'activation' by fluorescence correlation spectroscopy. Evidence for different modes of high affinity DNA binding
    • J. Wolcke M. Reimann M. Klumpp T. Gohler E. Kim W. Deppert Analysis of p53 'latency' and 'activation' by fluorescence correlation spectroscopy. Evidence for different modes of high affinity DNA binding J. Biol. Chem. 278 2003 32587-32595
    • (2003) J. Biol. Chem. , vol.278 , pp. 32587-32595
    • Wolcke, J.1    Reimann, M.2    Klumpp, M.3    Gohler, T.4    Kim, E.5    Deppert, W.6
  • 30
    • 0029736777 scopus 로고    scopus 로고
    • DNA-binding properties of Arabidopsis MADS domain homeotic proteins APETALA1, APETALA3, PISTILLATA and AGAMOUS
    • J.L. Riechmann M. Wang E.M. Meyerowitz DNA-binding properties of Arabidopsis MADS domain homeotic proteins APETALA1, APETALA3, PISTILLATA and AGAMOUS Nucleic Acids Res. 24 1996 3134-3141
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3134-3141
    • Riechmann, J.L.1    Wang, M.2    Meyerowitz, E.M.3
  • 31
    • 0029102041 scopus 로고
    • Structure of serum response factor core bound to DNA
    • L. Pellegrini S. Tan T. Richmond Structure of serum response factor core bound to DNA Nature 376 1995 490-497
    • (1995) Nature , vol.376 , pp. 490-497
    • Pellegrini, L.1    Tan, S.2    Richmond, T.3
  • 32
    • 0030950532 scopus 로고    scopus 로고
    • DNA-binding specificity of Mcm1: Operator mutations that alter DNA-binding and transcriptional activities by a MADS box protein
    • T.B. Acton H. Zhong A.K. Vershon DNA-binding specificity of Mcm1: operator mutations that alter DNA-binding and transcriptional activities by a MADS box protein Mol. Cell. Biol. 17 1997 1881-1889
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1881-1889
    • Acton, T.B.1    Zhong, H.2    Vershon, A.K.3
  • 33
    • 0032509980 scopus 로고    scopus 로고
    • Crystal structure of the yeast MATa2/MCM1/DNA ternary complex
    • S. Tan T.J. Richmond Crystal structure of the yeast MATa2/MCM1/DNA ternary complex Nature 391 1998 660-666
    • (1998) Nature , vol.391 , pp. 660-666
    • Tan, S.1    Richmond, T.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.