메뉴 건너뛰기




Volumn 18, Issue 9, 1999, Pages 2563-2579

Solution structure of the HMG protein NHP6A and its interaction with DNA reveals the structural determinants for non-sequence-specific binding

Author keywords

Chromatin; DNA bending; DNA recognition; HMG box; NMR

Indexed keywords

AMINO ACID; CARBON 13; DNA BINDING PROTEIN; DOUBLE STRANDED DNA; HIGH MOBILITY GROUP PROTEIN; METHIONINE; NITROGEN 15; PHENYLALANINE;

EID: 0033522480     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.9.2563     Document Type: Article
Times cited : (161)

References (71)
  • 1
    • 0032006926 scopus 로고    scopus 로고
    • Structure prediction of a complex between the chromosomal protein HMG-D and DNA
    • Balaeff, A., Churchill, M.E.A. and Schulten, K. (1998) Structure prediction of a complex between the chromosomal protein HMG-D and DNA. Proteins Struct. Funct. Genet., 30, 113-135.
    • (1998) Proteins Struct. Funct. Genet. , vol.30 , pp. 113-135
    • Balaeff, A.1    Churchill, M.E.A.2    Schulten, K.3
  • 3
    • 0000221195 scopus 로고
    • Computer-optimized homonuclear Tocsy experiments with suppression of cross relaxation
    • Briand, J. and Ernst, R.R. (1991) Computer-optimized homonuclear Tocsy experiments with suppression of cross relaxation. Chem. Phys. Lett., 185, 276-285.
    • (1991) Chem. Phys. Lett. , vol.185 , pp. 276-285
    • Briand, J.1    Ernst, R.R.2
  • 5
    • 0030358586 scopus 로고    scopus 로고
    • High-mobility-group chromosomal proteins: Architectural components that facilitate chromatin function
    • Bustin, M. and Reeves, R. (1996) High-mobility-group chromosomal proteins: Architectural components that facilitate chromatin function. Prog. Nucleic Acid Res. Mol. Biol., 54, 35-100.
    • (1996) Prog. Nucleic Acid Res. Mol. Biol. , vol.54 , pp. 35-100
    • Bustin, M.1    Reeves, R.2
  • 7
    • 0028950413 scopus 로고
    • HMG-D is an architecture-specific protein that preferentially binds to DNA containing the dinucleotide TG
    • Churchill, M.E., Jones, D.N., Glaser, T., Hefner, H., Searles, M.A. and Travers, A.A. (1995) HMG-D is an architecture-specific protein that preferentially binds to DNA containing the dinucleotide TG. EMBO J., 14, 1264-1275.
    • (1995) EMBO J. , vol.14 , pp. 1264-1275
    • Churchill, M.E.1    Jones, D.N.2    Glaser, T.3    Hefner, H.4    Searles, M.A.5    Travers, A.A.6
  • 8
    • 0028331458 scopus 로고
    • NHP6A and NHP6B, which encode HMG1-like proteins, are candidates for downstream components of the yeast SLT2 mitogen-activated protein kinase pathway
    • Costigan, C., Kolodrubetz, D. and Snyder, M. (1994) NHP6A and NHP6B, which encode HMG1-like proteins, are candidates for downstream components of the yeast SLT2 mitogen-activated protein kinase pathway. Mol. Cell. Biol., 14, 2391-2403.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2391-2403
    • Costigan, C.1    Kolodrubetz, D.2    Snyder, M.3
  • 9
    • 0032162021 scopus 로고    scopus 로고
    • Sensitivity enhancement in the TROSY experiment
    • Czisch, M. and Boelens, R. (1998) Sensitivity enhancement in the TROSY experiment. J. Magn. Reson., 134, 158-160.
