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Volumn 371, Issue 1, 2007, Pages 11-18

The Histone Domain of macroH2A1 Contains Several Dispersed Elements that Are Each Sufficient to Direct Enrichment on the Inactive X Chromosome

Author keywords

chromatin assembly; H2A; histone variants; macroH2A; X inactivation

Indexed keywords

DIMER; HISTONE H2A; HISTONE H2A1; UNCLASSIFIED DRUG;

EID: 34447099478     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.05.063     Document Type: Article
Times cited : (23)

References (34)
  • 3
    • 10044298120 scopus 로고    scopus 로고
    • Ubiquitinated proteins including uH2A on the human and mouse inactive X chromosome: enrichment in gene rich bands
    • Smith K.P., Byron M., Clemson C.M., and Lawrence J. B. Ubiquitinated proteins including uH2A on the human and mouse inactive X chromosome: enrichment in gene rich bands. Chromosoma 113 (2004) 324-335
    • (2004) Chromosoma , vol.113 , pp. 324-335
    • Smith, K.P.1    Byron, M.2    Clemson, C.M.3    Lawrence, J. B.4
  • 4
    • 22144448593 scopus 로고    scopus 로고
    • Histone H2A phosphorylation in DNA double-strand break repair
    • Foster E.R., and Downs J.A. Histone H2A phosphorylation in DNA double-strand break repair. FEBS J. 272 (2005) 3231-3240
    • (2005) FEBS J. , vol.272 , pp. 3231-3240
    • Foster, E.R.1    Downs, J.A.2
  • 5
    • 0037390327 scopus 로고    scopus 로고
    • Pericentric heterochromatin becomes enriched with H2A. Z during early mammalian development
    • Rangasamy D., Berven L., Ridgway P., and Tremethick D.J. Pericentric heterochromatin becomes enriched with H2A. Z during early mammalian development. EMBO J. 22 (2003) 1599-1607
    • (2003) EMBO J. , vol.22 , pp. 1599-1607
    • Rangasamy, D.1    Berven, L.2    Ridgway, P.3    Tremethick, D.J.4
  • 6
    • 3042642001 scopus 로고    scopus 로고
    • RNA interference demonstrates a novel role for H2A.Z in chromosome segregation
    • Rangasamy D., Greaves I., and Tremethick D.J. RNA interference demonstrates a novel role for H2A.Z in chromosome segregation. Nature Struct. Mol. Biol. 11 (2004) 650-655
    • (2004) Nature Struct. Mol. Biol. , vol.11 , pp. 650-655
    • Rangasamy, D.1    Greaves, I.2    Tremethick, D.J.3
  • 7
    • 0035931749 scopus 로고    scopus 로고
    • A novel chromatin protein, distantly related to histone H2A, is largely excluded from the inactive X chromosome
    • Chadwick B.P., and Willard H.F. A novel chromatin protein, distantly related to histone H2A, is largely excluded from the inactive X chromosome. J. Cell Biol. 152 (2001) 375-384
    • (2001) J. Cell Biol. , vol.152 , pp. 375-384
    • Chadwick, B.P.1    Willard, H.F.2
  • 8
    • 0032507949 scopus 로고    scopus 로고
    • Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals
    • Costanzi C., and Pehrson J.R. Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals. Nature 393 (1998) 599-601
    • (1998) Nature , vol.393 , pp. 599-601
    • Costanzi, C.1    Pehrson, J.R.2
  • 9
    • 0035336967 scopus 로고    scopus 로고
    • Histone H2A variants and the inactive X chromosome: identification of a second macroH2A variant
    • Chadwick B.P., and Willard H.F. Histone H2A variants and the inactive X chromosome: identification of a second macroH2A variant. Hum. Mol. Genet. 10 (2001) 1101-1113
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1101-1113
    • Chadwick, B.P.1    Willard, H.F.2
  • 10
    • 0035877759 scopus 로고    scopus 로고
    • MACROH2A2, a new member of the MARCOH2A core histone family
    • Costanzi C., and Pehrson J.R. MACROH2A2, a new member of the MARCOH2A core histone family. J. Biol. Chem. 276 (2001) 21776-21784
    • (2001) J. Biol. Chem. , vol.276 , pp. 21776-21784
    • Costanzi, C.1    Pehrson, J.R.2
  • 11
    • 0035858882 scopus 로고    scopus 로고
    • Synergism of Xist RNA, DNA methylation, and histone hypoacetylation in maintaining X chromosome inactivation
