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Volumn 31, Issue 11, 2011, Pages 2341-2348

Nucleosome linker DNA contacts and induces specific folding of the intrinsically disordered H1 Carboxyl-terminal domain

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE H1; LINK PROTEIN; NAKED DNA;

EID: 79958068470     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.05145-11     Document Type: Article
Times cited : (57)

References (43)
  • 1
    • 0019157001 scopus 로고
    • The structure of histone H1 and its location in chromatin
    • Allan, J., P. G. Hartman, C. Crane-Robinson, and F. X. Aviles. 1980. The structure of histone H1 and its location in chromatin. Nature 288:675-679.
    • (1980) Nature , vol.288 , pp. 675-679
    • Allan, J.1    Hartman, P.G.2    Crane-Robinson, C.3    Aviles, F.X.4
  • 2
    • 0022446807 scopus 로고
    • Roles of H1 domains in determining higher order chromatin structure and H1 location
    • Allan, J., T. Mitchell, N. Harborne, L. Bohm, and C. Crane-Robinson. 1986. Roles of H1 domains in determining higher order chromatin structure and H1 location. J. Mol. Biol. 187:591-601.
    • (1986) J. Mol. Biol. , vol.187 , pp. 591-601
    • Allan, J.1    Mitchell, T.2    Harborne, N.3    Bohm, L.4    Crane-Robinson, C.5
  • 3
    • 0019888694 scopus 로고
    • Histones H1 and H5: one or two molecules per nucleosome?
    • Bates, D. L., and J. O. Thomas. 1981. Histones H1 and H5: one or two molecules per nucleosome? Nucleic Acids Res. 2:5883-5894.
    • (1981) Nucleic Acids Res. , vol.2 , pp. 5883-5894
    • Bates, D.L.1    Thomas, J.O.2
  • 4
    • 0032564478 scopus 로고    scopus 로고
    • Nucleosomes, linker DNA, and linker histone form a unique structural motif that directs the higher-order folding and compaction of chromatin
    • Bednar, J., et al. 1998. Nucleosomes, linker DNA, and linker histone form a unique structural motif that directs the higher-order folding and compaction of chromatin. Proc. Natl. Acad. Sci. U. S. A. 95:14173-14178.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 14173-14178
    • Bednar, J.1
  • 5
    • 0029085907 scopus 로고
    • Electrostatic mechanism of nucleosome spacing
    • Blank, T. A., and P. B. Becker. 1995. Electrostatic mechanism of nucleosome spacing. J. Mol. Biol. 252:305-313.
    • (1995) J. Mol. Biol. , vol.252 , pp. 305-313
    • Blank, T.A.1    Becker, P.B.2
  • 6
    • 33644800314 scopus 로고    scopus 로고
    • Mapping the interaction surface of linker histone H1(0) with the nucleosome of native chromatin in vivo
    • Brown, D. T., T. Izard, and T. Misteli. 2006. Mapping the interaction surface of linker histone H1(0) with the nucleosome of native chromatin in vivo. Nat. Struct. Mol. Biol. 13:250-255.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 250-255
    • Brown, D.T.1    Izard, T.2    Misteli, T.3
  • 7
    • 0032553013 scopus 로고    scopus 로고
    • Linker histones stabilize the intrinsic salt-dependent folding of nucleosomal arrays: mechanistic ramifications for higher-order chromatin folding
    • Carruthers, L. M., J. Bednar, C. L. Woodcock, and J. C. Hansen. 1998. Linker histones stabilize the intrinsic salt-dependent folding of nucleosomal arrays: mechanistic ramifications for higher-order chromatin folding. Biochemistry 37:14776-14787.
    • (1998) Biochemistry , vol.37 , pp. 14776-14787
    • Carruthers, L.M.1    Bednar, J.2    Woodcock, C.L.3    Hansen, J.C.4
  • 8
    • 0023711642 scopus 로고
    • Alpha-helix in the carboxy-terminal domains of histones H1 and H5
    • Clark, D. J., C. S. Hill, S. R. Martin, and J. O. Thomas. 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
  • 9
    • 0025327471 scopus 로고
    • Electrostatic mechanism of chromatin folding
    • Clark, D. J., and T. Kimura. 1990. Electrostatic mechanism of chromatin folding. J. Mol. Biol. 211:883-896.