    • (1998) J. Magn. Reson. , vol.134 , pp. 158-160
    • Czisch, M.1    Boelens, R.2
  • 10
    • 0000347599 scopus 로고    scopus 로고
    • Helix structure and molecular recognition by B-DNA
    • Neidle, S. (ed.). Oxford University Press, Oxford, UK
    • Dickerson, R. (1998) Helix structure and molecular recognition by B-DNA. In Neidle, S. (ed.), Oxford Handbook of Nucleic Acid Structure. Oxford University Press, Oxford, UK, pp. 1-23.
    • (1998) Oxford Handbook of Nucleic Acid Structure , pp. 1-23
    • Dickerson, R.1
  • 11
    • 0032545156 scopus 로고    scopus 로고
    • Structure determination and analysis of helix parameters in the DNA decamer d(CATGGCCATG)2: Comparison of results from NMR and crystallography
    • Dornberger, U., Flemming, J. and Fritzsche, H. (1998) Structure determination and analysis of helix parameters in the DNA decamer d(CATGGCCATG)2: comparison of results from NMR and crystallography. J. Mol. Biol., 284, 1453-1463.
    • (1998) J. Mol. Biol. , vol.284 , pp. 1453-1463
    • Dornberger, U.1    Flemming, J.2    Fritzsche, H.3
  • 12
    • 0028329080 scopus 로고
    • Crystal structure of transcription factor E47: E-box recognition by a basic region helix-loop-helix dimer
    • Ellenberger, T., Fass, D., Arnaud, M. and Harrison, S.C. (1994) Crystal structure of transcription factor E47: E-box recognition by a basic region helix-loop-helix dimer. Genes Dev., 8, 970-980.
    • (1994) Genes Dev. , vol.8 , pp. 970-980
    • Ellenberger, T.1    Fass, D.2    Arnaud, M.3    Harrison, S.C.4
  • 13
    • 0028303884 scopus 로고
    • The high mobility group protein HMG1 can reversibly inhibit class II gene transcription by interaction with the TATA-binding protein
    • Ge, H. and Roeder, R.G. (1994) The high mobility group protein HMG1 can reversibly inhibit class II gene transcription by interaction with the TATA-binding protein. J. Biol. Chem., 269, 17136-17140.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17136-17140
    • Ge, H.1    Roeder, R.G.2
  • 14
    • 0028197368 scopus 로고
    • HMG domain proteins: Architectural elements in the assembly of nucleoprotein structures
    • Grosschedl, R., Giese, K. and Pagel, J. (1994) HMG domain proteins: Architectural elements in the assembly of nucleoprotein structures. Trends Genet., 10, 94-100.
    • (1994) Trends Genet. , vol.10 , pp. 94-100
    • Grosschedl, R.1    Giese, K.2    Pagel, J.3
  • 15
    • 9444245493 scopus 로고
    • Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR
    • Grzesiek, S. and Bax, A. (1992a) Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR. J. Am. Chem. Soc., 114, 6291-6293.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6291-6293
    • Grzesiek, S.1    Bax, A.2
  • 16
    • 44049109615 scopus 로고
    • An efficient experiment for sequential backbone assignment of medium-sized isotopically enriched proteins
    • Grzesiek, S. and Bax, A. (1992b) An efficient experiment for sequential backbone assignment of medium-sized isotopically enriched proteins. J. Magn. Reson., 99, 201-207.
    • (1992) J. Magn. Reson. , vol.99 , pp. 201-207
    • Grzesiek, S.1    Bax, A.2
  • 17
    • 0025328296 scopus 로고
    • A gene mapping to the sex-determining region of the mouse Y chromosome is a member of a novel family of embryonically expressed genes
    • Gubbay, J., Collignon, J., Koopman, P., Capel, B., Economou, A., Munsterberg, A., Vivian, N., Goodfellow, P. and Lovell-Badge, R. (1990) A gene mapping to the sex-determining region of the mouse Y chromosome is a member of a novel family of embryonically expressed genes. Nature, 346, 245-250.