    • Csankovszki G., Nagy A., and Jaenisch R. Synergism of Xist RNA, DNA methylation, and histone hypoacetylation in maintaining X chromosome inactivation. J. Cell. Biol. 153 (2001) 773-784
    • (2001) J. Cell. Biol. , vol.153 , pp. 773-784
    • Csankovszki, G.1    Nagy, A.2    Jaenisch, R.3
  • 12
    • 21144446865 scopus 로고    scopus 로고
    • Stable X chromosome inactivation involves the PRC1 Polycomb complex and requires histone MACROH2A1 and the CULLIN3/SPOP ubiquitin E3 ligase
    • Hernandez-Munoz I., Lund A.H., van der Stoop P., Boutsma E., Muijrers I., Verhoeven E., et al. Stable X chromosome inactivation involves the PRC1 Polycomb complex and requires histone MACROH2A1 and the CULLIN3/SPOP ubiquitin E3 ligase. Proc. Natl Acad. Sci. USA 102 (2005) 7635-7640
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 7635-7640
    • Hernandez-Munoz, I.1    Lund, A.H.2    van der Stoop, P.3    Boutsma, E.4    Muijrers, I.5    Verhoeven, E.6
  • 13
    • 0032805149 scopus 로고    scopus 로고
    • Conditional deletion of Xist disrupts histone macroH2A localization but not maintenance of X inactivation
    • Csankovszki G., Panning B., Bates B., Pehrson J. R., and Jaenisch R. Conditional deletion of Xist disrupts histone macroH2A localization but not maintenance of X inactivation. Nat. Genet. 22 (1999) 323-324
    • (1999) Nat. Genet. , vol.22 , pp. 323-324
    • Csankovszki, G.1    Panning, B.2    Bates, B.3    Pehrson, J. R.4    Jaenisch, R.5
  • 15
    • 0026737922 scopus 로고
    • MacroH2A, a core histone containing a large non-histone region
    • Pehrson J.R., and Fried V.A. MacroH2A, a core histone containing a large non-histone region. Science 257 (1992) 1398-1400
    • (1992) Science , vol.257 , pp. 1398-1400
    • Pehrson, J.R.1    Fried, V.A.2
  • 16
    • 0030975594 scopus 로고    scopus 로고
    • Developmental and tissue expression patterns of histone macroH2A1 subtypes
    • Pehrson J.R., Costanzi C., and Dharia C. Developmental and tissue expression patterns of histone macroH2A1 subtypes. J. Cell Biochem. 65 (1997) 107-113
    • (1997) J. Cell Biochem. , vol.65 , pp. 107-113
    • Pehrson, J.R.1    Costanzi, C.2    Dharia, C.3
  • 18
    • 0035394053 scopus 로고    scopus 로고
    • Histone variant macroH2A contains two distinct macrochromatin domains capable of directing macroH2A to the inactive X chromosome
    • Chadwick B.P., Valley C.M., and Willard H.F. Histone variant macroH2A contains two distinct macrochromatin domains capable of directing macroH2A to the inactive X chromosome. Nucl. Acids Res. 29 (2001) 2699-2705
    • (2001) Nucl. Acids Res. , vol.29 , pp. 2699-2705
    • Chadwick, B.P.1    Valley, C.M.2    Willard, H.F.3
  • 19
    • 28544442465 scopus 로고    scopus 로고
    • Swc2 is a widely conserved H2AZ-binding module essential for ATP-dependent histone exchange
    • Wu W.H., Alami S., Luk E., Wu C.H., Sen S., Mizuguchi G., et al. Swc2 is a widely conserved H2AZ-binding module essential for ATP-dependent histone exchange. Nature Struct. Mol. Biol. 12 (2005) 1064-1071
    • (2005) Nature Struct. Mol. Biol. , vol.12 , pp. 1064-1071
    • Wu, W.H.1    Alami, S.2    Luk, E.3    Wu, C.H.4    Sen, S.5    Mizuguchi, G.6
  • 20
    • 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. Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature 389 (1997) 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
  • 21
    • 34447108578 scopus 로고    scopus 로고
    • The histone variant macroh2a preferentially forms 'hybrid nucleosomes'
    • Chakravarthy S., and Luger K. The histone variant macroh2a preferentially forms 'hybrid nucleosomes'. J. Biol. Chem. 21 (2006) 133-153
    • (2006) J. Biol. Chem. , vol.21 , pp. 133-153
    • Chakravarthy, S.1    Luger, K.2
  • 23
    • 31644449378 scopus 로고    scopus 로고
    • Mapping post-translational modifications of the histone variant MacroH2A1 using tandem mass spectrometry
    • Chu F., Nusinow D.A., Chalkley R.J., Plath K., Panning B., and Burlingame A.L. Mapping post-translational modifications of the histone variant MacroH2A1 using tandem mass spectrometry. Mol. Cell. Proteomics 5 (2006) 194-203
