메뉴 건너뛰기




Volumn 48, Issue 27, 2009, Pages 6502-6507

Nucleosome binding properties and co-remodeling activities of native and in vivo acetylated HMGB-1 and HMGB-2 proteins

Author keywords

[No Author keywords available]

Indexed keywords

ATP-ASE ACTIVITY; BINDING PROPERTIES; CHROMATIN REMODELING; CORE PARTICLES; IN-VIVO; LINKER DNA; NUCLEOSOME; NUCLEOSOME SLIDING; NUCLEOSOMES; REMODELING ACTIVITY; SWI/SNF;

EID: 67650047868     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9004304     Document Type: Article
Times cited : (38)

References (41)
  • 1
    • 0003903126 scopus 로고
    • Springer Verlag KG, Berlin
    • Van Holde, K. (1988) Chromatin , Springer Verlag KG, Berlin.
    • (1988) Chromatin
    • Van Holde, K.1
  • 3
    • 0025837183 scopus 로고
    • The nucleosomal core histone octamer at 3.1 Å resolution: A tripartite protein assembly and a left-handed superhelix
    • Arents, G., Burlingame, R. W., Wang, B. C., Love, W. E., and Moudrianakis, E. N. (1991) The nucleosomal core histone octamer at 3.1 Å resolution: A tripartite protein assembly and a left-handed superhelix. Proc. Natl. Acad. Sci. U.S.A. 88, 10148-10152.
    • (1991) Proc. Natl. Acad. Sci. U.S.A , vol.88 , pp. 10148-10152
    • Arents, G.1    Burlingame, R.W.2    Wang, B.C.3    Love, W.E.4    Moudrianakis, E.N.5
  • 4
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosomal core particle at 2.8 Å resolution
    • Luger, K., Mäder, A. W., Richmond, R. U., Sargent, D. F., and Richmond, T. J. (1997) Crystal structure of the nucleosomal core particle at 2.8 Å resolution. Nature 389, 251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mäder, A.W.2    Richmond, R.U.3    Sargent, D.F.4    Richmond, T.J.5
  • 5
    • 0024573304 scopus 로고
    • Use of selectively trypsinized nucleosome core particles to analyze the role of the histone "tails" in the stabilization of the nucleosome
    • Ausio, J., Dong, F., and van Holde, K. E. (1989) Use of selectively trypsinized nucleosome core particles to analyze the role of the histone "tails" in the stabilization of the nucleosome. J. Mol. Biol. 206, 451-463.
    • (1989) J. Mol. Biol , vol.206 , pp. 451-463
    • Ausio, J.1    Dong, F.2    van Holde, K.E.3
  • 6
    • 0035890134 scopus 로고    scopus 로고
    • The N-terminus of histone H2B, but not that of histone H3 or its phosphorylation, is essential for chromosome condensation
    • de la Barre, A. E., Angelov, D., Molla, A., and Dimitrov, S. (2001) The N-terminus of histone H2B, but not that of histone H3 or its phosphorylation, is essential for chromosome condensation. EMBO J. 20, 6383-6393.
    • (2001) EMBO J , vol.20 , pp. 6383-6393
    • de la Barre, A.E.1    Angelov, D.2    Molla, A.3    Dimitrov, S.4
  • 7
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl, B. D., and Allis, C. D. (2000) The language of covalent histone modifications. Nature 403, 41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 11
    • 34250745886 scopus 로고    scopus 로고
    • Nucleosome stability mediated by histone variants H3.3 and H2A.Z
    • Jin, C., and Felsenfeld, G. (2007) Nucleosome stability mediated by histone variants H3.3 and H2A.Z. Genes Dev. 21, 1519-1529.
    • (2007) Genes Dev , vol.21 , pp. 1519-1529
    • Jin, C.1    Felsenfeld, G.2
  • 12
    • 34249795487 scopus 로고    scopus 로고
    • Histone variant nucleosomes: Structure, function and implication in disease
    • Boulard, M., Bouvet, P., Kundu, T. K., and Dimitrov, S. (2007) Histone variant nucleosomes: Structure, function and implication in disease. Subcell. Biochem. 41, 71-89.
