Animal cells and systems

  • 제13권4호
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  • Pages.405-409
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  • 2009
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  • 1976-8354(pISSN)
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  • 2151-2485(eISSN)
한국통합생물학회 (The Korean Society for Integrative Biology)
권호 표지

BAF53 is Critical for Focus Formation of $\gamma$-H2AX in Response to DNA Damage

  • Park, Pan-Kyu (Department of Bioscience and Biotechnology and Protein Research Center for Bio-Industry, Hankuk University of Foreign Studies) ;
  • Kang, Dong-Hyun (Department of Bioscience and Biotechnology and Protein Research Center for Bio-Industry, Hankuk University of Foreign Studies) ;
  • Kwon, Hyock-Man (Department of Bioscience and Biotechnology and Protein Research Center for Bio-Industry, Hankuk University of Foreign Studies)
  • 발행 : 2009.12.31
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초록

When DNA double-strand breaks (DSBs) were induced in mammalian cells, many DNA damage response proteins are accumulated at damage sites to form nuclear foci called IR-induced foci. Although the formation of foci has been shown to promote repair efficiency, the structural organization of chromatin in foci remains obscure. BAF53 is an actin-related protein which is required for maintenance of chromosome territory. In this study, we show that the formation of IR-induced foci by $\gamma$-H2AX and 53BP1 were reduced when BAF53 is depleted, while DSB- activated ATM pathway and the phosphorylation of H2AX remains intact after DNA damage in BAF53 knockdown cells. We also found that DSB repair efficiency was largely compromised in BAF53 knockdown cells. These results indicate that BAF53 is critical for formation of foci by $\gamma$-H2AX decorated chromatin at damage sites and the structural organization of chromatin in foci is an important factor to achieve the maximum efficiency of DNA repair.

