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Volumn 43, Issue 16, 2004, Pages 4773-4780

Role of Histone Tails in the Conformation and Interactions of Nucleosome Core Particles

Author keywords

[No Author keywords available]

Indexed keywords

ANGLE MEASUREMENT; CONCENTRATION (PROCESS); CONFORMATIONS; ELEMENTARY PARTICLES; SODIUM CHLORIDE; X RAY SCATTERING;

EID: 1942502793     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi036210g     Document Type: Article
Times cited : (75)

References (32)
  • 1
    • 0037385490 scopus 로고    scopus 로고
    • Structures and interactions of the core histone tail domains
    • Zheng, C., and Hayes, J. J. (2003) Structures and interactions of the core histone tail domains. Biopolymers 68, 539-546.
    • (2003) Biopolymers , vol.68 , pp. 539-546
    • Zheng, C.1    Hayes, J.J.2
  • 2
    • 0029882454 scopus 로고    scopus 로고
    • Reversible oligonucleosome self-association: Dependence on divalent cations and core histone tail domains
    • Schwarz, P. M., Felthauser, A., Fletcher, T. M., and Hansen, J. C. (1996) Reversible oligonucleosome self-association: dependence on divalent cations and core histone tail domains. Biochemistry 35, 4009-4015.
    • (1996) Biochemistry , vol.35 , pp. 4009-4015
    • Schwarz, P.M.1    Felthauser, A.2    Fletcher, T.M.3    Hansen, J.C.4
  • 3
    • 0031831516 scopus 로고    scopus 로고
    • Structure, dynamics, and function of chromatin in vitro
    • Widom, J. (1998) Structure, dynamics, and function of chromatin in vitro. Annu. Rev. Biophys. Biomol. Struct. 27, 285-327.
    • (1998) Annu. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 285-327
    • Widom, J.1
  • 4
    • 0035918170 scopus 로고    scopus 로고
    • Effects of histone acetylation on the solubility and folding of the chromatin fiber
    • Wang, X., He, C., Moore, S. C., and Ausio, J. (2001) Effects of histone acetylation on the solubility and folding of the chromatin fiber. J. Biol. Chem. 276, 12764-12768.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12764-12768
    • Wang, X.1    He, C.2    Moore, S.C.3    Ausio, J.4
  • 5
    • 0018148648 scopus 로고
    • High-resolution proton-magnetic-resonance studies of chromatin core particles
    • Cary, P., Moss, T., and Bradbury, M. (1978) High-resolution proton-magnetic-resonance studies of chromatin core particles. Eur. J. Biochem. 89, 475-482.
    • (1978) Eur. J. Biochem. , vol.89 , pp. 475-482
    • Cary, P.1    Moss, T.2    Bradbury, M.3
  • 6
    • 0021750061 scopus 로고
    • Differential dissociation of histone tails from core chromatin
    • Walker, I. O. (1984) Differential dissociation of histone tails from core chromatin. Biochemistry 23, 5622-5628.
    • (1984) Biochemistry , vol.23 , pp. 5622-5628
    • Walker, I.O.1
  • 7
    • 0022982049 scopus 로고
    • Natural abundance carbon-13 nuclear magnetic resonance studies of histone and DNA dynamics in nucleosome cores
    • Hilliard, P. R., Smith, R. M., and Rill, R. L. (1986) Natural abundance carbon-13 nuclear magnetic resonance studies of histone and DNA dynamics in nucleosome cores. J. Biol. Chem. 261, 5992-5998.
    • (1986) J. Biol. Chem. , vol.261 , pp. 5992-5998
    • Hilliard, P.R.1    Smith, R.M.2    Rill, R.L.3
  • 8
    • 0024338215 scopus 로고
    • Mobile histone tails in nucleosomes
    • Smith, R. M., and Rill, R. L. (1989) Mobile histone tails in nucleosomes. J. Biol. Chem. 264, 10574-10581.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10574-10581
    • Smith, R.M.1    Rill, R.L.2
  • 9
    • 0036221883 scopus 로고    scopus 로고
    • Salt-induced conformation and interaction changes of nucleosome core particles
    • Mangenot, S., Leforestier, A., Vachette, P., Durand, D., and 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
  • 10
    • 0036525256 scopus 로고    scopus 로고
    • Interactions between isolated nucleosome core particles: A tail-bridging effect?
    • Mangenot, S., Raspaud, E., Tribet, C., Belloni, L., and Livolant, F. (2002) Interactions between isolated nucleosome core particles: A tail-bridging effect? Eur. Phys. J. E 7, 221-231.
    • (2002) Eur. Phys. J. E , vol.7 , pp. 221-231
    • Mangenot, S.1    Raspaud, E.2    Tribet, C.3    Belloni, L.4    Livolant, F.5
  • 11
    • 0037778650 scopus 로고    scopus 로고
    • Two-body polyelectrolyte-mediated bridging interactions
    • Podgornik, R. (2003) Two-body polyelectrolyte-mediated bridging interactions. J. Chem. Phys. 118, 11286-11296.
    • (2003) J. Chem. Phys. , vol.118 , pp. 11286-11296
    • Podgornik, R.1
  • 12
    • 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
  • 13
    • 0019620604 scopus 로고
    • Proteolytic digestion studies of chromatin core-histone structure. Identification of the limit peptides of histones H3 and H4
    • Bohm, L., Briand, G., Sautiere, P., and Crane-Robinson, C. (1981) Proteolytic digestion studies of chromatin core-histone structure. Identification of the limit peptides of histones H3 and H4. Eur. J. Biochem. 119, 67-74.
    • (1981) Eur. J. Biochem. , vol.119 , pp. 67-74
