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Volumn 1, Issue 11, 2010, Pages 967-971

Dynamics of the higher-order structure of chromatin

Author keywords

chromatin; dynamics; higher order structure; transcriptional regulation

Indexed keywords

HETEROCHROMATIN PROTEIN 1; HISTONE H1; HISTONE H3; HISTONE H4; MAGNESIUM ION; POLYCOMB GROUP PROTEIN;

EID: 79952610998     PISSN: 1674800X     EISSN: 16748018     Source Type: Journal    
DOI: 10.1007/s13238-010-0130-y     Document Type: Article
Times cited : (14)

References (29)
  • 3
    • 33748483266 scopus 로고    scopus 로고
    • Trinucleosome compaction studied by fluorescence energy transfer and scanning force microscopy
    • Bussiek, M., Tóth, K., Schwarz, N., and Langowski, J. (2006). Trinucleosome compaction studied by fluorescence energy transfer and scanning force microscopy. Biochemistry 45, 10838-10846.
    • (2006) Biochemistry , vol.45 , pp. 10838-10846
    • Bussiek, M.1    Tóth, K.2    Schwarz, N.3    Langowski, J.4
  • 4
    • 33745020770 scopus 로고    scopus 로고
    • Determinants of histone H1 mobility and chromatin binding in living cells
    • Catez, F., Ueda, T., and Bustin, M. (2006). Determinants of histone H1 mobility and chromatin binding in living cells. Nat Struct Mol Biol 13, 305-310.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 305-310
    • Catez, F.1    Ueda, T.2    Bustin, M.3
  • 5
    • 9444297879 scopus 로고    scopus 로고
    • Nucleosome arrays reveal the two-start organization of the chromatin fiber
    • Dorigo, B., Schalch, T., Kulangara, A., Duda, S., Schroeder, R. R., and Richmond, T. J. (2004). Nucleosome arrays reveal the two-start organization of the chromatin fiber. Science 306, 1571-1573.
    • (2004) Science , vol.306 , pp. 1571-1573
    • Dorigo, B.1    Schalch, T.2    Kulangara, A.3    Duda, S.4    Schroeder, R.R.5    Richmond, T.J.6
  • 6
    • 58149401194 scopus 로고    scopus 로고
    • Analysis of cryo-electron microscopy images does not support the existence of 30-nm chromatin fibers in mitotic chromosomes in situ
    • Eltsov, M., Maclellan, K. M., Maeshima, K., Frangakis, A. S., and Dubochet, J. (2008). Analysis of cryo-electron microscopy images does not support the existence of 30-nm chromatin fibers in mitotic chromosomes in situ. Proc Natl Acad Sci U S A 105, 19732-19737.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 19732-19737
    • Eltsov, M.1    Maclellan, K.M.2    Maeshima, K.3    Frangakis, A.S.4    Dubochet, J.5
  • 7
    • 8844281536 scopus 로고    scopus 로고
    • H2A.Z alters the nucleosome surface to promote HP1alphamediated chromatin fiber folding
    • Fan, J. Y., Rangasamy, D., Luger, K., and Tremethick, D. J. (2004). H2A. Z alters the nucleosome surface to promote HP1alphamediated chromatin fiber folding. Mol Cell 16, 655-666.
    • (2004) Mol Cell , vol.16 , pp. 655-666
    • Fan, J.Y.1    Rangasamy, D.2    Luger, K.3    Tremethick, D.J.4
  • 8
    • 9444244427 scopus 로고    scopus 로고
    • Chromatin compaction by a polycomb group protein complex
    • Francis, N. J., Kingston, R. E., and Woodcock, C. L. (2004). Chromatin compaction by a polycomb group protein complex. Science 306, 1574-1577.
    • (2004) Science , vol.306 , pp. 1574-1577
    • Francis, N.J.1    Kingston, R.E.2    Woodcock, C.L.3
  • 10
    • 2442574861 scopus 로고    scopus 로고
    • The C-terminal domain is the primary determinant of histone H1 binding to chromatin in vivo
    • Hendzel, M. J., Lever, M. A., Crawford, E., and Th'ng, J. P. (2004). The C-terminal domain is the primary determinant of histone H1 binding to chromatin in vivo. J Biol Chem 279, 20028-20034.