    • (2007) Subcell. Biochem , vol.41 , pp. 71-89
    • Boulard, M.1    Bouvet, P.2    Kundu, T.K.3    Dimitrov, S.4
  • 13
    • 0037119967 scopus 로고    scopus 로고
    • Nucleosome sliding: Facts and fiction
    • Becker, P. B. (2002) Nucleosome sliding: Facts and fiction. EMBO J. 21, 4749-4753.
    • (2002) EMBO J , vol.21 , pp. 4749-4753
    • Becker, P.B.1
  • 14
    • 1542328273 scopus 로고    scopus 로고
    • Nucleosome remodelling: One mechanism, many phenomena?
    • Langst, G. L., and Becker, P. B. (2004) Nucleosome remodelling: One mechanism, many phenomena? Biochim. Biophys. Acta 1677, 58-63.
    • (2004) Biochim. Biophys. Acta , vol.1677 , pp. 58-63
    • Langst, G.L.1    Becker, P.B.2
  • 15
    • 34548544648 scopus 로고    scopus 로고
    • Chromatin remodeling and cancer, Part II: ATP-dependent chromatin remodeling
    • Wang, G. G., Allis, C. D., and Chi, P. (2007) Chromatin remodeling and cancer, Part II: ATP-dependent chromatin remodeling. Trends Mol. Med. 13, 373-380.
    • (2007) Trends Mol. Med , vol.13 , pp. 373-380
    • Wang, G.G.1    Allis, C.D.2    Chi, P.3
  • 20
    • 0032814140 scopus 로고    scopus 로고
    • Regulation of DNA-dependent activities by the functional motifs of the high-mobility group chromosomal proteins
    • Bustin, M. (1999) Regulation of DNA-dependent activities by the functional motifs of the high-mobility group chromosomal proteins. Mol. Cell. Biol. 19, 5237-5246.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 5237-5246
    • Bustin, M.1
  • 21
    • 35948985223 scopus 로고    scopus 로고
    • Chromosomal HMG-box proteins
    • Zlatanova, J, and Leuba, S. H, Eds, pp, Elsevier B.V, Amsterdam
    • Travers, A., and Thomas, J. O. (2004) Chromosomal HMG-box proteins. In Chromatin Structure and Dynamics: State-of-the-Art (Zlatanova, J., and Leuba, S. H., Eds.) pp 103-1134, Elsevier B.V., Amsterdam.
    • (2004) Chromatin Structure and Dynamics: State-of-the-Art , pp. 103-1134
    • Travers, A.1    Thomas, J.O.2
  • 22
    • 4243824006 scopus 로고    scopus 로고
    • The DNA chaperone HMGB1 facilitates ACF/CHRAC-dependent nucleosome sliding
    • Bonaldi, T., Langst, G., Strohner, R., Becker, P. B., and Bianchi, M. E. (2002) The DNA chaperone HMGB1 facilitates ACF/CHRAC-dependent nucleosome sliding. EMBO J. 21, 6865-6873.
    • (2002) EMBO J , vol.21 , pp. 6865-6873
    • Bonaldi, T.1    Langst, G.2    Strohner, R.3    Becker, P.B.4    Bianchi, M.E.5
  • 23
    • 0035807789 scopus 로고    scopus 로고
    • In vivo acetylation of HMGB1 protein enhances its binding affinity to distorted DNA structures
    • Ugrinova, I., Pasheva, E. A., Armengaud, J., and Pashev, I. G. (2001) In vivo acetylation of HMGB1 protein enhances its binding affinity to distorted DNA structures. Biochemistry 40, 14655-14660.
    • (2001) Biochemistry , vol.40 , pp. 14655-14660
    • Ugrinova, I.1    Pasheva, E.A.2    Armengaud, J.3    Pashev, I.G.4
  • 24
    • 33847646297 scopus 로고    scopus 로고
    • DNA bending versus DNA end-joining activity of HMGB1 protein is modulated by in vitro by acetylation
    • Ugrinova, I., Mitkova, E., Moskalenko, C., Pasherv, I. G., and Pasheva, E. A. (2007) DNA bending versus DNA end-joining activity of HMGB1 protein is modulated by in vitro by acetylation. Biochemistry 46, 2111-2117.
    • (2007) Biochemistry , vol.46 , pp. 2111-2117
    • Ugrinova, I.1    Mitkova, E.2    Moskalenko, C.3    Pasherv, I.G.4    Pasheva, E.A.5
  • 25
    • 0020198155 scopus 로고