    • (1990) J. Mol. Biol. , vol.211 , pp. 883-896
    • Clark, D.J.1    Kimura, T.2
  • 10
    • 0024264685 scopus 로고
    • Differences in the binding of H1 variants to DNA.. Cooperativity and linker-length related distribution
    • Clark, D. J., and J. O. Thomas. 1988. Differences in the binding of H1 variants to DNA. Cooperativity and linker-length related distribution. Eur. J. Biochem. 178:225-233.
    • (1988) Eur. J. Biochem. , vol.178 , pp. 225-233
    • Clark, D.J.1    Thomas, J.O.2
  • 11
    • 0022470051 scopus 로고
    • Salt-dependent co-operative interaction of histone H1 with linear DNA
    • Clark, D. J., and J. O. Thomas. 1986. Salt-dependent co-operative interaction of histone H1 with linear DNA. J. Mol. Biol. 187:569-580.
    • (1986) J. Mol. Biol. , vol.187 , pp. 569-580
    • Clark, D.J.1    Thomas, J.O.2
  • 12
    • 0031106457 scopus 로고    scopus 로고
    • Where is the globular domain of linker histone located on the nucleosome? Trends Biochem
    • Crane-Robinson, C. 1997. Where is the globular domain of linker histone located on the nucleosome? Trends Biochem. Sci. 22:75-77.
    • (1997) Sci , vol.22 , pp. 75-77
    • Crane-Robinson, C.1
  • 13
    • 33744813570 scopus 로고    scopus 로고
    • Complex of linker histone H5 with the nucleosome and its implications for chromatin packing
    • Fan, L., and V. A. Roberts. 2006. Complex of linker histone H5 with the nucleosome and its implications for chromatin packing. Proc. Natl. Acad. Sci. U. S. A. 103:8384-8389.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 8384-8389
    • Fan, L.1    Roberts, V.A.2
  • 14
    • 29244449333 scopus 로고    scopus 로고
    • Histone H1 depletion in mammals alters global chromatin structure but causes specific changes in gene regulation
    • Fan, Y., et al. 2005. Histone H1 depletion in mammals alters global chromatin structure but causes specific changes in gene regulation. Cell 123: 1199-1212.
    • (2005) Cell , vol.123 , pp. 1199-1212
    • Fan, Y.1
  • 15
    • 33644865137 scopus 로고    scopus 로고
    • Intrinsic protein disorder, amino acid composition, and histone terminal domains
    • Hansen, J. C., X. Lu, E. D. Ross, and R. W. Woody. 2006. Intrinsic protein disorder, amino acid composition, and histone terminal domains. J. Biol. Chem. 281:1853-1856.
    • (2006) J. Biol. Chem. , vol.281 , pp. 1853-1856
    • Hansen, J.C.1    Lu, X.2    Ross, E.D.3    Woody, R.W.4
  • 16
    • 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
    • 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.
    • (1996) Biochemistry , vol.35 , pp. 11931-11937
    • Hayes, J.J.1
  • 17
    • 0029966744 scopus 로고    scopus 로고
    • A putative DNA binding surface in the globular domain of a linker histone is not essential for specific binding to the nucleosome
    • Hayes, J. J., R. Kaplan, K. Ura, D. Pruss, and A. Wolffe. 1996. A putative DNA binding surface in the globular domain of a linker histone is not essential for specific binding to the nucleosome. J. Biol. Chem. 271:25817-25822.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25817-25822
    • Hayes, J.J.1    Kaplan, R.2    Ura, K.3    Pruss, D.4    Wolffe, A.5
  • 18
    • 0031148959 scopus 로고    scopus 로고
    • In vitro reconstitution and analysis of mononucleosomes containing defined DNAs and proteins
    • Hayes, J. J., and K. M. Lee. 1997. In vitro reconstitution and analysis of mononucleosomes containing defined DNAs and proteins. Methods 12:2-9.
