메뉴 건너뛰기




Volumn 44, Issue 37, 2005, Pages 12480-12490

Cardiac-specific Nkx2.5 homeodomain: Conformational stability and specific DNA binding of Nkx2.5(C56S)

Author keywords

[No Author keywords available]

Indexed keywords

BIOMEDICAL ENGINEERING; CARDIOLOGY; CONFORMATIONS; DIFFERENTIAL SCANNING CALORIMETRY; STOICHIOMETRY; THERMOANALYSIS; THERMODYNAMICS;

EID: 24944574310     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050835s     Document Type: Article
Times cited : (13)

References (41)
  • 4
    • 0036789946 scopus 로고    scopus 로고
    • Sequence-specific DNA binding by the vnd/NK-2 homeodomain of Drosophila
    • Wang, L. H., Chmelik, R., and Nirenberg, M. (2002) Sequence-specific DNA binding by the vnd/NK-2 homeodomain of Drosophila, Proc. Natl. Acad. Sci. U.S.A. 99, 12721-12726.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 12721-12726
    • Wang, L.H.1    Chmelik, R.2    Nirenberg, M.3
  • 5
    • 0029046714 scopus 로고
    • Identification of novel DNA binding targets and regulatory domains of a murine tinman homeodomain factor, Nkx2.5
    • Chen, C. Y., and Schwartz, R. J. (1995) Identification of novel DNA binding targets and regulatory domains of a murine tinman homeodomain factor, Nkx2.5, J. Biol. Chem. 270, 15628-15633.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15628-15633
    • Chen, C.Y.1    Schwartz, R.J.2
  • 6
    • 0031016315 scopus 로고    scopus 로고
    • Energetics of folding and DNA binding of the MAT α2 homeodomain
    • Carra, J. H., and Privalov, P. L. (1997) Energetics of folding and DNA binding of the MAT α2 homeodomain, Biochemistry 36, 526-535.
    • (1997) Biochemistry , vol.36 , pp. 526-535
    • Carra, J.H.1    Privalov, P.L.2
  • 7
    • 0035942321 scopus 로고    scopus 로고
    • The vnd/NK-2 homeodomain: Thermodynamics of reversible unfolding and DNA binding for wild-type and with residue replacements H52R and H52R/T56W in helix III
    • Gonzalez, M., Weiler, S., Ferretti, J. A., and Ginsburg, A. (2001) The vnd/NK-2 homeodomain: Thermodynamics of reversible unfolding and DNA binding for wild-type and with residue replacements H52R and H52R/T56W in helix III, Biochemistry 40, 4923-4931.
    • (2001) Biochemistry , vol.40 , pp. 4923-4931
    • Gonzalez, M.1    Weiler, S.2    Ferretti, J.A.3    Ginsburg, A.4
  • 9
    • 0035877733 scopus 로고    scopus 로고
    • Aromatic amino acids are critical for stability of the bicoid homeodomain
    • Subramaniam, V., Jovin, T. M., and Rivera-Pomar, R. V. (2001) Aromatic amino acids are critical for stability of the bicoid homeodomain, J. Biol. Chem. 276, 21506-21511.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21506-21511
    • Subramaniam, V.1    Jovin, T.M.2    Rivera-Pomar, R.V.3
  • 10
    • 0032079543 scopus 로고    scopus 로고
    • Site-directed mutations in the vnd/NK-2 homeodomain. Basis of variations in structure and sequence-specific DNA binding
    • Weiler, S., Gruschus, J. M., Tsao, D. H., Yu, L., Wang, L. H., Nirenberg, M., and Ferretti, J. A. (1998) Site-directed mutations in the vnd/NK-2 homeodomain. Basis of variations in structure and sequence-specific DNA binding, J. Biol. Chem. 273, 10994-11000.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10994-11000
    • Weiler, S.1    Gruschus, J.M.2    Tsao, D.H.3    Yu, L.4    Wang, L.H.5    Nirenberg, M.6    Ferretti, J.A.7
  • 11
    • 0024240703 scopus 로고
