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Volumn 40, Issue 4, 2012, Pages 1475-1484

DNA and nucleosomes direct distinct folding of a linker histone H1 C-terminal domain

Author keywords

[No Author keywords available]

Indexed keywords

DNA; DNA FRAGMENT; HISTONE H1; HYDROGEN; NAKED DNA;

EID: 84857876439     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkr866     Document Type: Article
Times cited : (62)

References (39)
  • 1
    • 0019888694 scopus 로고
    • Histones H1 and H5: One or two molecules per nucleosomë
    • Bates, D. L. and Thomas, J. O. (1981) Histones H1 and H5: one or two molecules per nucleosomëNucleic Acids Res., 2, 5883-5894.
    • (1981) Nucleic Acids Res. , vol.2 , pp. 5883-5894
    • Bates, D.L.1    Thomas, J.O.2
  • 2
    • 0019157001 scopus 로고
    • The structure of histone H1 and its location in chromatin
    • DOI 10.1038/288675a0
    • Allan, J., Hartman, P. G., Crane-Robinson, C. and Aviles, F. X. (1980) The structure of histone H1 and its location in chromatin. Nature, 288, 675-679. (Pubitemid 11168522)
    • (1980) Nature , vol.288 , Issue.5792 , pp. 675-679
    • Allan, J.1    Hartman, P.G.2    Crane-Robinson, C.3    Aviles, F.X.4
  • 3
    • 0018866555 scopus 로고
    • Points of contact between histone H1 and the histone octamer
    • Boulikas, T., Wiseman, J. M. and Garrard, W. T. (1980) Points of contact between histone H1 and the histone octamer. Proc. Natl Acad. Sci. USA, 77, 127-131.
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 127-131
    • Boulikas, T.1    Wiseman, J.M.2    Garrard, W.T.3
  • 4
    • 0003903126 scopus 로고
    • Springer Verlag New York
    • van Holde, K. E. (1989) Chromatin. Springer Verlag, New York.
    • (1989) Chromatin
    • Van Holde, K.E.1
  • 5
    • 0030576509 scopus 로고    scopus 로고
    • Linker histone H1 regulates specific gene expression but not global transcription in vivo
    • DOI 10.1016/S0092-8674(00)80120-8
    • Shen, X. and Gorovsky, M. A. (1996) Linker histone H1 regulates specific gene expression but not global transcription in vivo. Cell, 86, 475-483. (Pubitemid 26272087)
    • (1996) Cell , vol.86 , Issue.3 , pp. 475-483
    • Shen, X.1    Gorovsky, M.A.2
  • 6
    • 79955041234 scopus 로고    scopus 로고
    • Structure of the H1 C-terminal domain and function in chromatin condensation
    • Caterino, T. L. and Hayes, J. J. (2011) Structure of the H1 C-terminal domain and function in chromatin condensation. Biochem. Cell Biol., 89, 35-44.
    • (2011) Biochem. Cell Biol. , vol.89 , pp. 35-44
    • Caterino, T.L.1    Hayes, J.J.2
  • 7
    • 58549094957 scopus 로고    scopus 로고
    • Chromatin condensing functions of the linker histone C-terminal domain are mediated by specific amino acid composition and intrinsic protein disorder
    • Lu, X., Hamkalo, B., Parseghian, M. H. and Hansen, J. C. (2009) Chromatin condensing functions of the linker histone C-terminal domain are mediated by specific amino acid composition and intrinsic protein disorder. Biochemistry, 48, 164-172.