    • (1997) Methods , vol.12 , pp. 2-9
    • Hayes, J.J.1    Lee, K.M.2
  • 19
    • 0027248504 scopus 로고
    • Preferential and asymmetric interaction of linker histones with 5S DNA in the nucleosome
    • Hayes, J. J., and A. P. Wolffe. 1993. Preferential and asymmetric interaction of linker histones with 5S DNA in the nucleosome. Proc. Natl. Acad. Sci. U. S. A. 90:6415-6419.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 6415-6419
    • Hayes, J.J.1    Wolffe, A.P.2
  • 20
    • 2442574861 scopus 로고    scopus 로고
    • The C-terminal domain is the primary determinant of histone H1 binding to chromatin in vivo
    • Hendzel, M. J., M. A. Lever, E. Crawford, and J. P. Th'ng. 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
  • 21
    • 0029946736 scopus 로고    scopus 로고
    • Drosophila NAP-1 is a core histone chaperone that functions in ATP-facilitated assembly of regularly spaced nucleosomal arrays
    • Ito, T., M. Bulger, R. Kobayashi, and J. T. Kadonaga. 1996. Drosophila NAP-1 is a core histone chaperone that functions in ATP-facilitated assembly of regularly spaced nucleosomal arrays. Mol. Cell. Biol. 16:3112-3124.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3112-3124
    • Ito, T.1    Bulger, M.2    Kobayashi, R.3    Kadonaga, J.T.4
  • 23
    • 0034649621 scopus 로고    scopus 로고
    • Rapid exchange of histone H1.1 on chromatin in living human cells
    • Lever, M. A., J. P. Th'ng, X. Sun, and M. J. Hendzel. 2000. Rapid exchange of histone H1.1 on chromatin in living human cells. Nature 408:873-876.
    • (2000) Nature , vol.408 , pp. 873-876
    • Lever, M.A.1    Th'ng, J.P.2    Sun, X.3    Hendzel, M.J.4
  • 24
    • 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 J. Widom. 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
  • 25
    • 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., B. Hamkalo, M. H. Parseghian, and J. C. Hansen. 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
  • 26
    • 1542305640 scopus 로고    scopus 로고
    • Identification of specific functional subdomains within the linker histone H10 C-terminal domain
    • Lu, X., and J. C. Hansen. 2004. Identification of specific functional subdomains within the linker histone H10 C-terminal domain. J. Biol. Chem. 279:8701-8707.
    • (2004) J. Biol. Chem. , vol.279 , pp. 8701-8707
    • Lu, X.1    Hansen, J.C.2
  • 27
    • 0034649663 scopus 로고    scopus 로고
    • Dynamic binding of histone H1 to chromatin in living cells
    • Misteli, T., A. Gunjan, R. Hock, M. Bustin, and D. T. Brown. 2000. Dynamic binding of histone H1 to chromatin in living cells. Nature 408:877-881.
    • (2000) Nature , vol.408 , pp. 877-881
    • Misteli, T.1    Gunjan, A.2    Hock, R.3    Bustin, M.4    Brown, D.T.5
  • 29
    • 0027402969 scopus 로고
    • Crystal structure of globular domain of histone H5 and its implications for nucleosome binding
    • Ramakrishnan, V., J. T. Finch, V. Graziano, P. L. Lee, and R. M. Sweet. 1993. Crystal structure of globular domain of histone H5 and its implications for nucleosome binding. Nature 362:219-224.