    • (1990) Nature , vol.346 , pp. 245-250
    • Gubbay, J.1    Collignon, J.2    Koopman, P.3    Capel, B.4    Economou, A.5    Munsterberg, A.6    Vivian, N.7    Goodfellow, P.8    Lovell-Badge, R.9
  • 18
    • 0026089657 scopus 로고
    • Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA
    • Guntert, P., Braun, W. and Wuthrich, K. (1991) Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA. J. Mol. Biol., 217, 517-530.
    • (1991) J. Mol. Biol. , vol.217 , pp. 517-530
    • Guntert, P.1    Braun, W.2    Wuthrich, K.3
  • 19
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Guntert, P., Mumenthaler, C. and Wuthrich, K. (1997) Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol., 273, 283-298.
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 20
    • 0028657623 scopus 로고
    • Molecular basis of mammalian sexual determination: Activation of Mullerian inhibiting substance gene expression by SRY
    • published erratum appears in Science (1995) 267, 317
    • Haqq, C.M., King, C.Y., Ukiyama, E., Falsafi, S., Haqq, T.N., Donahoe, P.K. and Weiss, M.A. (1994) Molecular basis of mammalian sexual determination: Activation of Mullerian inhibiting substance gene expression by SRY [published erratum appears in Science (1995) 267, 317]. Science, 266, 1494-1500.
    • (1994) Science , vol.266 , pp. 1494-1500
    • Haqq, C.M.1    King, C.Y.2    Ukiyama, E.3    Falsafi, S.4    Haqq, T.N.5    Donahoe, P.K.6    Weiss, M.A.7
  • 21
    • 0029563931 scopus 로고
    • Structure of the A-domain of HMG1 and its interaction with DNA as studied by heteronuclear three- and four-dimensional NMR spectroscopy
    • Hardman, C.H., Broadhurst, R.W., Raine, A.R., Grasser, K.D., Thomas, J.O. and Laue, E.D. (1995) Structure of the A-domain of HMG1 and its interaction with DNA as studied by heteronuclear three- and four-dimensional NMR spectroscopy. Biochemistry, 34, 16596-16607.
    • (1995) Biochemistry , vol.34 , pp. 16596-16607
    • Hardman, C.H.1    Broadhurst, R.W.2    Raine, A.R.3    Grasser, K.D.4    Thomas, J.O.5    Laue, E.D.6
  • 22
    • 0029976603 scopus 로고    scopus 로고
    • Using CLUSTAL for multiple sequence alignments
    • Higgins, D.G., Thompson, J.D. and Gibson, T.J. (1996) Using CLUSTAL for multiple sequence alignments. Methods Enzymol., 266, 383-402.
    • (1996) Methods Enzymol. , vol.266 , pp. 383-402
    • Higgins, D.G.1    Thompson, J.D.2    Gibson, T.J.3
  • 23
    • 0028286473 scopus 로고
    • Evidence of novel secondary structure in DNA-bound protamine is revealed by Raman spectroscopy
    • Hud, N.V., Milanovich, F.P. and Balhorn, R. (1994) Evidence of novel secondary structure in DNA-bound protamine is revealed by Raman spectroscopy. Biochemistry, 33, 7528-7535.
    • (1994) Biochemistry , vol.33 , pp. 7528-7535
    • Hud, N.V.1    Milanovich, F.P.2    Balhorn, R.3
  • 26
    • 0024284648 scopus 로고
    • Structure of the lambda complex at 2.5 Å resolution: Details of the repressor-operator interactions
    • Jordan, S.R. and Pabo, C.O. (1988) Structure of the lambda complex at 2.5 Å resolution: Details of the repressor-operator interactions. Science, 242, 893-899.
    • (1988) Science , vol.242 , pp. 893-899
    • Jordan, S.R.1    Pabo, C.O.2
  • 27
    • 0030031440 scopus 로고    scopus 로고
    • Photoreactivity of platinum (II) in cisplatin-modified DNA affords specific cross-links to HMG domain proteins
    • Kane, S.A. and Lippard, S.J. (1996) Photoreactivity of platinum (II) in cisplatin-modified DNA affords specific cross-links to HMG domain proteins. Biochemistry, 35, 2180-2188.