    • (2009) Biochemistry , vol.48 , pp. 164-172
    • Lu, X.1    Hamkalo, B.2    Parseghian, M.H.3    Hansen, J.C.4
  • 8
    • 79958068470 scopus 로고    scopus 로고
    • Nucleosome linker DNA contacts and induces specific folding of the intrinsically disordered h1 carboxyl-terminal domain
    • Caterino, T. L., Fang, H. and Hayes, J. J. (2011) Nucleosome linker DNA contacts and induces specific folding of the intrinsically disordered h1 carboxyl-terminal domain. Mol. Cell. Biol., 31, 2341-2348.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 2341-2348
    • Caterino, T.L.1    Fang, H.2    Hayes, J.J.3
  • 9
    • 25444523218 scopus 로고    scopus 로고
    • DNA-induced secondary structure of the carboxyl-terminal domain of histone H1
    • DOI 10.1074/jbc.M505636200
    • Roque, A., Iloro, I., Ponte, I., Arrondo, J. L. and Suau, P. (2005) DNA-induced secondary structure of the carboxyl-terminal domain of histone H1. J. Biol. Chem., 280, 32141-32147. (Pubitemid 41361820)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.37 , pp. 32141-32147
    • Roque, A.1    Iloro, I.2    Ponte, I.3    Arrondo, J.L.R.4    Suau, P.5
  • 10
    • 23044489675 scopus 로고    scopus 로고
    • H1 family histones in the nucleus: Control of binding and localization by the C-terminal domain
    • DOI 10.1074/jbc.M501627200
    • Th'ng, J. P., Sung, R., Ye, M. and Hendzel, M. J. (2005) H1 family histones in the nucleus. Control of binding and localization by the C-terminal domain. J. Biol. Chem., 280, 27809-27814. (Pubitemid 41076896)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.30 , pp. 27809-27814
    • Th'ng, J.P.H.1    Sung, R.2    Ye, M.3    Hendzel, M.J.4
  • 11
    • 0027284143 scopus 로고
    • An NMR study on the DNA-binding SPKK motif and a model for its interaction with DNA
    • Suzuki, M., Gerstein, M. and Johnson, T. (1993) An NMR study on the DNA-binding SPKK motif and a model for its interaction with DNA. Protein Eng., 6, 565-574. (Pubitemid 23246507)
    • (1993) Protein Engineering , vol.6 , Issue.6 , pp. 565-574
    • Suzuki, M.1    Gerstein, M.2    Johnson, T.3
  • 12
    • 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. (Pubitemid 14076152)
    • (1984) Bioscience Reports , vol.4 , Issue.5 , pp. 365-386
    • Bohm, L.1    Crane-Robinson, C.2
  • 13
    • 0017128574 scopus 로고
    • Studies on the role and mode of operation of the very-lysine-rich histones in eukaryote chromatin. Nuclear-magnetic-resonance studies on nucleoprotein and histone phi 1-DNA complexes from marine invertebrate sperm
    • Puigdomenech, P., Martinez, P., Palau, J., Bradbury, E. M. and Crane-Robinson, C. (1976) Studies on the role and mode of operation of the very-lysine-rich histones in eukaryote chromatin. Nuclear-magnetic-resonance studies on nucleoprotein and histone phi 1-DNA complexes from marine invertebrate sperm. Eur. J. Biochem., 65, 357-363.
    • (1976) Eur. J. Biochem. , vol.65 , pp. 357-363
    • Puigdomenech, P.1    Martinez, P.2    Palau, J.3    Bradbury, E.M.4    Crane-Robinson, C.5
  • 14
    • 0023711642 scopus 로고
    • Alpha-helix in the carboxy-terminal domains of histones H1 and H5
    • Clark, D. J., Hill, C. S., Martin, S. R. and Thomas, J. O. (1988) Alpha-helix in the carboxy-terminal domains of histones H1 and H5. EMBO J., 7, 69-75.