    • (1993) Nature , vol.362 , pp. 219-224
    • Ramakrishnan, V.1    Finch, J.T.2    Graziano, V.3    Lee, P.L.4    Sweet, R.M.5
  • 30
    • 49249102932 scopus 로고    scopus 로고
    • Phosphorylation of the carboxy-terminal domain of histone H1: effects on secondary structure and DNA condensation
    • Roque, A., I. Ponte, J. L. Arrondo, and P. Suau. 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
  • 31
    • 69549124299 scopus 로고    scopus 로고
    • Role of charge neutralization in the folding of the carboxy-terminal domain of histone H1
    • Roque, A., I. Ponte, and P. Suau. 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
  • 33
    • 0018266771 scopus 로고
    • Structure of the chromatosome, a chromatin particle containing 160 base pairs of DNA and all the histones
    • Simpson, R. T. 1978. Structure of the chromatosome, a chromatin particle containing 160 base pairs of DNA and all the histones. Biochemistry 17: 5524-5531.
    • (1978) Biochemistry , vol.17 , pp. 5524-5531
    • Simpson, R.T.1
  • 34
    • 0028850059 scopus 로고
    • Overcoming a nucleosomal barrier to transcription
    • Studitsky, V. M., D. J. Clark, and G. Felsenfeld. 1995. Overcoming a nucleosomal barrier to transcription. Cell 83:19-27.
    • (1995) Cell , vol.83 , pp. 19-27
    • Studitsky, V.M.1    Clark, D.J.2    Felsenfeld, G.3
  • 35
    • 0025295030 scopus 로고
    • Analysis of the charge distribution in the C-terminal region of histone H1 as related to its interaction with DNA
    • 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.
    • (1990) Biopolymers , vol.29 , pp. 1351-1357
    • Subirana, J.A.1
  • 36
    • 77953104932 scopus 로고    scopus 로고
    • Single-base resolution mapping of H1-nucleosome interactions and 3D organization of the nucleosome
    • Syed, S. H., et al. 2010. Single-base resolution mapping of H1-nucleosome interactions and 3D organization of the nucleosome. Proc. Natl. Acad. Sci. U. S. A. 107:9620-9625.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 9620-9625
    • Syed, S.H.1
  • 37
    • 0018581187 scopus 로고
    • Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin
    • Thoma, F., T. Koller, and A. Klug. 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
  • 38
    • 33748454896 scopus 로고    scopus 로고
    • Toward an accurate theoretical framework for describing ensembles for proteins under strongly denaturing conditions
    • Tran, H. T., and R. V. Pappu. 2006. Toward an accurate theoretical framework for describing ensembles for proteins under strongly denaturing conditions. Biophys. J. 91:1868-1886.
    • (2006) Biophys. J. , vol.91 , pp. 1868-1886
    • Tran, H.T.1    Pappu, R.V.2
  • 39
    • 0029790690 scopus 로고    scopus 로고
    • Differential association of HMG1 and linker histones B4 and H1 with dinucleosomal DNA: structural transitions and transcriptional repression
    • Ura, K., K. Nightingale, and A. P. Wolffe. 1996. Differential association of HMG1 and linker histones B4 and H1 with dinucleosomal DNA: structural transitions and transcriptional repression. EMBO J. 15:4959-4969.
    • (1996) EMBO J , vol.15 , pp. 4959-4969
    • Ura, K.1    Nightingale, K.2    Wolffe, A.P.3
  • 40
    • 77956323721 scopus 로고    scopus 로고
    • Seven lessons from one IDP structural analysis
    • Uversky, V. N. 2010. Seven lessons from one IDP structural analysis. Structure 18:1069-1071.
    • (2010) Structure , vol.18 , pp. 1069-1071
    • Uversky, V.N.1
  • 41
    • 0003903126 scopus 로고
    • Springer Verlag, New York, NY
    • van Holde, K. E. 1989. Chromatin. Springer Verlag, New York, NY.
    • (1989) Chromatin
    • van Holde, K.E.1
  • 43
    • 0020537659 scopus 로고
    • Regular arrangement of nucleosomes on 5S rRNA genes in Xenopus laevis
    • Young, D., and D. Carroll. 1983. Regular arrangement of nucleosomes on 5S rRNA genes in Xenopus laevis. Mol. Cell. Biol. 3:720-730.
    • (1983) Mol. Cell. Biol. , vol.3 , pp. 720-730
    • Young, D.1    Carroll, D.2


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