    • (2004) J Biol Chem , vol.279 , pp. 20028-20034
    • Hendzel, M.J.1    Lever, M.A.2    Crawford, E.3    Th'Ng, J.P.4
  • 11
    • 35948933368 scopus 로고    scopus 로고
    • Single-pair FRET microscopy reveals mononucleosome dynamics
    • Koopmans, W. J., Brehm, A., Logie, C., Schmidt, T., and van Noort, J. (2007). Single-pair FRET microscopy reveals mononucleosome dynamics. J Fluoresc 17, 785-795.
    • (2007) J Fluoresc , vol.17 , pp. 785-795
    • Koopmans, W.J.1    Brehm, A.2    Logie, C.3    Schmidt, T.4    van Noort, J.5
  • 12
    • 77950342430 scopus 로고    scopus 로고
    • Highly compacted chromatin formed in vitro reflects the dynamics of transcription activation in vivo
    • Li, G., Margueron, R., Hu, G., Stokes, D., Wang, Y. H., and Reinberg, D. (2010). Highly compacted chromatin formed in vitro reflects the dynamics of transcription activation in vivo. Mol Cell 38, 41-53.
    • (2010) Mol Cell , vol.38 , pp. 41-53
    • Li, G.1    Margueron, R.2    Hu, G.3    Stokes, D.4    Wang, Y.H.5    Reinberg, D.6
  • 13
    • 73349095064 scopus 로고    scopus 로고
    • Quantitative analysis of chromatin compaction in living cells using FLIM-FRET
    • Llères, D., James, J., Swift, S., Norman, D. G., and Lamond, A. I. (2009). Quantitative analysis of chromatin compaction in living cells using FLIM-FRET. J Cell Biol 187, 481-496.
    • (2009) J Cell Biol , vol.187 , pp. 481-496
    • Llères, D.1    James, J.2    Swift, S.3    Norman, D.G.4    Lamond, A.I.5
  • 14
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • Luger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F., and Richmond, T. J. (1997). Crystal structure of the nucleosome core particle at 2. 8 A resolution. Nature 389, 251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mäder, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 16
    • 69949132193 scopus 로고    scopus 로고
    • Dynamics and function of compact nucleosome arrays
    • Poirier, M. G., Oh, E., Tims, H. S., and Widom, J. (2009). Dynamics and function of compact nucleosome arrays. Nat Struct Mol Biol 16, 938-944.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 938-944
    • Poirier, M.G.1    Oh, E.2    Tims, H.S.3    Widom, J.4
  • 17
    • 33646242052 scopus 로고    scopus 로고
    • EM measurements define the dimensions of the "30-nm" chromatin fiber: evidence for a compact, interdigitated structure
    • Robinson, P. J., Fairall, L., Huynh, V. A., and Rhodes, D. (2006). EM measurements define the dimensions of the "30-nm" chromatin fiber: evidence for a compact, interdigitated structure. Proc Natl Acad Sci U S A 103, 6506-6511.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 6506-6511
    • Robinson, P.J.1    Fairall, L.2    Huynh, V.A.3    Rhodes, D.4
  • 18
    • 33744831161 scopus 로고    scopus 로고
    • Structure of the '30 nm' chromatin fibre: a key role for the linker histone
    • Robinson, P. J., and Rhodes, D. (2006). Structure of the '30 nm' chromatin fibre: a key role for the linker histone. Curr Opin Struct Biol 16, 336-343.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 336-343
    • Robinson, P.J.1    Rhodes, D.2
  • 19
    • 48249103503 scopus 로고    scopus 로고
    • Nucleosome repeat length and linker histone stoichiometry determine chromatin fiber structure
    • Routh, A., Sandin, S., and Rhodes, D. (2008). Nucleosome repeat length and linker histone stoichiometry determine chromatin fiber structure. Proc Natl Acad Sci U S A 105, 8872-8877.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 8872-8877
