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Volumn 50, Issue , 2010, Pages 43-54

Chromatin assembly and signalling the end of DNA repair requires acetylation of histone H3 on lysine 56

Author keywords

Acetylation; Chromatin; DNA repair; Genome stability; H3K56; Histones

Indexed keywords

SACCHAROMYCETALES;

EID: 77953016138     PISSN: 03060225     EISSN: None     Source Type: Journal    
DOI: 10.1007/978-90-481-3471-7_3     Document Type: Article
Times cited : (11)

References (37)
  • 2
    • 0028841317 scopus 로고
    • The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability
    • Brachmann, C. B., Sherman, J. M., Devine, S. E., Cameron, E. E., Pillus, L., and Boeke, J. D. (1995) The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability. Genes Dev, 9, 2888–2902
    • (1995) Genes Dev , vol.9 , pp. 2888-2902
    • Brachmann, C.B.1    Sherman, J.M.2    Devine, S.E.3    Cameron, E.E.4    Pillus, L.5    Boeke, J.D.6
  • 3
    • 33745520486 scopus 로고    scopus 로고
    • The sirtuins hst3 and Hst4p preserve genome integrity by controlling histone h3 lysine 56 deacetylation
    • Celic, I., Masumoto, H., Griffith, W. P., Meluh, P., Cotter, R. J., Boeke, J. D., and Verreault, A. (2006) The sirtuins hst3 and Hst4p preserve genome integrity by controlling histone h3 lysine 56 deacetylation. Curr Biol, 16, 1280–1289
    • (2006) Curr Biol , vol.16 , pp. 1280-1289
    • Celic, I.1    Masumoto, H.2    Griffith, W.P.3    Meluh, P.4    Cotter, R.J.5    Boeke, J.D.6    Verreault, A.7
  • 4
    • 47549105301 scopus 로고    scopus 로고
    • Acetylated lysine 56 on histone H3 drives chromatin assembly after repair and signals for the completion of repair
    • Chen, C. C., Carson, J. J., Feser, J., Tamburini, B., Zabaronick, S., Linger, J., and Tyler, J. K. (2008) Acetylated lysine 56 on histone H3 drives chromatin assembly after repair and signals for the completion of repair. Cell, 134, 231–243
    • (2008) Cell , vol.134 , pp. 231-243
    • Chen, C.C.1    Carson, J.J.2    Feser, J.3    Tamburini, B.4    Zabaronick, S.5    Linger, J.6    Tyler, J.K.7
  • 5
    • 0036889332 scopus 로고    scopus 로고
    • NuA4 subunit Yng2 function in intra-S-phase DNA damage response
    • Choy, J. S. and Kron, S. J. (2002) NuA4 subunit Yng2 function in intra-S-phase DNA damage response. Mol Cell Biol, 22, 8215–8225
    • (2002) Mol Cell Biol , vol.22 , pp. 8215-8225
    • Choy, J.S.1    Kron, S.J.2
  • 6
    • 65549113750 scopus 로고    scopus 로고
    • CBP/p300-mediated acetylation of histone H3 on lysine 56
    • Das, C., Lucia, M. S., Hansen, K. C., and Tyler, J. K. (2009) CBP/p300-mediated acetylation of histone H3 on lysine 56. Nature, 459, 113–117
    • (2009) Nature , vol.459 , pp. 113-117
    • Das, C.1    Lucia, M.S.2    Hansen, K.C.3    Tyler, J.K.4
  • 7
    • 0036307707 scopus 로고    scopus 로고
    • Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 a resolution
    • Davey, C. A., Sargent, D. F., Luger, K., Maeder, A. W., and Richmond, T. J. (2002) Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 a resolution. J Mol Biol, 319, 1097–1113
    • (2002) J Mol Biol , vol.319 , pp. 1097-1113
    • Davey, C.A.1    Sargent, D.F.2    Luger, K.3    Maeder, A.W.4    Richmond, T.J.5
  • 9
    • 34250820438 scopus 로고    scopus 로고
    • Chromatin dynamics and the preservation of genetic information