    • (1988) EMBO J. , vol.7 , pp. 69-75
    • Clark, D.J.1    Hill, C.S.2    Martin, S.R.3    Thomas, J.O.4
  • 15
    • 33644865137 scopus 로고    scopus 로고
    • Intrinsic protein disorder, amino acid composition, and histone terminal domains
    • DOI 10.1074/jbc.R500022200
    • Hansen, J. C., Lu, X., Ross, E. D. and Woody, R. W. (2006) Intrinsic protein disorder, amino acid composition, and histone terminal domains. J. Biol. Chem., 281, 1853-1856. (Pubitemid 43845769)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.4 , pp. 1853-1856
    • Hansen, J.C.1    Lu, X.2    Ross, E.D.3    Woody, R.W.4
  • 16
    • 33746845357 scopus 로고    scopus 로고
    • Localization of linker histone in chromatosomes by cryo-atomic force microscopy
    • DOI 10.1529/biophysj.106.090423
    • Sheng, S., Czajkowsky, D. M. and Shao, Z. (2006) Localization of linker histone in chromatosomes by cryo-atomic force microscopy. Biophys. J., 91, L35-L37. (Pubitemid 44174236)
    • (2006) Biophysical Journal , vol.91 , Issue.4
    • Sheng, S.1    Czajkowsky, D.M.2    Shao, Z.3
  • 18
    • 0029151148 scopus 로고
    • DNA at the entry-exit of the nucleosome observed by cryoelectron microscopy
    • Furrer, P., Bednar, J., Dubochet, J., Hamiche, A. and Prunell, A. (1995) DNA at the entry-exit of the nucleosome observed by cryoelectron microscopy. J. Struct. Biol., 114, 177-183.
    • (1995) J. Struct. Biol. , vol.114 , pp. 177-183
    • Furrer, P.1    Bednar, J.2    Dubochet, J.3    Hamiche, A.4    Prunell, A.5
  • 21
    • 0034649621 scopus 로고    scopus 로고
    • Rapid exchange of histone H1.1 on chromatin in living human cells
    • DOI 10.1038/35048603
    • Lever, M. A., Th'ng, J. P., Sun, X. and Hendzel, M. J. (2000) Rapid exchange of histone H1. 1 on chromatin in living human cells. Nature, 408, 873-876. (Pubitemid 32016099)
    • (2000) Nature , vol.408 , Issue.6814 , pp. 873-876
    • Lever, M.A.1    Th'ng, J.P.H.2    Sun, X.3    Hendzel, M.J.4
  • 22
    • 0034649663 scopus 로고    scopus 로고
    • Dynamic binding of histone H1 to chromatin in living cells
    • DOI 10.1038/35048610
    • Misteli, T., Gunjan, A., Hock, R., Bustin, M. and Brown, D. T. (2000) Dynamic binding of histone H1 to chromatin in living cells. Nature, 408, 877-881. (Pubitemid 32016100)
    • (2000) Nature , vol.408 , Issue.6814 , pp. 877-881
    • Misteli, T.1    Gunjan, A.2    Hock, R.3    Bustin, M.4    Brown, D.T.5
  • 23
    • 0019880525 scopus 로고
    • Exchange of histone H1 between segments of chromatin
    • Caron, F. and Thomas, J. O. (1981) Exchange of histone H1 between segments of chromatin. J. Mol. Biol., 146, 513-537.
