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Volumn 36, Issue 8, 2007, Pages 1083-1094

H2A and H2B tails are essential to properly reconstitute nucleosome core particles

Author keywords

Chromatin; Histone tails; Nucleosome; SAXS

Indexed keywords

DNA; HISTONE; NUCLEASE; POLYACRYLAMIDE GEL;

EID: 35748982118     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-007-0212-9     Document Type: Article
Times cited : (22)

References (41)
  • 1
    • 0024573304 scopus 로고
    • Use of selectively trypsinized nucleosome core particles to analyse the role of histone tails in the stabilisation of the nucleosome
    • Ausio J, van Holde KV (1989) Use of selectively trypsinized nucleosome core particles to analyse the role of histone tails in the stabilisation of the nucleosome. J Mol Biol 206:451-463
    • (1989) J Mol Biol , vol.206 , pp. 451-463
    • Ausio, J.1    Van Holde, K.V.2
  • 2
    • 1942502793 scopus 로고    scopus 로고
    • Role of histone tails in the conformation and interactions of nucleosome core particles
    • Bertin A, Leforestier A, Durand D, Livolant F (2004) Role of histone tails in the conformation and interactions of nucleosome core particles. Biochemistry 43:4773-4780
    • (2004) Biochemistry , vol.43 , pp. 4773-4780
    • Bertin, A.1    Leforestier, A.2    Durand, D.3    Livolant, F.4
  • 3
    • 34047232501 scopus 로고    scopus 로고
    • H3 and H4 histone tails play a central role in the interactions of recombinant NCPs.
    • Bertin A, Renouard M, Pedersen JS, Livolant F, Durand D (2007) H3 and H4 histone tails play a central role in the interactions of recombinant NCPs. Biophys J 92:2633-2645
    • (2007) Biophys J , vol.92 , pp. 2633-2645
    • Bertin, A.1    Renouard, M.2    Pedersen, J.S.3    Livolant, F.4    Durand, D.5
  • 4
    • 12344284012 scopus 로고    scopus 로고
    • Specific Contributions of histone tails and their acetylation to the mechanical stability of nucleosomes
    • Brower-Toland B, Wacker DA, Fulbright RM, Lis JT, Kraus WL, Wang MD (2005) Specific Contributions of histone tails and their acetylation to the mechanical stability of nucleosomes. J Mol Biol 346:135-146
    • (2005) J Mol Biol , vol.346 , pp. 135-146
    • Brower-Toland, B.1    Wacker, D.A.2    Fulbright, R.M.3    Lis, J.T.4    Kraus, W.L.5    Wang, M.D.6
  • 9
    • 0036307707 scopus 로고    scopus 로고
    • Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 a resolution
    • Davey CA, Sargent DF, Luger K, Maeder AW, Richmond TJ (2002) Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 A resolution. J Mol Biol 319:1097-1113
    • (2002) J Mol Biol , vol.319 , pp. 1097-1113
    • Davey, C.A.1    Sargent, D.F.2    Luger, K.3    Maeder, A.W.4    Richmond, T.J.5
  • 10
    • 0025667179 scopus 로고
    • Analysis of the changes in the structure and hydration of the nucleosome core particle at moderate ionic strengths
    • Dong F, Nelson C, Ausio J (1990) Analysis of the changes in the structure and hydration of the nucleosome core particle at moderate ionic strengths. Biochemistry 29:10710-10716
    • (1990) Biochemistry , vol.29 , pp. 10710-10716
    • Dong, F.1    Nelson, C.2    Ausio, J.3
  • 11
    • 0037436410 scopus 로고    scopus 로고
    • Chromatin fiber folding: Requirement for the histone H4 N-terminal tail
    • Dorigo B, Schalch T, Bystricky K, Richmond T (2003) Chromatin fiber folding: requirement for the histone H4 N-terminal tail. J Mol Biol 327:85-96
    • (2003) J Mol Biol , vol.327 , pp. 85-96
    • Dorigo, B.1    Schalch, T.2    Bystricky, K.3    Richmond, T.4
  • 14
    • 0024268331 scopus 로고