    • Routh, A.1    Sandin, S.2    Rhodes, D.3
  • 20
    • 21844436803 scopus 로고    scopus 로고
    • X-ray structure of a tetranucleosome and its implications for the chromatin fibre
    • Schalch, T., Duda, S., Sargent, D. F., and Richmond, T. J. (2005). X-ray structure of a tetranucleosome and its implications for the chromatin fibre. Nature 436, 138-141.
    • (2005) Nature , vol.436 , pp. 138-141
    • Schalch, T.1    Duda, S.2    Sargent, D.F.3    Richmond, T.J.4
  • 21
    • 32444434989 scopus 로고    scopus 로고
    • Histone H4-K16 acetylation controls chromatin structure and protein interactions
    • Shogren-Knaak, M., Ishii, H., Sun, J. M., Pazin, M. J., Davie, J. R., and Peterson, C. L. (2006). Histone H4-K16 acetylation controls chromatin structure and protein interactions. Science 311, 844-847.
    • (2006) Science , vol.311 , pp. 844-847
    • Shogren-Knaak, M.1    Ishii, H.2    Sun, J.M.3    Pazin, M.J.4    Davie, J.R.5    Peterson, C.L.6
  • 22
    • 0035842899 scopus 로고    scopus 로고
    • Cationchromatin binding as shown by ion microscopy is essential for the structural integrity of chromosomes
    • Strick, R., Strissel, P. L., Gavrilov, K., and Levi-Setti, R. (2001). Cationchromatin binding as shown by ion microscopy is essential for the structural integrity of chromosomes. J Cell Biol 155, 899-910.
    • (2001) J Cell Biol , vol.155 , pp. 899-910
    • Strick, R.1    Strissel, P.L.2    Gavrilov, K.3    Levi-Setti, R.4
  • 23
    • 0018581187 scopus 로고
    • Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin
    • Thoma, F., Koller, T., and Klug, A. (1979). Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin. J Cell Biol 83, 403-427.
    • (1979) J Cell Biol , vol.83 , pp. 403-427
    • Thoma, F.1    Koller, T.2    Klug, A.3
  • 26
    • 0022273023 scopus 로고
    • Structure of the 300A chromatin filament: X-ray diffraction from oriented samples
    • Widom, J., and Klug, A. (1985). Structure of the 300A chromatin filament: X-ray diffraction from oriented samples. Cell 43, 207-213.
    • (1985) Cell , vol.43 , pp. 207-213
    • Widom, J.1    Klug, A.2
  • 27
    • 0022650876 scopus 로고
    • Chromatin fibers are left-handed double helices with diameter and mass per unit length that depend on linker length
    • Williams, S. P., Athey, B. D., Muglia, L. J., Schappe, R. S., Gough, A. H., and Langmore, J. P. (1986). Chromatin fibers are left-handed double helices with diameter and mass per unit length that depend on linker length. Biophys J 49, 233-248.
    • (1986) Biophys J , vol.49 , pp. 233-248
    • Williams, S.P.1    Athey, B.D.2    Muglia, L.J.3    Schappe, R.S.4    Gough, A.H.5    Langmore, J.P.6
  • 28
    • 0021250785 scopus 로고
    • The higherorder structure of chromatin: evidence for a helical ribbon arrangement
    • Woodcock, C. L., Frado, L. L., and Rattner, J. B. (1984). The higherorder structure of chromatin: evidence for a helical ribbon arrangement. J Cell Biol 99, 42-52.
    • (1984) J Cell Biol , vol.99 , pp. 42-52
    • Woodcock, C.L.1    Frado, L.L.2    Rattner, J.B.3
  • 29
    • 0033813699 scopus 로고    scopus 로고
    • Linker histone binding and displacement: versatile mechanism for transcriptional regulation
    • Zlatanova, J., Caiafa, P., and van Holde, K. (2000). Linker histone binding and displacement: versatile mechanism for transcriptional regulation. FASEB J 14, 1697-1704.
    • (2000) FASEB J , vol.14 , pp. 1697-1704
    • Zlatanova, J.1    Caiafa, P.2    van Holde, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.