    • (1981) J. Mol. Biol. , vol.146 , pp. 513-537
    • Caron, F.1    Thomas, J.O.2
  • 24
    • 0022470051 scopus 로고
    • Salt-dependent co-operative interaction of histone H1 with linear DNA
    • Clark, D. J. and Thomas, J. O. (1986) Salt-dependent co-operative interaction of histone H1 with linear DNA. J. Mol. Biol., 187, 569-580. (Pubitemid 16041058)
    • (1986) Journal of Molecular Biology , vol.187 , Issue.4 , pp. 569-580
    • Clark, D.J.1    Thomas, J.O.2
  • 25
    • 2442574861 scopus 로고    scopus 로고
    • The C-terminal domain is the primary determinant of histone H1 binding to chromatin in vivo
    • DOI 10.1074/jbc.M400070200
    • 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. (Pubitemid 38623446)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.19 , pp. 20028-20034
    • Hendzel, M.J.1    Lever, M.A.2    Crawford, E.3    Th'Ng, J.P.H.4
  • 26
    • 0029787814 scopus 로고    scopus 로고
    • Site-directed cleavage of DNA by a linker histone-Fe(II) EDTA conjugate: Localization of a globular domain binding site within a nucleosome
    • DOI 10.1021/bi961590+
    • Hayes, J. J. (1996) Site-directed cleavage of DNA by a linker histone-Fe(II) EDTA conjugate: localization of a globular domain binding site within a nucleosome. Biochemistry, 35, 11931-11937. (Pubitemid 26313662)
    • (1996) Biochemistry , vol.35 , Issue.37 , pp. 11931-11937
    • Hayes, J.J.1
  • 27
    • 37549023859 scopus 로고    scopus 로고
    • Acetylation mimics within individual core histone tail domains indicate distinct roles in regulating the stability of higher-order chromatin structure
    • Wang, X. and Hayes, J. J. (2008) Acetylation mimics within individual core histone tail domains indicate distinct roles in regulating the stability of higher-order chromatin structure. Mol. Cell. Biol., 28, 227-236.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 227-236
    • Wang, X.1    Hayes, J.J.2
  • 28
    • 23644433196 scopus 로고    scopus 로고
    • Measurements of internal distance changes of the 30 S ribosome using FRET with multiple donor-acceptor pairs: Quantitative spectroscopic methods
    • DOI 10.1016/j.jmb.2005.06.027, PII S0022283605006777
    • Majumdar, Z. K., Hickerson, R., Noller, H. F. and Clegg, R. M. (2005) Measurements of internal distance changes of the 30S ribosome using FRET with multiple donor-acceptor pairs: quantitative spectroscopic methods. J. Mol. Biol., 351, 1123-1145. (Pubitemid 41133457)
    • (2005) Journal of Molecular Biology , vol.351 , Issue.5 , pp. 1123-1145
    • Majumdar, Z.K.1    Hickerson, R.2    Noller, H.F.3    Clegg, R.M.4
  • 29
  • 30
    • 0033413080 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer between single fluorophores attached to a coiled-coil protein in aqueous solution
    • Ishii, Y., Yoshida, T., Funatsu, T., Wazawa, T. and Yanagida, T. Y. (1999) Fluorescence resonance energy transfer between single fluorophores attached to a coiled-coil protein in aqueous solution. Chem. Phys., 247, 163-173.
    • (1999) Chem. Phys. , vol.247 , pp. 163-173
    • Ishii, Y.1    Yoshida, T.2    Funatsu, T.3    Wazawa, T.4    Yanagida, T.Y.5
  • 31
    • 33748454896 scopus 로고    scopus 로고
    • Toward an accurate theoretical framework for describing ensembles for proteins under strongly denaturing conditions
    • DOI 10.1529/biophysj.106.086264
    • Tran, H. T. and Pappu, R. V. (2006) Toward an accurate theoretical framework for describing ensembles for proteins under strongly denaturing conditions. Biophys. J., 91, 1868-1886. (Pubitemid 44352450)
    • (2006) Biophysical Journal , vol.91 , Issue.5 , pp. 1868-1886
    • Tran, H.T.1    Pappu, R.V.2
  • 32
    • 0025295030 scopus 로고
    • Analysis of the charge distribution in the C-terminal region of histone H1 as related to its interaction with DNA
    • DOI 10.1002/bip.360291003
    • Subirana, J. A. (1990) Analysis of the charge distribution in the C-terminal region of histone H1 as related to its interaction with DNA. Biopolymers, 29, 1351-1357. (Pubitemid 20180257)
    • (1990) Biopolymers , vol.29 , Issue.10-11 , pp. 1351-1357
    • Subirana, J.A.1
  • 33
    • 69549124299 scopus 로고    scopus 로고
    • Role of charge neutralization in the folding of the carboxy-terminal domain of histone H1
    • Roque, A., Ponte, I. and Suau, P. (2009) Role of charge neutralization in the folding of the carboxy-terminal domain of histone H1. J. Phys. Chem. B, 113, 12061-12066.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 12061-12066
    • Roque, A.1    Ponte, I.2    Suau, P.3
  • 34
    • 0014095983 scopus 로고
    • The use of computed optical rotatory dispersion curves for the evaluation of protein conformation
    • Greenfield, N., Davidson, B. and Fasman, G. D. (1967) The use of computed optical rotatory dispersion curves for the evaluation of protein conformation. Biochemistry, 6, 1630-1637.