    • H2a-specific proteolysis as a unique probe in the analysis of the histone octamer
    • Eickbush TH, Godfrey JE, Elia MC, Moudrianakis EN (1988) H2a-specific proteolysis as a unique probe in the analysis of the histone octamer. J Biol Chem 263:18972-18978
    • (1988) J Biol Chem , vol.263 , pp. 18972-18978
    • Eickbush, T.H.1    Godfrey, J.E.2    Elia, M.C.3    Moudrianakis, E.N.4
  • 15
    • 0028858566 scopus 로고
    • Core histone tail domains mediate oligonucleosome folding and nucleosomal DNA organization through distinct molecular mechanisms
    • Fletcher TM, Hansen JC (1995) Core histone tail domains mediate oligonucleosome folding and nucleosomal DNA organization through distinct molecular mechanisms. J Biol Chem 270:25359-25362
    • (1995) J Biol Chem , vol.270 , pp. 25359-25362
    • Fletcher, T.M.1    Hansen, J.C.2
  • 16
    • 0026782131 scopus 로고
    • Role of the histone tails in the folding of oligonucleosomes depleted of histone H1
    • Garcia-Ramirez M, Dong F, Ausio J (1992) Role of the histone tails in the folding of oligonucleosomes depleted of histone H1. J Biol Chem 267:19587-19595
    • (1992) J Biol Chem , vol.267 , pp. 19587-19595
    • Garcia-Ramirez, M.1    Dong, F.2    Ausio, J.3
  • 17
    • 26644471508 scopus 로고    scopus 로고
    • The core histone N-terminal tail domains function independently and additively during salt-dependent oligomerization of nucleosomal arrays
    • Gordon F, Luger K, Hansen JC (2005) The core histone N-terminal tail domains function independently and additively during salt-dependent oligomerization of nucleosomal arrays. J Biol Chem 280:33701-33706
    • (2005) J Biol Chem , vol.280 , pp. 33701-33706
    • Gordon, F.1    Luger, K.2    Hansen, J.C.3
  • 18
    • 0035807901 scopus 로고    scopus 로고
    • Histone tails modulate nucleosome mobility and regulate ATP-dependent nucleosome sliding by NURF
    • Hamiche A, Kang JG, Dennis C, Xiao H, Wu C (2001) Histone tails modulate nucleosome mobility and regulate ATP-dependent nucleosome sliding by NURF. Proc Natl Acad Sci USA 98:14316-14321
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14316-14321
    • Hamiche, A.1    Kang, J.G.2    Dennis, C.3    Xiao, H.4    Wu, C.5
  • 19
    • 0035980285 scopus 로고    scopus 로고
    • Thermodynamic studies of the core histones: Stability of the octamer subunits is not altered by removal of their terminal domains
    • Karantza V, Freire E, Moudrianakis EN (2001) Thermodynamic studies of the core histones: stability of the octamer subunits is not altered by removal of their terminal domains. Biochemistry 40:13114-13123
    • (2001) Biochemistry , vol.40 , pp. 13114-13123
    • Karantza, V.1    Freire, E.2    Moudrianakis, E.N.3
  • 21
    • 0030008538 scopus 로고    scopus 로고
    • Modulation of the higher-order folding of chromatin by deletion of histone H3 and H4 terminal domains
    • Krajewski WA, Ausio J (1996) Modulation of the higher-order folding of chromatin by deletion of histone H3 and H4 terminal domains. Biochem J 316:395-400
    • (1996) Biochem J , vol.316 , pp. 395-400
    • Krajewski, W.A.1    Ausio, J.2
  • 22
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 angstrom resolution
    • Luger K, Mader AW, Richmond RK, Sargent DF, Richmond TJ (1997a) Crystal structure of the nucleosome core particle at 2.8 angstrom resolution. Nature 389:251-260
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 23
    • 0031587289 scopus 로고    scopus 로고
    • Characterization of nucleosome core particles containing histone proteins made in bacteria
    • Luger K, Rechsteiner TJ, Flaus AJ, Waye MMY, Richmond TJ (1997b) Characterization of nucleosome core particles containing histone proteins made in bacteria. J Mol Biol 272:301-311