    • (1996) Biochemistry , vol.35 , pp. 2180-2188
    • Kane, S.A.1    Lippard, S.J.2
  • 28
    • 0027483012 scopus 로고
    • Co-crystal structure of TBP recognizing the minor groove of a TATA element
    • Kim, J.L., Nikolov, D.B. and Burley, S.K. (1993a) Co-crystal structure of TBP recognizing the minor groove of a TATA element. Nature, 365, 520-527.
    • (1993) Nature , vol.365 , pp. 520-527
    • Kim, J.L.1    Nikolov, D.B.2    Burley, S.K.3
  • 29
    • 0027504913 scopus 로고
    • Crystal structure of a yeast TBP/TATA-box complex
    • Kim, Y., Geiger, J.H., Hahn, S. and Sigler, P.B. (1993b) Crystal structure of a yeast TBP/TATA-box complex. Nature, 365, 512-520.
    • (1993) Nature , vol.365 , pp. 512-520
    • Kim, Y.1    Geiger, J.H.2    Hahn, S.3    Sigler, P.B.4
  • 30
    • 0027142992 scopus 로고
    • The SRY high-mobility-group box recognizes DNA by partial intercalation in the minor groove: A topclogical mechanism of sequence specificity
    • King, C.Y. and Weiss, M.A. (1993) The SRY high-mobility-group box recognizes DNA by partial intercalation in the minor groove: A topclogical mechanism of sequence specificity. Proc. Natl Acad. Sci. USA, 90, 11990-11994.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 11990-11994
    • King, C.Y.1    Weiss, M.A.2
  • 31
    • 0025239027 scopus 로고
    • Duplicated NHP6 genes of Saccharomyces cerevisiae encode proteins homologous to bovine high mobility group protein 1
    • Kolodrubetz, D. and Burgum, A. (1990) Duplicated NHP6 genes of Saccharomyces cerevisiae encode proteins homologous to bovine high mobility group protein 1. J. Biol. Chem., 265, 3234-3239.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3234-3239
    • Kolodrubetz, D.1    Burgum, A.2
  • 32
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M. and Wuthrich, K. (1996) MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graph., 14, 51-55, 29-32.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 33
    • 0021285494 scopus 로고
    • Concentrations of high-mobility-group proteins in the nucleus and cytoplasm of several rat tissues
    • Kuehl, L., Salmond, B. and Tran, L. (1984) Concentrations of high-mobility-group proteins in the nucleus and cytoplasm of several rat tissues. J. Cell Biol., 99, 648-654.
    • (1984) J. Cell Biol. , vol.99 , pp. 648-654
    • Kuehl, L.1    Salmond, B.2    Tran, L.3
  • 34
    • 0025643362 scopus 로고
    • A general method for rapid site-directed mutagenesis using the polymerase chain reaction
    • Landt, O., Grunert, H.P. and Hahn, U. (1990) A general method for rapid site-directed mutagenesis using the polymerase chain reaction. Gene, 96, 125-128.
    • (1990) Gene , vol.96 , pp. 125-128
    • Landt, O.1    Grunert, H.P.2    Hahn, U.3
  • 35
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R.A., Rullmann, J.A., MacArthur, M.W., Kaptein, R. and Thornton, J.M. (1996) AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR, 8, 477-486.
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmann, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 36
    • 0028022578 scopus 로고
    • 13C HMQC-NOESY experiment for extracting intermolecular NOE contacts in molecular complexes
    • 13C HMQC-NOESY experiment for extracting intermolecular NOE contacts in molecular complexes. FEBS Lett., 350, 87-90.