    • Molecular analysis of even-skipped mutants in Drosophila development
    • Frasch, M., Warrior, R., Tugwood, J., and Levine, M. (1988) Molecular analysis of even-skipped mutants in Drosophila development, Genes Dev. 2, 1824-1838.
    • (1988) Genes Dev. , vol.2 , pp. 1824-1838
    • Frasch, M.1    Warrior, R.2    Tugwood, J.3    Levine, M.4
  • 12
    • 0028023149 scopus 로고
    • The C-terminus of the homeodomain is required for functional specificity of the Drosophila rough gene
    • Heberlein, U., Penton, A., Falsafi, S., Hackett, D., and Rubin, G. M. (1994) The C-terminus of the homeodomain is required for functional specificity of the Drosophila rough gene, Mech. Dev. 48, 35-49.
    • (1994) Mech. Dev. , vol.48 , pp. 35-49
    • Heberlein, U.1    Penton, A.2    Falsafi, S.3    Hackett, D.4    Rubin, G.M.5
  • 13
    • 0021139598 scopus 로고
    • Sequence of a Drosophila segmentation gene: Protein structure homology with DNA-binding proteins
    • Laughon, A., and Scott, M. P. (1984) Sequence of a Drosophila segmentation gene: Protein structure homology with DNA-binding proteins, Nature 310, 25-31.
    • (1984) Nature , vol.310 , pp. 25-31
    • Laughon, A.1    Scott, M.P.2
  • 14
    • 0029595248 scopus 로고
    • Structure of the even-skipped homeodomain complexed to AT-rich DNA: New perspectives on homeodomain specificity
    • Hirsch, J. A., and Aggarwal, A. K. (1995) Structure of the even-skipped homeodomain complexed to AT-rich DNA: New perspectives on homeodomain specificity, EMBO J. 14, 6280-6291.
    • (1995) EMBO J. , vol.14 , pp. 6280-6291
    • Hirsch, J.A.1    Aggarwal, A.K.2
  • 15
    • 0037155776 scopus 로고    scopus 로고
    • Transcriptional regulation of vertebrate cardiac morphogenesis
    • Bruneau, B. G. (2002) Transcriptional regulation of vertebrate cardiac morphogenesis, Circ. Res. 90, 509-519.
    • (2002) Circ. Res. , vol.90 , pp. 509-519
    • Bruneau, B.G.1
  • 16
    • 0037144658 scopus 로고    scopus 로고
    • Early signals in cardiac development
    • Zaffran, S., and Frasch, M. (2002) Early signals in cardiac development, Circ. Res. 91, 457-469.
    • (2002) Circ. Res. , vol.91 , pp. 457-469
    • Zaffran, S.1    Frasch, M.2
  • 17
    • 0027184211 scopus 로고
    • Csx: A murine homeobox-containing gene specifically expressed in the developing heart
    • Komuro, I., and Izumo, S. (1993) Csx: A murine homeobox-containing gene specifically expressed in the developing heart, Proc. Natl. Acad. Sci. U.S.A. 90, 8145-8149.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 8145-8149
    • Komuro, I.1    Izumo, S.2
  • 20
    • 0035923555 scopus 로고    scopus 로고
    • NKX2.5 mutations in patients with tetralogy of fallot
    • Goldmuntz, E., Geiger, E., and Benson, D. W. (2001) NKX2.5 mutations in patients with tetralogy of fallot, Circulation 104, 2565-2568.
    • (2001) Circulation , vol.104 , pp. 2565-2568
    • Goldmuntz, E.1    Geiger, E.2    Benson, D.W.3
  • 21
    • 4444223413 scopus 로고    scopus 로고
    • Biochemical analyses of eight NKX2.5 homeodomain missense mutations causing atrioventricular block and cardiac anomalies
    • Kasahara, H., and Benson, D. W. (2004) Biochemical analyses of eight NKX2.5 homeodomain missense mutations causing atrioventricular block and cardiac anomalies, Cardiovasc. Res. 64, 40-51.
    • (2004) Cardiovasc. Res. , vol.64 , pp. 40-51
    • Kasahara, H.1    Benson, D.W.2
  • 22