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 194-203
    • Chu, F.1    Nusinow, D.A.2    Chalkley, R.J.3    Plath, K.4    Panning, B.5    Burlingame, A.L.6
  • 24
    • 0018036390 scopus 로고
    • Assembly of newly replicated chromatin
    • Worcel A., Han S., and Wong M.L. Assembly of newly replicated chromatin. Cell 15 (1978) 969-977
    • (1978) Cell , vol.15 , pp. 969-977
    • Worcel, A.1    Han, S.2    Wong, M.L.3
  • 25
    • 0029053420 scopus 로고
    • Thermodynamic studies of the core histones: ionic strength and pH dependence of H2A-H2B dimer stability
    • Karantza V., Baxevanis A.D., Freire E., and Moudrianakis E.N. Thermodynamic studies of the core histones: ionic strength and pH dependence of H2A-H2B dimer stability. Biochemistry 34 (1995) 5988-5996
    • (1995) Biochemistry , vol.34 , pp. 5988-5996
    • Karantza, V.1    Baxevanis, A.D.2    Freire, E.3    Moudrianakis, E.N.4
  • 26
    • 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. Characterization of nucleosome core particles containing histone proteins made in bacteria. J. Mol. Biol. 272 (1997) 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
  • 27
    • 0037126715 scopus 로고    scopus 로고
    • The effect of salts on the stability of the H2A-H2B histone dimer
    • Gloss L.M., and Placek B.J. The effect of salts on the stability of the H2A-H2B histone dimer. Biochemistry 41 (2002) 14951-14959
    • (2002) Biochemistry , vol.41 , pp. 14951-14959
    • Gloss, L.M.1    Placek, B.J.2
  • 28
    • 0348184963 scopus 로고    scopus 로고
    • ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex
    • Mizuguchi G., Shen X., Landry J., Wu W.H., Sen S., and Wu C. ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex. Science 303 (2004) 343-348
    • (2004) Science , vol.303 , pp. 343-348
    • Mizuguchi, G.1    Shen, X.2    Landry, J.3    Wu, W.H.4    Sen, S.5    Wu, C.6
  • 29
    • 9144269660 scopus 로고    scopus 로고
    • A Snf2 family ATPase complex required for recruitment of the histone H2A variant Htz1
    • Krogan N.J., Keogh M.C., Datta N., Sawa C., Ryan O.W., Ding H., et al. A Snf2 family ATPase complex required for recruitment of the histone H2A variant Htz1. Mol. Cell 12 (2003) 1565-1576
    • (2003) Mol. Cell , vol.12 , pp. 1565-1576
    • Krogan, N.J.1    Keogh, M.C.2    Datta, N.3    Sawa, C.4    Ryan, O.W.5    Ding, H.6
  • 30
    • 19344372948 scopus 로고    scopus 로고
    • A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A, Z into euchromatin
    • Kobor M.S., Venkatasubrahmanyam S., Meneghini M.D., Gin J.W., Jennings J.L., Link A.J., et al. A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A, Z into euchromatin. PLoS Biol. 2 (2004) E131
    • (2004) PLoS Biol. , vol.2
    • Kobor, M.S.1    Venkatasubrahmanyam, S.2    Meneghini, M.D.3    Gin, J.W.4    Jennings, J.L.5    Link, A.J.6
  • 31
    • 0033664380 scopus 로고    scopus 로고
    • Crystal structure of a nucleosome core particle containing the variant histone H2A
    • Suto R.K., Clarkson M.J., Tremethick D.J., and Luger K. Crystal structure of a nucleosome core particle containing the variant histone H2A. Z. Nature Struct. Biol. 7 (2000) 1121-1124
    • (2000) Z. Nature Struct. Biol. , vol.7 , pp. 1121-1124
    • Suto, R.K.1    Clarkson, M.J.2    Tremethick, D.J.3    Luger, K.4
  • 33
    • 11244313165 scopus 로고    scopus 로고
    • Developmentally regulated alterations in Polycomb repressive complex 1 proteins on the inactive X chromosome
    • Plath K., Talbot D., Hamer K.M., Otte A.P., Yang T. P., Jaenisch R., and Panning B. Developmentally regulated alterations in Polycomb repressive complex 1 proteins on the inactive X chromosome. J. Cell Biol. 167 (2004) 1025-1035
    • (2004) J. Cell Biol. , vol.167 , pp. 1025-1035
    • Plath, K.1    Talbot, D.2    Hamer, K.M.3    Otte, A.P.4    Yang, T. P.5    Jaenisch, R.6    Panning, B.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.