    • Downs, J. A., Nussenzweig, M. C., and Nussenzweig, A. (2007) Chromatin dynamics and the preservation of genetic information. Nature, 447, 951–958
    • (2007) Nature , vol.447 , pp. 951-958
    • Downs, J.A.1    Nussenzweig, M.C.2    Nussenzweig, A.3
  • 10
    • 33846818840 scopus 로고    scopus 로고
    • Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56
    • Driscoll, R., Hudson, A., and Jackson, S. P. (2007) Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56. Science, 315, 649–652
    • (2007) Science , vol.315 , pp. 649-652
    • Driscoll, R.1    Hudson, A.2    Jackson, S.P.3
  • 11
    • 15444373985 scopus 로고    scopus 로고
    • The DNA damage checkpoint response requires histone H2B ubiquitination by Rad6-Bre1 and H3 methylation by Dot1
    • Giannattasio, M., Lazzaro, F., Plevani, P., and Muzi-Falconi, M. (2005) The DNA damage checkpoint response requires histone H2B ubiquitination by Rad6-Bre1 and H3 methylation by Dot1. J Biol Chem, 280, 9879–9886
    • (2005) J Biol Chem , vol.280 , pp. 9879-9886
    • Giannattasio, M.1    Lazzaro, F.2    Plevani, P.3    Muzi-Falconi, M.4
  • 13
    • 33847076248 scopus 로고    scopus 로고
    • Chromatin challenges during DNA replication and repair
    • Groth, A., Rocha, W., Verreault, A., and Almouzni, G. (2007) Chromatin challenges during DNA replication and repair. Cell, 128, 721–733
    • (2007) Cell , vol.128 , pp. 721-733
    • Groth, A.1    Rocha, W.2    Verreault, A.3    Almouzni, G.4
  • 14
    • 33846796258 scopus 로고    scopus 로고
    • Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication
    • Han, J., Zhou, H., Horazdovsky, B., Zhang, K., Xu, R. M., and Zhang, Z. (2007) Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Science, 315, 653–655
    • (2007) Science , vol.315 , pp. 653-655
    • Han, J.1    Zhou, H.2    Horazdovsky, B.3    Zhang, K.4    Xu, R.M.5    Zhang, Z.6
  • 16
    • 27644467857 scopus 로고    scopus 로고
    • Insights into the role of histone H3 and histone H4 core modifiable residues in Saccharomyces cerevisiae
    • Hyland, E. M., Cosgrove, M. S., Molina, H., Wang, D., Pandey, A., Cottee, R. J., and Boeke, J. D. (2005) Insights into the role of histone H3 and histone H4 core modifiable residues in Saccharomyces cerevisiae. Mol Cell Biol, 25, 10060–10070
    • (2005) Mol Cell Biol , vol.25 , pp. 10060-10070
    • Hyland, E.M.1    Cosgrove, M.S.2    Molina, H.3    Wang, D.4    Pandey, A.5    Cottee, R.J.6    Boeke, J.D.7
  • 17
    • 0033529565 scopus 로고    scopus 로고
    • Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome
    • Kornberg, R. D. and Lorch, Y. (1999) Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome. Cell, 98, 285–294
    • (1999) Cell , vol.98 , pp. 285-294
    • Kornberg, R.D.1    Lorch, Y.2
  • 18
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides, T. (2007) Chromatin modifications and their function. Cell, 128, 693–705
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 19
    • 0033565609 scopus 로고    scopus 로고
    • Role of yeast SIR genes and mating type in directing DNA double-strand breaks to homologous and non-homologous repair paths
    • Lee, S. E., Paques, F., Sylvan, J., and Haber, J. E. (1999) Role of yeast SIR genes and mating type in directing DNA double-strand breaks to homologous and non-homologous repair paths. Curr Biol, 9, 767–770
    • (1999) Curr Biol , vol.9 , pp. 767-770
    • Lee, S.E.1    Paques, F.2    Sylvan, J.3    Haber, J.E.4