    • The binding sites for large and small high-mobility-group (HMG) proteins. Studies on HMG-nucleosome interactions in vitro
    • Schroter, H., and Bode, J. (1982) The binding sites for large and small high-mobility-group (HMG) proteins. Studies on HMG-nucleosome interactions in vitro. Eur. J. Biochem. 127, 429-436.
    • (1982) Eur. J. Biochem , vol.127 , pp. 429-436
    • Schroter, H.1    Bode, J.2
  • 26
    • 0030064348 scopus 로고    scopus 로고
    • Evidence for a shared structural role for HMG1 and linker histones B4 and Hi 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 Hi 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
  • 27
    • 0032500508 scopus 로고    scopus 로고
    • The non-histone chromatin protein HMG1 protects linker DNA on the opposite to the protected by linker histones
    • An, W., van Holde, K., and Zlatanova, J. (1998) The non-histone chromatin protein HMG1 protects linker DNA on the opposite to the protected by linker histones. J. Biol. Chem. 273, 26289-26291.
    • (1998) J. Biol. Chem , vol.273 , pp. 26289-26291
    • An, W.1    van Holde, K.2    Zlatanova, J.3
  • 28
    • 0032512794 scopus 로고    scopus 로고
    • New DNA sequence rules for high affinity binding to histone octamer and sequence-directed nucleosome positioning
    • Lowary, P. T., and Widom, J. (1998) New DNA sequence rules for high affinity binding to histone octamer and sequence-directed nucleosome positioning. J. Mol. Biol. 276, 19-42.
    • (1998) J. Mol. Biol , vol.276 , pp. 19-42
    • Lowary, P.T.1    Widom, J.2
  • 29
    • 0033289822 scopus 로고    scopus 로고
    • Expression and purification of recombinant histones and nucleosome reconstitution
    • Luger, K., Rechsteiner, T. J., and Richmond, T. J. (1999) Expression and purification of recombinant histones and nucleosome reconstitution. Methods Mol. Biol. 119, 1-16.
    • (1999) Methods Mol. Biol , vol.119 , pp. 1-16
    • Luger, K.1    Rechsteiner, T.J.2    Richmond, T.J.3
  • 30
    • 0028467446 scopus 로고
    • Stimulation of GAL4 derivative binding to nucleosomal DNA by the yeast SWI/SNF complex
    • Cote, J., Quinn, J., Workman, J. L., and Peterson, C. L. (1994) Stimulation of GAL4 derivative binding to nucleosomal DNA by the yeast SWI/SNF complex. Science 265, 53-60.
    • (1994) Science , vol.265 , pp. 53-60
    • Cote, J.1    Quinn, J.2    Workman, J.L.3    Peterson, C.L.4
  • 31
    • 0031741231 scopus 로고    scopus 로고
    • Persistent interactions of core histone tails with nucleosomal DNA following acetylation and transcription factor binding
    • Mutskov, V., Gerber, D., Angelov, D., Ausio, J., Workman, J., and Dimitrov, S. (1998) Persistent interactions of core histone tails with nucleosomal DNA following acetylation and transcription factor binding. Mol. Cell. Biol. 18, 6293-6304.
    • (1998) Mol. Cell. Biol , vol.18 , pp. 6293-6304
    • Mutskov, V.1    Gerber, D.2    Angelov, D.3    Ausio, J.4    Workman, J.5    Dimitrov, S.6
  • 32
    • 0037961635 scopus 로고    scopus 로고
    • The histone variant Macro-H2A interferes with transcription factor binding and SWI/SNF nucleosome remodeling
    • Angelov, D., Molla, A., Perche, P. Y., Hans, F., Cote, J., Khochbin, S., Bouvet, P., and Dimitrov, S. (2003) The histone variant Macro-H2A interferes with transcription factor binding and SWI/SNF nucleosome remodeling. Mol. Cell 11, 1033-1041.
    • (2003) Mol. Cell , vol.11 , pp. 1033-1041
    • Angelov, D.1    Molla, A.2    Perche, P.Y.3    Hans, F.4    Cote, J.5    Khochbin, S.6    Bouvet, P.7    Dimitrov, S.8
  • 33
    • 3342939967 scopus 로고    scopus 로고