    • (1994) FEBS Lett. , vol.350 , pp. 87-90
    • Lee, W.1    Revington, M.J.2    Arrowsmith, C.3    Kay, L.E.4
  • 37
    • 0029131298 scopus 로고
    • Structural basis for DNA bending by the architectural transcription factor LEF-1
    • Love, J.J., Li, X., Case, D.A., Giese, K., Grosschedi, R. and Wright, P.E. (1995) Structural basis for DNA bending by the architectural transcription factor LEF-1. Nature, 376, 791-795.
    • (1995) Nature , vol.376 , pp. 791-795
    • Love, J.J.1    Li, X.2    Case, D.A.3    Giese, K.4    Grosschedi, R.5    Wright, P.E.6
  • 38
    • 0025780755 scopus 로고
    • Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA
    • Luisi, B.F., Xu, W.X., Otwinowski, Z., Freedman, L.P., Yamamoto, K.R. and Sigler, P.B. (1991) Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA. Nature, 352, 497-505.
    • (1991) Nature , vol.352 , pp. 497-505
    • Luisi, B.F.1    Xu, W.X.2    Otwinowski, Z.3    Freedman, L.P.4    Yamamoto, K.R.5    Sigler, P.B.6
  • 40
    • 0033553164 scopus 로고    scopus 로고
    • 15N-labeled DNA in a non-sequence specific protein-DNA complex resolves ambiguous assignments of intermolecular NOES
    • in press
    • 15N-labeled DNA in a non-sequence specific protein-DNA complex resolves ambiguous assignments of intermolecular NOES. J. Am. Chem. Soc., in press.
    • (1999) J. Am. Chem. Soc.
    • Masse, J.E.1    Allain, F.H.-T.2    Yen, Y.3    Johnson, R.C.4    Feigon, J.5
  • 41
  • 42
    • 0029048413 scopus 로고
    • Structure of BamHI endonuclease bound to DNA: Partial folding and unfolding on DNA binding
    • Newman, M., Strzelecka, T., Dorner, L.F., Schildkraut, I. and Aggarwal, A.K. (1995) Structure of BamHI endonuclease bound to DNA: Partial folding and unfolding on DNA binding. Science, 269, 656-663.
    • (1995) Science , vol.269 , pp. 656-663
    • Newman, M.1    Strzelecka, T.2    Dorner, L.F.3    Schildkraut, I.4    Aggarwal, A.K.5
  • 43
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A. and Honig, B. (1991) Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins, 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 44
    • 0030064348 scopus 로고    scopus 로고
    • Evidence for a shared structural role for HMG1 and linker histones B4 and H1 in organizing chromatin
    • Nightingale, K., Dimitrov, S., Reeves, R. and Wolffe, A.P. (1996) Evidence for a shared structural role for HMG1 and linker histones B4 and H1 in organizing chromatin. EMBO J., 15, 548-561.
    • (1996) EMBO J. , vol.15 , pp. 548-561
    • Nightingale, K.1    Dimitrov, S.2    Reeves, R.3    Wolffe, A.P.4
  • 45
    • 0028970118 scopus 로고
    • DNA looping by Saccharomyces cerevisiae high mobility group proteins NHP6A/B. Consequences for nucleoprotein complex assembly and chromatin condensation
    • Paull, T.T. and Johnson, R.C. (1995) DNA looping by Saccharomyces cerevisiae high mobility group proteins NHP6A/B. Consequences for nucleoprotein complex assembly and chromatin condensation. J. Biol. Chem., 270, 8744-8754.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8744-8754
    • Paull, T.T.1    Johnson, R.C.2
  • 46
    • 0027216519 scopus 로고
    • The nonspecific DNA-binding and -bending proteins HMG1 and HMG2 promote the assembly of complex nucleoprotein structures
    • Paull, T.T., Haykinson, M.J. and Johnson, R.C. (1993) The nonspecific DNA-binding and -bending proteins HMG1 and HMG2 promote the assembly of complex nucleoprotein structures. Genes Dev., 7, 1521-1534.