  • 20
    • 47549092547 scopus 로고    scopus 로고
    • Acetylation of histone H3 lysine 56 regulates replication-coupled nucleosome assembly
    • Li, Q., Zhou, H., Wurtele, H., Davies, B., Horazdovsky, B., Verreault, A., and Zhang, Z. (2008) Acetylation of histone H3 lysine 56 regulates replication-coupled nucleosome assembly. Cell, 134, 244–255
    • (2008) Cell , vol.134 , pp. 244-255
    • Li, Q.1    Zhou, H.2    Wurtele, H.3    Davies, B.4    Horazdovsky, B.5    Verreault, A.6    Zhang, Z.7
  • 21
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A 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 A 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
  • 22
    • 33745496607 scopus 로고    scopus 로고
    • Cell cycle and checkpoint regulation of histone H3 K56 acetylation by Hst3 and Hst4
    • Maas, N. L., Miller, K. M., Defazio, L. G., and Toczyski, D. P. (2006) Cell cycle and checkpoint regulation of histone H3 K56 acetylation by Hst3 and Hst4. Mol Cell, 23, 109–119
    • (2006) Mol Cell , vol.23 , pp. 109-119
    • Maas, N.L.1    Miller, K.M.2    Defazio, L.G.3    Toczyski, D.P.4
  • 23
    • 22444448143 scopus 로고    scopus 로고
    • A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response
    • Masumoto, H., Hawke, D., Kobayashi, R., and Verreault, A. (2005) A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response. Nature, 436, 294–298
    • (2005) Nature , vol.436 , pp. 294-298
    • Masumoto, H.1    Hawke, D.2    Kobayashi, R.3    Verreault, A.4
  • 24
    • 33751226576 scopus 로고    scopus 로고
    • Taking it off: Regulation of H3 K56 acetylation by Hst3 and Hst4
    • Miller, K. M., Maas, N. L., and Toczyski, D. P. (2006) Taking it off: regulation of H3 K56 acetylation by Hst3 and Hst4. Cell Cycle, 5, 2561–2565
    • (2006) Cell Cycle , vol.5 , pp. 2561-2565
    • Miller, K.M.1    Maas, N.L.2    Toczyski, D.P.3
  • 25
    • 34548569327 scopus 로고    scopus 로고
    • Diverse roles for histone H2A modifications in DNA damage response pathways in yeast
    • Moore, J. D., Yazgan, O., Ataian, Y., and Krebs, J. E. (2007) Diverse roles for histone H2A modifications in DNA damage response pathways in yeast. Genetics, 176, 15–25
    • (2007) Genetics , vol.176 , pp. 15-25
    • Moore, J.D.1    Yazgan, O.2    Ataian, Y.3    Krebs, J.E.4
  • 26
    • 30344444484 scopus 로고    scopus 로고
    • Histone acetylation by Trrap-Tip60 modulates loading of repair proteins and repair of DNA double-strand breaks
    • Murr, R., Loizou, J. I., Yang, Y. G., Cuenin, C., Li, H., Wang, Z. Q., and Herceg, Z. (2006) Histone acetylation by Trrap-Tip60 modulates loading of repair proteins and repair of DNA double-strand breaks. Nat Cell Biol, 8, 91–99
    • (2006) Nat Cell Biol , vol.8 , pp. 91-99
    • Murr, R.1    Loizou, J.I.2    Yang, Y.G.3    Cuenin, C.4    Li, H.5    Wang, Z.Q.6    Herceg, Z.7
  • 28
    • 0036888874 scopus 로고    scopus 로고
    • Histone H3 and the histone acetyltransferase Hat1p contribute to DNA double-strand break repair
    • Qin, S. and Parthun, M. R. (2002) Histone H3 and the histone acetyltransferase Hat1p contribute to DNA double-strand break repair. Mol Cell Biol, 22, 8353–8365
    • (2002) Mol Cell Biol , vol.22 , pp. 8353-8365
    • Qin, S.1    Parthun, M.R.2
  • 30
    • 33745790132 scopus 로고    scopus 로고
    • Chromatin remodelling: The industrial revolution of DNA around histones