    • Acidic C-tail of HMGB1 is required for its target binding to nucleosome linker DNA and transcription stimulation
    • Ueda, T., Chou, H., Kawase, T., Shirakawa, H., and Yoshida, M. (2004) Acidic C-tail of HMGB1 is required for its target binding to nucleosome linker DNA and transcription stimulation. Biochemistry 43, 9901-9908.
    • (2004) Biochemistry , vol.43 , pp. 9901-9908
    • Ueda, T.1    Chou, H.2    Kawase, T.3    Shirakawa, H.4    Yoshida, M.5
  • 34
    • 0032574802 scopus 로고    scopus 로고
    • Perturbation of nucleosome core structure by the SWI/SNF complex persists after its attachment, enhancing subsequent transcription factor binding
    • Cote, J., Peterson, C. L., and Workman, J. L. (1998) Perturbation of nucleosome core structure by the SWI/SNF complex persists after its attachment, enhancing subsequent transcription factor binding. Proc. Natl. Acad. Sci. U.S.A. 95, 4947-4952.
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 4947-4952
    • Cote, J.1    Peterson, C.L.2    Workman, J.L.3
  • 35
    • 0032015582 scopus 로고    scopus 로고
    • Absence of Gcn5 HAT activity defines a novel state in the opening of chromatin at the PHO5 promoter in yeast
    • Gregory, P. D., Schmid, A., Zavari, M., Lui, L., Berger, S. L., and Hörz, W. (1998) Absence of Gcn5 HAT activity defines a novel state in the opening of chromatin at the PHO5 promoter in yeast. Mol. Cell 1, 495-505.
    • (1998) Mol. Cell , vol.1 , pp. 495-505
    • Gregory, P.D.1    Schmid, A.2    Zavari, M.3    Lui, L.4    Berger, S.L.5    Hörz, W.6
  • 36
    • 0033571273 scopus 로고    scopus 로고
    • Chromatin remodeling at the PHo8 promoter requires SWI/SNF and SAGA at a step subsequent to activator binding
    • Gregory, P. D., Schmid, A., Zavari, M., Muunsterkötter, M., and Horz, W. (1999) Chromatin remodeling at the PHo8 promoter requires SWI/SNF and SAGA at a step subsequent to activator binding. EMBO J. 18, 6407-6417.
    • (1999) EMBO J , vol.18 , pp. 6407-6417
    • Gregory, P.D.1    Schmid, A.2    Zavari, M.3    Muunsterkötter, M.4    Horz, W.5
  • 37
    • 0034704815 scopus 로고    scopus 로고
    • The Gcn5 bromodomain co-ordinates nucleosome remodeling
    • Syntichaki, P., Topalidou, I., and Thireos, G. (2000) The Gcn5 bromodomain co-ordinates nucleosome remodeling. Nature 404, 414-417.
    • (2000) Nature , vol.404 , pp. 414-417
    • Syntichaki, P.1    Topalidou, I.2    Thireos, G.3
  • 38
    • 0018801554 scopus 로고
    • Studies of acetylation and deacetylation in high mobility group proteins. Identification of the sites of acetylation in HMG-1
    • Sterner, R., Vidali, G., and Allfrey, V. G. (1979) Studies of acetylation and deacetylation in high mobility group proteins. Identification of the sites of acetylation in HMG-1. J. Biol. Chem. 254, 11577-11583.
    • (1979) J. Biol. Chem , vol.254 , pp. 11577-11583
    • Sterner, R.1    Vidali, G.2    Allfrey, V.G.3
  • 40
    • 0037295617 scopus 로고    scopus 로고
    • Priming the nucleosome: A role for HMGB proteins?
    • 4
    • Travers, A. (2003) Priming the nucleosome: A role for HMGB proteins? EMBO Rep. 4, 131-136.
    • (2003) EMBO Rep , pp. 131-136
    • Travers, A.1
  • 41
    • 0035325163 scopus 로고    scopus 로고
    • Histone acetylation and chromatin remodeling
    • Gregory, P. D., Wagner, K., and Horz, W. (2001) Histone acetylation and chromatin remodeling. Exp. Cell Res. 265, 195-202.
    • (2001) Exp. Cell Res , vol.265 , pp. 195-202
    • Gregory, P.D.1    Wagner, K.2    Horz, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.