    • (1993) Genes Dev. , vol.7 , pp. 1521-1534
    • Paull, T.T.1    Haykinson, M.J.2    Johnson, R.C.3
  • 47
    • 0029825332 scopus 로고    scopus 로고
    • Yeast HMG proteins NHP6A/B potentiate promoter-specific transcriptional activation in vivo and assembly of preinitiation complexes in vitro
    • Paull, T.T., Carey, M. and Johnson, R.C. (1996) Yeast HMG proteins NHP6A/B potentiate promoter-specific transcriptional activation in vivo and assembly of preinitiation complexes in vitro. Genes Dev., 10, 2769-2781.
    • (1996) Genes Dev. , vol.10 , pp. 2769-2781
    • Paull, T.T.1    Carey, M.2    Johnson, R.C.3
  • 48
    • 0031566959 scopus 로고    scopus 로고
    • The acidic tail of the high mobility group protein HMG-D modulates the structural selectivity of DNA binding
    • Payet, D. and Travers, A. (1997) The acidic tail of the high mobility group protein HMG-D modulates the structural selectivity of DNA binding. J. Mol. Biol., 266, 66-75.
    • (1997) J. Mol. Biol. , vol.266 , pp. 66-75
    • Payet, D.1    Travers, A.2
  • 49
    • 0028921099 scopus 로고
    • An SRY mutation causing human sex reversal resolves a general mechanism of structure-specific DNA recognition: Application to the four-way DNA junction
    • Peters, R., King, C.Y., Ukiyama, E., Falsafi, S., Donahoe, P.K. and Weiss, M.A. (1995) An SRY mutation causing human sex reversal resolves a general mechanism of structure-specific DNA recognition: Application to the four-way DNA junction. Biochemistry, 34, 4569-4576.
    • (1995) Biochemistry , vol.34 , pp. 4569-4576
    • Peters, R.1    King, C.Y.2    Ukiyama, E.3    Falsafi, S.4    Donahoe, P.K.5    Weiss, M.A.6
  • 50
    • 0026569275 scopus 로고
    • Specific binding of chromosomal protein HMG1 to DNA damaged by the anticancer drug cisplatin
    • Pil, P.M. and Lippard, S.J. (1992) Specific binding of chromosomal protein HMG1 to DNA damaged by the anticancer drug cisplatin. Science, 256, 234-237.
    • (1992) Science , vol.256 , pp. 234-237
    • Pil, P.M.1    Lippard, S.J.2
  • 51
    • 0027359690 scopus 로고
    • High-mobilily-group 1 protein mediates DNA bending as determined by ring closures
    • Pil, P.M., Chow, C.S. and Lippard, S.J. (1993) High-mobilily-group 1 protein mediates DNA bending as determined by ring closures. Proc. Natl Acad. Sci. USA, 90, 9465-9469.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 9465-9469
    • Pil, P.M.1    Chow, C.S.2    Lippard, S.J.3
  • 53
    • 0032506009 scopus 로고    scopus 로고
    • TROSY in triple-resonance experiments: New perspectives for sequential NMR assignment of large proteins
    • Salzmann, M., Pervushin, K., Wider, G., Senn, H. and Wuthrich, K. (1998) TROSY in triple-resonance experiments: New perspectives for sequential NMR assignment of large proteins. Proc. Natl Acad. Sci. USA, 95, 13585-13590.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 13585-13590
    • Salzmann, M.1    Pervushin, K.2    Wider, G.3    Senn, H.4    Wuthrich, K.5
  • 54
    • 0029078364 scopus 로고
    • Activation of the TFIID-TFIIA complex with HMG-2
    • Shykind, B.M., Kim, J. and Sharp, P.A. (1995) Activation of the TFIID-TFIIA complex with HMG-2. Genes Dev., 9, 1354-1365.