    • Saha, A., Wittmeyer, J., and Cairns, B. R. (2006) Chromatin remodelling: the industrial revolution of DNA around histones. Nat Rev Mol Cell Biol, 7, 437–447
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 437-447
    • Saha, A.1    Wittmeyer, J.2    Cairns, B.R.3
  • 31
    • 21844436803 scopus 로고    scopus 로고
    • X-ray structure of a tetranucleo-some and its implications for the chromatin fibre
    • Schalch, T., Duda, S., Sargent, D. F., and Richmond, T. J. (2005) X-ray structure of a tetranucleo-some 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
  • 32
    • 38049115760 scopus 로고    scopus 로고
    • Hst3 is regulated by Mec1-dependent proteolysis and controls the S phase checkpoint and sister chromatid cohesion by deacetylating histone H3 at lysine 56
    • Thaminy, S., Newcomb, B., Kim, J., Gatbonton, T., Foss, E., Simon, J., and Bedalov, A. (2007) Hst3 is regulated by Mec1-dependent proteolysis and controls the S phase checkpoint and sister chromatid cohesion by deacetylating histone H3 at lysine 56. J Biol Chem, 282, 37805–37814
    • (2007) J Biol Chem , vol.282 , pp. 37805-37814
    • Thaminy, S.1    Newcomb, B.2    Kim, J.3    Gatbonton, T.4    Foss, E.5    Simon, J.6    Bedalov, A.7
  • 33
    • 77049121576 scopus 로고    scopus 로고
    • Screen for DNA-damage-responsive histone modifications identifies H3K9Ac and H3K56Ac in human cells
    • Tjeertes, J. V., Miller, K. M., and Jackson, S. P. (2009) Screen for DNA-damage-responsive histone modifications identifies H3K9Ac and H3K56Ac in human cells. EMBO J, 19, 6141–6149
    • (2009) EMBO J , vol.19 , pp. 6141-6149
    • Tjeertes, J.V.1    Miller, K.M.2    Jackson, S.P.3
  • 34
    • 0037077178 scopus 로고    scopus 로고
    • Dot1p modulates silencing in yeast by methylation of the nucleosome core
    • van Leeuwen, F., Gafken, P. R., and Gottschling, D. E. (2002) Dot1p modulates silencing in yeast by methylation of the nucleosome core. Cell, 109, 745–756
    • (2002) Cell , vol.109 , pp. 745-756
    • Van Leeuwen, F.1    Gafken, P.R.2    Gottschling, D.E.3
  • 35
    • 25444466892 scopus 로고    scopus 로고
    • Role of Dot1-dependent histone H3 methylation in G1 and S phase DNA damage checkpoint functions of Rad9
    • Wysocki, R., Javaheri, A., Allard, S., Sha, F., Cote, J., and Kron, S. J. (2005) Role of Dot1-dependent histone H3 methylation in G1 and S phase DNA damage checkpoint functions of Rad9. Mol Cell Biol, 25, 8430–8443
    • (2005) Mol Cell Biol , vol.25 , pp. 8430-8443
    • Wysocki, R.1    Javaheri, A.2    Allard, S.3    Sha, F.4    Cote, J.5    Kron, S.J.6
  • 36
    • 18844413266 scopus 로고    scopus 로고
    • Acetylation in histone H3 globular domain regulates gene expression in yeast
    • Xu, F., Zhang, K., and Grunstein, M. (2005) Acetylation in histone H3 globular domain regulates gene expression in yeast. Cell, 121, 375–385
    • (2005) Cell , vol.121 , pp. 375-385
    • Xu, F.1    Zhang, K.2    Grunstein, M.3
  • 37
    • 66749102871 scopus 로고    scopus 로고
    • Histone H3-K56 acetylation is important for genomic stability in mammals
    • Yuan, J., Pu, M., Zhang, Z., and Lou, Z. (2009) Histone H3-K56 acetylation is important for genomic stability in mammals. Cell Cycle, 8, 1747–1753.
    • (2009) Cell Cycle , vol.8 , pp. 1747-1753
    • Yuan, J.1    Pu, M.2    Zhang, Z.3    Lou, Z.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.