    • (1967) Biochemistry , vol.6 , pp. 1630-1637
    • Greenfield, N.1    Davidson, B.2    Fasman, G.D.3
  • 35
    • 0024426046 scopus 로고
    • A stable α-helical element in the carboxy-terminal domain of free and chromatin-bound histone H1 from sea urchin sperm
    • Hill, C. S., Martin, S. R. and Thomas, J. O. (1989) A stable alpha-helical element in the carboxy-terminal domain of free and chromatin-bound histone H1 from sea urchin sperm. EMBO J., 8, 2591-2599. (Pubitemid 19273343)
    • (1989) EMBO Journal , vol.8 , Issue.9 , pp. 2591-2599
    • Hill, C.S.1    Martin, S.R.2    Thomas, J.O.3
  • 36
    • 0019615938 scopus 로고
    • Secondary and tertiary structural differences between histone H1 molecules from calf thymus and sea-urchin (Sphaerechinus granularis) sperm
    • Giancotti, V., Russo, E., Cosimi, S., Cary, P. D. and Crane-Robinson, C. (1981) Secondary and tertiary structural differences between histone H1 molecules from calf thymus and sea-urchin (Sphaerechinus granularis) sperm. Biochem. J., 197, 655-660.
    • (1981) Biochem. J. , vol.197 , pp. 655-660
    • Giancotti, V.1    Russo, E.2    Cosimi, S.3    Cary, P.D.4    Crane-Robinson, C.5
  • 37
    • 0242285999 scopus 로고    scopus 로고
    • Molecular modeling of the chromatosome particle
    • DOI 10.1093/nar/gkg481
    • Bharath, M. M., Chandra, N. R. and Rao, M. R. (2003) Molecular modeling of the chromatosome particle. Nucleic Acids Res., 31, 4264-4274. (Pubitemid 37442306)
    • (2003) Nucleic Acids Research , vol.31 , Issue.14 , pp. 4264-4274
    • Srinivas Bharath, M.M.1    Chandra, N.R.2    Rao, M.R.S.3
  • 38
    • 49249102932 scopus 로고    scopus 로고
    • Phosphorylation of the carboxy-terminal domain of histone H1: Effects on secondary structure and DNA condensation
    • Roque, A., Ponte, I., Arrondo, J. L. and Suau, P. (2008) Phosphorylation of the carboxy-terminal domain of histone H1: effects on secondary structure and DNA condensation. Nucleic Acids Res., 36, 4719-4726.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 4719-4726
    • Roque, A.1    Ponte, I.2    Arrondo, J.L.3    Suau, P.4
  • 39
    • 82255183226 scopus 로고    scopus 로고
    • From crystal and NMR structures, footprints and cryo-electron-micrographs to large and soft structures: Nanoscale modeling of the nucleosomal stem
    • Meyer, S., Becker, N., Syed, S. H., Goutte-Gattat, D., Shukla, M. S., Hayes, J., Angelov, D., Bednar, J., Dimitrov, S. and Everaers, R. (2011) From crystal and NMR structures, footprints and cryo-electron-micrographs to large and soft structures: nanoscale modeling of the nucleosomal stem. Nucleic Acids Res., 39, 9139-9154.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 9139-9154
    • Meyer, S.1    Becker, N.2    Syed, S.H.3    Goutte-Gattat, D.4    Shukla, M.S.5    Hayes, J.6    Angelov, D.7    Bednar, J.8    Dimitrov, S.9    Everaers, R.10


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