    • (1995) Genes Dev. , vol.9 , pp. 1354-1365
    • Shykind, B.M.1    Kim, J.2    Sharp, P.A.3
  • 55
    • 0025364886 scopus 로고
    • A gene from the human sex-determining region encodes a protein with homology to a conserved DNA-binding motif
    • Sinclair, A.H. et al. (1990) A gene from the human sex-determining region encodes a protein with homology to a conserved DNA-binding motif. Nature, 346, 240-244.
    • (1990) Nature , vol.346 , pp. 240-244
    • Sinclair, A.H.1
  • 56
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar, R.S. and Record, M.T., Jr (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., Jr.2
  • 57
    • 0028999513 scopus 로고
    • Differences in the DNA-binding properties of the HMG-box domains of HMG1 and the sex-determining factor SRY
    • Teo, S.H., Grasser, K.D. and Thomas, J.O. (1995) Differences in the DNA-binding properties of the HMG-box domains of HMG1 and the sex-determining factor SRY. Eur. J. Biochem., 230, 943-950.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 943-950
    • Teo, S.H.1    Grasser, K.D.2    Thomas, J.O.3
  • 58
    • 0025794148 scopus 로고
    • LEF-1, a gene encoding a lymphoid-specific protein with an HMG domain, regulates T-cell receptor alpha enhancer function
    • Travis, A., Amsterdam, A., Belanger, C. and Grosschedl, R. (1991) LEF-1, a gene encoding a lymphoid-specific protein with an HMG domain, regulates T-cell receptor alpha enhancer function. Genes Dev., 5, 880-894.
    • (1991) Genes Dev. , vol.5 , pp. 880-894
    • Travis, A.1    Amsterdam, A.2    Belanger, C.3    Grosschedl, R.4
  • 59
    • 0029790690 scopus 로고    scopus 로고
    • Differential association of HMG1 and linker histones B4 and H1 with dinucleosomal DNA: Structural transitions and transcriptional repression
    • Ura, K., Nightingale, K. and Wolffe, A.P. (1996) Differential association of HMG1 and linker histones B4 and H1 with dinucleosomal DNA: Structural transitions and transcriptional repression. EMBO J., 15, 4959-4969.
    • (1996) EMBO J. , vol.15 , pp. 4959-4969
    • Ura, K.1    Nightingale, K.2    Wolffe, A.P.3
  • 60
    • 0026019629 scopus 로고
    • Identification and cloning of TCF-1, a T lymphocyte-specific transcription factor containing a sequence-specific HMG box
    • van de Wetering, M., Oosterwegel, M., Dooijes, D. and Clevers, H. (1991) Identification and cloning of TCF-1, a T lymphocyte-specific transcription factor containing a sequence-specific HMG box. EMBO J., 10, 123-132.
    • (1991) EMBO J. , vol.10 , pp. 123-132
    • Van De Wetering, M.1    Oosterwegel, M.2    Dooijes, D.3    Clevers, H.4
  • 61
    • 0030994385 scopus 로고    scopus 로고
    • Stimulation of V(D)J cleavage by high mobility group proteins
    • van Gent, D.C., Hiom, K., Paull, T.T. and Gellert, M. (1997) Stimulation of V(D)J cleavage by high mobility group proteins. EMBO J., 16, 2665-2670.