    • 0029669183 scopus 로고    scopus 로고
    • Molecular cloning, chromosomal mapping, and characterization of the human cardiac-specific homeobox gene hCsx
    • Turbay, D., Wechsler, S. B., Blanchard, K. M., and Izumo, S. (1996) Molecular cloning, chromosomal mapping, and characterization of the human cardiac-specific homeobox gene hCsx, Mol. Med. 2, 86-96.
    • (1996) Mol. Med. , vol.2 , pp. 86-96
    • Turbay, D.1    Wechsler, S.B.2    Blanchard, K.M.3    Izumo, S.4
  • 23
    • 0033546260 scopus 로고    scopus 로고
    • The three-dimensional structure of the vnd/NK-2 homeodomain-DNA complex by NMR spectroscopy
    • Gruschus, J. M., Tsao, D. H. H., Wang, L. H., Nirenberg, M., and Ferretti, J. A. (1999) The three-dimensional structure of the vnd/NK-2 homeodomain-DNA complex by NMR spectroscopy, J. Mol. Biol. 289, 529-545.
    • (1999) J. Mol. Biol. , vol.289 , pp. 529-545
    • Gruschus, J.M.1    Tsao, D.H.H.2    Wang, L.H.3    Nirenberg, M.4    Ferretti, J.A.5
  • 24
    • 0023049766 scopus 로고
    • Protein volumes and hydration effects. The calculations of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences
    • Perkins, S. J. (1986) Protein volumes and hydration effects. The calculations of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences, Eur. J. Biochem. 157, 169-180.
    • (1986) Eur. J. Biochem. , vol.157 , pp. 169-180
    • Perkins, S.J.1
  • 25
    • 0014725117 scopus 로고
    • Oligonucleotide interactions. III. Circular dichroism studies of the conformation of deoxyoligonucleotides
    • Cantor, C. R., Warshaw, M. M., and Shapiro, H. (1970) Oligonucleotide interactions. III. Circular dichroism studies of the conformation of deoxyoligonucleotides, Biopolymers 9, 1059-1077.
    • (1970) Biopolymers , vol.9 , pp. 1059-1077
    • Cantor, C.R.1    Warshaw, M.M.2    Shapiro, H.3
  • 26
    • 0028658407 scopus 로고
    • Elongation of helix III of the NK-2 homeodomain upon binding to DNA: A secondary structure study by NMR
    • Tsao, D. H., Gruschus, J. M., Wang, L. H., Nirenberg, M., and Ferretti, J. A. (1994) Elongation of helix III of the NK-2 homeodomain upon binding to DNA: A secondary structure study by NMR, Biochemistry 33, 15053-15060.
    • (1994) Biochemistry , vol.33 , pp. 15053-15060
    • Tsao, D.H.1    Gruschus, J.M.2    Wang, L.H.3    Nirenberg, M.4    Ferretti, J.A.5
  • 27
    • 22444438859 scopus 로고    scopus 로고
    • Letter to the Editor: NMR assignments of the DNA-bound human Csx/Nkx2.5 homeodomain and NK-2-specific domain
    • Lee, H. S., Gruschus, J. M., Zang, T., and Ferretti, J. A. (2005) Letter to the Editor: NMR assignments of the DNA-bound human Csx/Nkx2.5 homeodomain and NK-2-specific domain, J. Biomol. NMR 31, 75-76.
    • (2005) J. Biomol. NMR , vol.31 , pp. 75-76
    • Lee, H.S.1    Gruschus, J.M.2    Zang, T.3    Ferretti, J.A.4
  • 28
    • 0033210750 scopus 로고    scopus 로고
    • Signal enhancement using 45 degrees water flipback for 3D N-15-edited ROESY and NOESY HMQC and HSQC
    • Gruschus, J. M., and Ferretti, J. A. (1999) Signal enhancement using 45 degrees water flipback for 3D N-15-edited ROESY and NOESY HMQC and HSQC, J. Magn. Reson. 140, 451-459.
    • (1999) J. Magn. Reson. , vol.140 , pp. 451-459
    • Gruschus, J.M.1    Ferretti, J.A.2
  • 29
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes, J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 30
    • 0026696116 scopus 로고