    • (1997) J Mol Biol , vol.272 , pp. 301-311
    • Luger, K.1    Rechsteiner, T.J.2    Flaus, A.J.3    Waye, M.M.Y.4    Richmond, T.J.5
  • 24
    • 0036221883 scopus 로고    scopus 로고
    • Salt-induced conformation and interaction changes of nucleosome core particles
    • Mangenot S, Leforestier A, Vachette P, Durand D, Livolant F (2002) Salt-induced conformation and interaction changes of nucleosome core particles. Biophys J 82:345-356
    • (2002) Biophys J , vol.82 , pp. 345-356
    • Mangenot, S.1    Leforestier, A.2    Vachette, P.3    Durand, D.4    Livolant, F.5
  • 25
    • 0026642219 scopus 로고
    • Mobile nucleosomes: A general behavior
    • Meersseman G, Pennings S, Bradbury EM (1992) Mobile nucleosomes: a general behavior. EMBO J 11:2951-2959
    • (1992) EMBO J , vol.11 , pp. 2951-2959
    • Meersseman, G.1    Pennings, S.2    Bradbury, E.M.3
  • 26
    • 0016133106 scopus 로고
    • Internal structure of the chromatine subunit
    • Noll M (1974) Internal structure of the chromatine subunit. Nucleic Acids Res 1:1573-1578
    • (1974) Nucleic Acids Res , vol.1 , pp. 1573-1578
    • Noll, M.1
  • 27
    • 3442880149 scopus 로고    scopus 로고
    • A flux- and background-optimized version of the NanoSTAR small-angle X-ray scattering camera for solution scattering
    • Pedersen JS (2004) A flux- and background-optimized version of the NanoSTAR small-angle X-ray scattering camera for solution scattering. J Appl Crystallogr 37:369-380
    • (2004) J Appl Crystallogr , vol.37 , pp. 369-380
    • Pedersen, J.S.1
  • 28
    • 0025887821 scopus 로고
    • Mobility of positioned nucleosomes on 5-SRdna
    • Pennings S, Meersseman G, Bradbury EM (1991) Mobility of positioned nucleosomes on 5-SRdna. J Mol Biol 220:101-110
    • (1991) J Mol Biol , vol.220 , pp. 101-110
    • Pennings, S.1    Meersseman, G.2    Bradbury, E.M.3
  • 29
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • Petoukhov MV, Svergun DI (2005) Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophys J 89:1237-1250
    • (2005) Biophys J , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 30
    • 0037126691 scopus 로고    scopus 로고
    • The N-terminal tails of the H2A-H2B histones affect dimer structure and stability
    • Placek BJ, Gloss LM (2002) The N-terminal tails of the H2A-H2B histones affect dimer structure and stability. Biochemistry 41:14960-14968
    • (2002) Biochemistry , vol.41 , pp. 14960-14968
    • Placek, B.J.1    Gloss, L.M.2
  • 31
    • 0033569769 scopus 로고    scopus 로고
    • Functional Interaction between GCN5 and polyamines: A new role for core histone acetylation
    • Pollard K, Samuels ML, Crowley KA, Hansen JC, Peterson CL (1999) Functional Interaction between GCN5 and polyamines: a new role for core histone acetylation. EMBO J 18:5622-5633
    • (1999) EMBO J , vol.18 , pp. 5622-5633
    • Pollard, K.1    Samuels, M.L.2    Crowley, K.A.3    Hansen, J.C.4    Peterson, C.L.5
  • 32
    • 0034461003 scopus 로고    scopus 로고
    • Effects of histone tail domains on the rate of transcriptional elongation through a nucleosome
    • Protacio RU, Li G, Lowary PT, Widom J (2000) Effects of histone tail domains on the rate of transcriptional elongation through a nucleosome. Mol Cell Biol 20:8866-8878
    • (2000) Mol Cell Biol , vol.20 , pp. 8866-8878
    • Protacio, R.U.1    Li, G.2    Lowary, P.T.3    Widom, J.4
  • 33
    • 0023928212 scopus 로고
    • Crystal of a nucleosome core particle containing defined sequence DNA