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참고문헌

  1. Banin S, Moyal L, Shieh S, Taya Y, Anderson CW, Chessa L, Smorodinsky NI, Prives C, Reiss Y, Shiloh Y, and Ziv Y (1998) Enhanced phosphorylation of p53 by ATM in response to DNA damage. Science 281: 1674-1677 https://doi.org/10.1126/science.281.5383.1674
  2. Bassing CH and Alt FW (2004) H2AX may function as an anchor to hold broken chromosomal DNA ends in close proximity. Cell Cycle 3:149-153 https://doi.org/10.4161/cc.3.2.689
  3. Belmont AS and Bruce K (1994)Visualization of G1 chromosomes: a folded, twisted, supercoiled chromonema model of interphase chromatid structure. J Cell Biol. 127: 287-302 https://doi.org/10.1083/jcb.127.2.287
  4. Celeste A, Petersen S, Romanienko PJ, Fernandez-Capetillo O, Chen HT, Sedelnikova OA, Reina-San-Martin B, Coppola V, Mellie E, Difilippantonio MJ, Redon C, Pilch DR, Olam A, Eckhaus M, Camerini-Otero RD, Tessarollo L, Livak F, Manova K, Bonner WM, Nussenzweig MC, and Nussenzweig A (2002) Genomic instability in mice lacking histone H2AX. Science 296: 922-927 https://doi.org/10.1126/science.1069398
  5. Choi EY, Park JA, Sung YR, Kwon H (2001) Generation of the Dominant-Negative Mutant of hArpN$\beta$: A Component of Human SWI/SNF Chromatin Remodeling Complex. Exp. Cell Res. 271; 180-188 https://doi.org/10.1006/excr.2001.5355
  6. Galarneau L, Nourani A, Boudreault AA, Zhang Y, Heliot L, Allard S, Savard J, Lane WS, Stillman DJ, and Cote J (2000) Multiple links between the NuA4 histone acetyltransferase complex and epigenetic control of transcription. Mol. Cell 5: 927-937 https://doi.org/10.1016/S1097-2765(00)80258-0
  7. Harata M, Oma Y, Mizuno S, Jiang YW, Stillman DJ, and Wintersberger U (1999) The nuclear actin-related protein of Saccharomyces cerevisiae, Act3p/Arp4, interacts with core histones. Mol. Biol. Cell 10: 2595-2605
  8. Kleckner N, Zickler D, Jones GH, Dekker J, Padmore R, Henle J, and Hutchinson J (2004) A mechanical basis for chromosome function. Proc. Natl. Acad. Sci. USA 101, 12592-12597 https://doi.org/10.1073/pnas.0402724101
  9. Koundrioukoff S, Polo S, and Almouzni G (2004) Interplay between chromatin and cell cycle checkpoints in the context of ATR/ATM-dependent checkpoints. DNA Repair 3: 969-978 https://doi.org/10.1016/j.dnarep.2004.03.010
  10. Lee JH, Chang SH, Shim JH, Lee JY, Yoshida M, Kwon H (2003) Cytoplasmic localization and nucleo-cytoplasmic shuttling of BAF53, a component of chromatin-modifying complexes. Mol. Cells 16; 78-83
  11. Lee K, Kang MJ, Kwon SJ, Kwon YK, Kim KW, Lim JH, and Kwon H (2007) Expansion of chromosome territories with chromatin decompaction in BAF53-depleted interphase cells. Mol. Biol. Cell. 18: 4013-4023 https://doi.org/10.1091/mbc.E07-05-0437
  12. Lim JS, Kim H, Choi YS, Kwon H, Shin KS, Joung I, Shin M, and Kwon YK (2008) Neuroprotective effects of berberine in neurodegeneration model rats induced by ibotenic acid. Animal Cells and Systems 12: 203-209 https://doi.org/10.1080/19768354.2008.9647174
  13. Lou Z, Minter-Dykhouse K, Franco S, Gostissa M, Rivera MA, Celeste A, Manis JP, van Deursen J, Nussenzweig A, Paull TT, Alt FW, and Chen J (2006) MDC1 maintains genomic stability by participating in the amplification of ATM-dependent DNA damage signals. Mol. Cell 21: 187-200 https://doi.org/10.1016/j.molcel.2005.11.025
  14. Matsuoka S, Rotman G, Ogawa A, Shiloh Y, Tamai K, and Elledge SJ (2000) Ataxia telangiectasia-mutated phosphorylates Chk2 in vivo and in vitro. Proc. Natl. Acad. Sci. USA 97: 10389-10394 https://doi.org/10.1073/pnas.190030497
  15. Muller WG, Rieder D, Kreth G, Cremer C, Trajanoski Z, and McNally JG (2004) Generic features of tertiary chromatin structure as detected in natural chromosomes. Mol. Cell Biol. 24: 9359-9370 https://doi.org/10.1128/MCB.24.21.9359-9370.2004
  16. Munkel C, Eils R, Dietzel S, Zink D, Mehring C, Wedemann G, Cremer T, and Langowski J (1999) Compartmentalization of interphase chromosomes observed in simulation and experiment. J Mol. Biol. 285: 1053-1065 https://doi.org/10.1006/jmbi.1998.2361
  17. Paull TT, Rogakou EP, Yamazaki V, Kirchgessner CU, Gellert M, and Bonner WM (2000) A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage. Curr. Biol. 10: 886-895 https://doi.org/10.1016/S0960-9822(00)00610-2
  18. Rando OJ, Zhao K, Janmey P, and Crabtree GR (2002) Phosphatidylinositol-dependent actin filament binding by the SWI/SNF-like BAF chromatin remodeling complex. Proc. Natl. Acad. Sci. USA 99: 2824-2829 https://doi.org/10.1073/pnas.032662899
  19. Rogakou EP, Boon C, Redon C, and Bonner WM (1999) Megabase chromatin domains involved in DNA doublestrand breaks in vivo. J Cell Biol. 146: 905-915 https://doi.org/10.1083/jcb.146.5.905
  20. Rogakou EP, Pilch DR, Orr AH, Ivanova VS, and Bonner WM (1998) DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139. J Biol Chem. 273: 5858-5868 https://doi.org/10.1074/jbc.273.10.5858
  21. Schardin M, Cremer T, Hager HD, and Lang M (1985) Specific staining of human chromosomes in Chinese hamster x man hybrid cell lines demonstrates interphase chromosome territories. Hum. Genet. 71: 281-287 https://doi.org/10.1007/BF00388452
  22. Shopland LS, Lynch CR, Peterson KA, Thornton K, Kepper N, Hase J, Stein S, Vincent S, Molloy KR, Kreth G, Cremer C, Bult CJ, and O'Brien TP (2006) Folding and organization of a contiguous chromosome region according to the gene distribution pattern in primary genomic sequence. J Cell Biol. 174: 27-38 https://doi.org/10.1083/jcb.200603083
  23. Sung YH, Choi EY, and Kwon H (2001) Identification of a nuclear protein ArpN as a component of human SWI/SNF complex and its selective association with a subset of active genes. Mol. Cells 11: 75-81
  24. van Attikum H and Gasser SM (2009) Crosstalk between histone modifications during the DNA damage response. Trends Cell Biol. 19: 207-217 https://doi.org/10.1016/j.tcb.2009.03.001
  25. Xie A, Puget N, Shim I, Odate S, Jarzyna I, Bassing CH, Alt FW, and Scully R (2004) Control of sister chromatid recombination by histone H2AX. Mol. Cell 16: 1017-1025 https://doi.org/10.1016/j.molcel.2004.12.007