    • Analysis of the circular dichroism spectrum of proteins using the convex constraint algorithm: A practical guide
    • Perczel, A., Park, K., and Fasman, G. D. (1992) Analysis of the circular dichroism spectrum of proteins using the convex constraint algorithm: A practical guide, Anal. Biochem. 203, 83-93.
    • (1992) Anal. Biochem. , vol.203 , pp. 83-93
    • Perczel, A.1    Park, K.2    Fasman, G.D.3
  • 33
    • 0025925409 scopus 로고
    • Differential scanning calorimetry study of reversible, partial unfolding transitions in dodecameric glutamine synthetase from Escherichia coli
    • Ginsburg, A., and Zolkiewski, M. (1991) Differential scanning calorimetry study of reversible, partial unfolding transitions in dodecameric glutamine synthetase from Escherichia coli, Biochemistry 30, 9421-9429.
    • (1991) Biochemistry , vol.30 , pp. 9421-9429
    • Ginsburg, A.1    Zolkiewski, M.2
  • 34
    • 0034581192 scopus 로고    scopus 로고
    • Problems and prospects in microcalorimetry of biological macromolecules
    • Privalov, G. P., and Privalov, P. L. (2000) Problems and prospects in microcalorimetry of biological macromolecules, Methods Enzymol. 323, 31-62.
    • (2000) Methods Enzymol. , vol.323 , pp. 31-62
    • Privalov, G.P.1    Privalov, P.L.2
  • 35
    • 0034237284 scopus 로고    scopus 로고
    • Aromatic interactions in homeodomains contribute to the low quantum yield of a conserved, buried tryptophan
    • Nanda, V., and Brand, L. (2000) Aromatic interactions in homeodomains contribute to the low quantum yield of a conserved, buried tryptophan, Proteins 40, 112-125.
    • (2000) Proteins , vol.40 , pp. 112-125
    • Nanda, V.1    Brand, L.2
  • 36
    • 10044223573 scopus 로고    scopus 로고
    • Kinetics of protein-DNA interaction: Facilitated target location in sequence-dependent potential
    • Slutsky, M., and Mirny, L. A. (2004) Kinetics of protein-DNA interaction: Facilitated target location in sequence-dependent potential, Biophys. J. 87, 4021-4035.
    • (2004) Biophys. J. , vol.87 , pp. 4021-4035
    • Slutsky, M.1    Mirny, L.A.2
  • 38
    • 0000866128 scopus 로고
    • Hydrophobic effect in protein folding and other noncovalent processes involving proteins
    • Spolar, R. S., Ha, J.-H., and Record, M. T. (1989) Hydrophobic effect in protein folding and other noncovalent processes involving proteins, Proc. Natl. Acad. Sci. U.S.A. 86, 8382-8385.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 8382-8385
    • Spolar, R.S.1    Ha, J.-H.2    Record, M.T.3
  • 39
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar, R. S., and Record, M. T. (1994) Coupling of local folding to site-specific binding of proteins to DNA, Science 263, 777-784.
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record, M.T.2
  • 41
    • 0030916275 scopus 로고    scopus 로고
    • Interaction of the vnd/NK-2 homeodomain with DNA by nuclear magnetic resonance spectroscopy: Basis of binding specificity
    • Gruschus, J. M., Tsao, D. H. H., Wang, L.-H., Nirenberg, M., and Ferretti, J. A. (1997) Interaction of the vnd/NK-2 homeodomain with DNA by nuclear magnetic resonance spectroscopy: Basis of binding specificity, Biochemistry 36, 5372-5380.
    • (1997) Biochemistry , vol.36 , pp. 5372-5380
    • Gruschus, J.M.1    Tsao, D.H.H.2    Wang, L.-H.3    Nirenberg, M.4    Ferretti, J.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.