    • Richmond TJ, Searles MA, Simpson RT (1988) Crystal of a nucleosome core particle containing defined sequence DNA. J Mol Biol 199:161-170
    • (1988) J Mol Biol , vol.199 , pp. 161-170
    • Richmond, T.J.1    Searles, M.A.2    Simpson, R.T.3
  • 34
    • 34247520870 scopus 로고    scopus 로고
    • Structural flexibility of the nucleosome core particle at atomic resolution studied by molecular dynamics simulation
    • Roccatano D, Barthel A, Zacharias M (2007) Structural flexibility of the nucleosome core particle at atomic resolution studied by molecular dynamics simulation. Biopolymers 85:407-421
    • (2007) Biopolymers , vol.85 , pp. 407-421
    • Roccatano, D.1    Barthel, A.2    Zacharias, M.3
  • 35
    • 0037423733 scopus 로고    scopus 로고
    • Sequence-dependent nucleosome structural and dynamic polymorphism. Potential involvement of histone H2BN-terminal tall proximal domain
    • Sivolob A, Lavelle C, Prunell A (2003) Sequence-dependent nucleosome structural and dynamic polymorphism. Potential involvement of histone H2BN-terminal tall proximal domain. J Mol Biol 326:49-63
    • (2003) J Mol Biol , vol.326 , pp. 49-63
    • Sivolob, A.1    Lavelle, C.2    Prunell, A.3
  • 36
    • 0024338215 scopus 로고
    • Mobile histone tails in nucleosomes. Assignments of mobile segments and investigations of their role in chromatin folding
    • Smith RM, Rill RL (1989) Mobile histone tails in nucleosomes. Assignments of mobile segments and investigations of their role in chromatin folding. J Biol Chem 264:10574-10581
    • (1989) J Biol Chem , vol.264 , pp. 10574-10581
    • Smith, R.M.1    Rill, R.L.2
  • 37
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun DI (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J Appl Crystallogr 25:495-503
    • (1992) J Appl Crystallogr , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 38
    • 0029185933 scopus 로고
    • CRYSOL: A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun D, Barberato C, Koch MHJ (1995) CRYSOL: a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J Appl Crystallogr 28:768-773
    • (1995) J Appl Crystallogr , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 39
    • 0030922941 scopus 로고    scopus 로고
    • Hybrid trypsinized nucleosomal arrays: Identification of multiple functional roles of the H2A/H2B and H3/H4 N-termini in chromatin fiber compaction
    • Tse C, Hansen JC (1997) Hybrid trypsinized nucleosomal arrays: identification of multiple functional roles of the H2A/H2B and H3/H4 N-termini in chromatin fiber compaction. Biochemistry 36:11381-11388
    • (1997) Biochemistry , vol.36 , pp. 11381-11388
    • Tse, C.1    Hansen, J.C.2
  • 40
    • 11144334742 scopus 로고    scopus 로고
    • The core histone N-terminal tail domains negatively regulate binding of transcription factor IIIA to a nucleosome containing a 5S RNA gene via a novel mechanism
    • Yang ZY, Zheng CY, Thiriet C, Hayes JJ (2005) The core histone N-terminal tail domains negatively regulate binding of transcription factor IIIA to a nucleosome containing a 5S RNA gene via a novel mechanism. Mol Cell Biol 25:241-249
    • (2005) Mol Cell Biol , vol.25 , pp. 241-249
    • Yang, Z.Y.1    Zheng, C.Y.2    Thiriet, C.3    Hayes, J.J.4
  • 41
    • 34247181137 scopus 로고    scopus 로고
    • The core histone tail domains contribute to sequence-dependent nucleosome positioning.
    • Yang Z, Zheng C, Hayes JJ (2007) The core histone tail domains contribute to sequence-dependent nucleosome positioning. J Biol Chem 282:7930-7938
    • (2007) J Biol Chem , vol.282 , pp. 7930-7938
    • Yang, Z.1    Zheng, C.2    Hayes, J.J.3


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