    • Bohm, L.1    Briand, G.2    Sautiere, P.3    Crane-Robinson, C.4
  • 14
    • 0021266689 scopus 로고
    • Proteases as structural probes for chromatin: The domain structure of histones
    • Bohm, L., and Crane-Robinson, C. (1984) Proteases as structural probes for chromatin: the domain structure of histones. Biosci. Rep. 4, 365-386.
    • (1984) Biosci. Rep. , vol.4 , pp. 365-386
    • Bohm, L.1    Crane-Robinson, C.2
  • 15
    • 0019017430 scopus 로고
    • Proteolytic digestion studies of chromatin core-histone structure. Identification of a limit peptide of histone H2A
    • Bohm, L., Crane-Robinson, C., and Sautiere, P. (1980) Proteolytic digestion studies of chromatin core-histone structure. Identification of a limit peptide of histone H2A. Eur. J. Biochem. 106, 525-530.
    • (1980) Eur. J. Biochem. , vol.106 , pp. 525-530
    • Bohm, L.1    Crane-Robinson, C.2    Sautiere, P.3
  • 16
    • 0025712580 scopus 로고
    • Silver staining of proteins and DNA
    • Merril, C. R. (1990) Silver staining of proteins and DNA. Nature 343, 779-780.
    • (1990) Nature , vol.343 , pp. 779-780
    • Merril, C.R.1
  • 18
    • 0029185933 scopus 로고
    • CRYSOL: A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun, D. I., Barberato, C., and Koch, M. H. J. (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.I.1    Barberato, C.2    Koch, M.H.J.3
  • 22
    • 0026782131 scopus 로고
    • Role of the histone "tails" in the folding of oligonucleosomes depleted of histone H1
    • Garcia-Ramirez, M., Dong, F., and 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
  • 23
    • 0025873957 scopus 로고
    • Influence of DNA topology and histone tails in nucleosome organization on pBR322 DNA
    • Buttinelli, M., Leoni, L., Sampaolese, B., and Savino, M. (1991) Influence of DNA topology and histone tails in nucleosome organization on pBR322 DNA. Nucleic Acid Res. 19, 4543-4549.
    • (1991) Nucleic Acid Res. , vol.19 , pp. 4543-4549
    • Buttinelli, M.1    Leoni, L.2    Sampaolese, B.3    Savino, M.4
  • 24
    • 0034603742 scopus 로고    scopus 로고
    • DNA sequence-dependent contributions of core histone tails to nucleosome stability: Differential effects of acetylation and proteolytic tail removal
    • Widlund, H. R., Vitolo, J. M., Thiriet, C., and Hayes, J. J. (2000) DNA sequence-dependent contributions of core histone tails to nucleosome stability: differential effects of acetylation and proteolytic tail removal. Biochemistry 39, 3835-3841.
    • (2000) Biochemistry , vol.39 , pp. 3835-3841
    • Widlund, H.R.1    Vitolo, J.M.2    Thiriet, C.3    Hayes, J.J.4
  • 25
    • 0028858566 scopus 로고
    • Core histone tail domains mediate oligonucleosome folding and nucleosomal DNA organization through distinct molecular mechanisms
    • Fletcher, T. M., and Hansen, J. C. (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
  • 26
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger, K., Mader, A. W., Richmond, R. K., Sargent, D. F., and Richmond, T. J. (1997) Crystal structure of the nucleosome core particle at 2.8 Å 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
  • 27
    • 0022551060 scopus 로고
    • Histone hyperacetylation: Its effects on nucleosome conformation and stability
    • Ausio, J., and van Holde, K. E. (1986) Histone hyperacetylation: its effects on nucleosome conformation and stability. Biochemistry 25, 1421-1428.
    • (1986) Biochemistry , vol.25 , pp. 1421-1428
    • Ausio, J.1    Van Holde, K.E.2
  • 29
    • 0026010309 scopus 로고
    • Histone contributions to the structure of DNA in the nucleosome
    • Hayes, J. J., Clark, D. J., and Wolffe, A. P. (1991) Histone contributions to the structure of DNA in the nucleosome. Proc. Natl. Acad. Sci. U.S.A. 88, 6829-6833.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 6829-6833
    • Hayes, J.J.1    Clark, D.J.2    Wolffe, A.P.3
  • 30
    • 0031587289 scopus 로고    scopus 로고
    • Characterization of nucleosome core particles containing histone proteins made in bacteria
    • Luger, K., Rechsteiner, T. J., Flaus, A. J., Waye, M. M., and Richmond, T. J. (1997) 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.4    Richmond, T.J.5
  • 31
    • 0034724562 scopus 로고    scopus 로고
    • Effects of core histone tail domains on the equilibrium constants for dynamic DNA site accessibility in nucleosomes
    • Polach, K. J., Lowary, P. T., and Widom, J. (2000) Effects of core histone tail domains on the equilibrium constants for dynamic DNA site accessibility in nucleosomes. J. Mol. Biol. 298, 211-223.
    • (2000) J. Mol. Biol. , vol.298 , pp. 211-223
    • Polach, K.J.1    Lowary, P.T.2    Widom, J.3
  • 32
    • 0024537375 scopus 로고
    • Salt-induced release of DNA from nucleosome core particles
    • Yager, T. D., McMurray, C. T., and van Holde, K. E. (1989) Salt-induced release of DNA from nucleosome core particles. Biochemistry 28, 2271-2281.
    • (1989) Biochemistry , vol.28 , pp. 2271-2281
    • Yager, T.D.1    McMurray, C.T.2    Van Holde, K.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.