    • (1997) EMBO J. , vol.16 , pp. 2665-2670
    • Van Gent, D.C.1    Hiom, K.2    Paull, T.T.3    Gellert, M.4
  • 62
    • 0029584667 scopus 로고
    • Solution structure of the sequence-specific HMG box of the lymphocyte transcriptional activator Sox-4
    • van Houte, L.P., Chuprina, V.P., van der Wetering, M., Boelens, R., Kaptein, R. and Clevers, H. (1995) Solution structure of the sequence-specific HMG box of the lymphocyte transcriptional activator Sox-4. J. Biol. Chem., 270, 30516-30524.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30516-30524
    • Van Houte, L.P.1    Chuprina, V.P.2    Van Der Wetering, M.3    Boelens, R.4    Kaptein, R.5    Clevers, H.6
  • 64
    • 0024590341 scopus 로고
    • A human placental cDNA clone that encodes nonhistone chromosomal protein HMG-1
    • Wen, L., Huang, J.K., Johnson, B.H. and Reeck, G.R. (1989) A human placental cDNA clone that encodes nonhistone chromosomal protein HMG-1. Nucleic Acids Res., 17, 1197-1214.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 1197-1214
    • Wen, L.1    Huang, J.K.2    Johnson, B.H.3    Reeck, G.R.4
  • 65
    • 0029096665 scopus 로고
    • NMR spectroscopic analysis of the DNA conformation induced by the human testis determining factor SRY
    • Werner, M.H., Bianchi, M.E., Gronenborn, A.M. and Clore, G.M. (1995a) NMR spectroscopic analysis of the DNA conformation induced by the human testis determining factor SRY. Biochemistry, 34, 11998-12004.
    • (1995) Biochemistry , vol.34 , pp. 11998-12004
    • Werner, M.H.1    Bianchi, M.E.2    Gronenborn, A.M.3    Clore, G.M.4
  • 66
    • 0029075461 scopus 로고
    • Molecular basis of human 46X,Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex
    • Werner, M.H., Huth, J.R., Gronenborn, A.M. and Clore, G.M. (1995b) Molecular basis of human 46X,Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex. Cell, 81, 705-714.
    • (1995) Cell , vol.81 , pp. 705-714
    • Werner, M.H.1    Huth, J.R.2    Gronenborn, A.M.3    Clore, G.M.4
  • 67
    • 0027159254 scopus 로고
    • The crystal structure of EcoRV endonuclease and of its complexes with cognate and non-cognate DNA fragments
    • Winkler, F.K. et al. (1993) The crystal structure of EcoRV endonuclease and of its complexes with cognate and non-cognate DNA fragments. EMBO J., 12, 1781-1795.
    • (1993) EMBO J. , vol.12 , pp. 1781-1795
    • Winkler, F.K.1
  • 69
    • 0032548929 scopus 로고    scopus 로고
    • Determinants of DNA binding and bending by the Saccharomyces cerevisiae high mobility group protein NHP6A that are important for its biological activities. Role of the unique N terminus and putative intercalating methionine
    • Yen, Y.M., Wong, B. and Johnson, R.C. (1998) Determinants of DNA binding and bending by the Saccharomyces cerevisiae high mobility group protein NHP6A that are important for its biological activities. Role of the unique N terminus and putative intercalating methionine. J. Biol. Chem., 273, 4424-4435.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4424-4435
    • Yen, Y.M.1    Wong, B.2    Johnson, R.C.3
  • 70
    • 0029811475 scopus 로고    scopus 로고
    • HMG1 interacts with HOX proteins and enhances their DNA binding and transcriptional activation
    • Zappavigna, V., Falciola, L., Citterich, M.H., Mavilio, F. and Bianchi, M.E. (1996) HMG1 interacts with HOX proteins and enhances their DNA binding and transcriptional activation. EMBO J., 15, 4981-4991.
    • (1996) EMBO J. , vol.15 , pp. 4981-4991
    • Zappavigna, V.1    Falciola, L.2    Citterich, M.H.3    Mavilio, F.4    Bianchi, M.E.5
  • 71
    • 0028921810 scopus 로고
    • High mobility group protein 2 functionally interacts with the POU domains of octamer transcription factors
    • Zwilling, S., Konig, H. and Wirth, T. (1995) High mobility group protein 2 functionally interacts with the POU domains of octamer transcription factors. EMBO J., 14, 1198-1208.
    • (1995) EMBO J. , vol.14 , pp. 1198-1208
    • Zwilling, S.1    Konig, H.2    Wirth, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.