De novo phosphorylation of H2AX by WSTF regulates transcription-coupled homologous recombination repair
作者： Jae-Hoon Ji , Sunwoo Min , Sunyoung Chae , Geun-Hyoung Ha , Yonghyeon Kim
DOI: 10.1093/NAR/GKZ309
关键词: DNA 、 Transcription (biology) 、 Biology 、 RNA polymerase II 、 Homologous recombination 、 Chromatin 、 Transcription factor 、 Cell biology 、 RAD51 、 DNA damage
摘要: Histone H2AX undergoes a phosphorylation switch from pTyr142 (H2AX-pY142) to pSer139 (γH2AX) in the DNA damage response (DDR); however, functional role of H2AX-pY142 remains elusive. Here, we report new layer regulation involving transcription-coupled DDR. We found that constitutive generated by Williams-Beuren syndrome transcription factor (WSTF) interacts with RNA polymerase II (RNAPII) and is associated RNAPII-mediated active proliferating cells. Also, removal pre-existing ATM-dependent EYA1/3 phosphatases disrupts this association requires for transcriptional silencing at transcribed sites. The following recovery via translocation WSTF lesions facilitates homologous recombination (TC-HR) G1 phase, whereby RAD51 loading, but not RPA32, utilizes RNAPII-dependent transcripts as donor templates. propose WSTF-H2AX-RNAPII axis regulates TC-HR repair maintain genome integrity.
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mendeley.com参考文章(37)
Jia Fang, Taiping Chen, Brian Chadwick, En Li, Yi Zhang, Ring1b-mediated H2A Ubiquitination Associates with Inactive X Chromosomes and Is Involved in Initiation of X Inactivation Journal of Biological Chemistry. ,vol. 279, pp. 52812- 52815 ,(2004) , 10.1074/JBC.C400493200
Mads Daugaard, Annika Baude, Kasper Fugger, Lou Klitgaard Povlsen, Halfdan Beck, Claus Storgaard Sørensen, Nikolaj H T Petersen, Poul H B Sorensen, Claudia Lukas, Jiri Bartek, Jiri Lukas, Mikkel Rohde, Marja Jäättelä, LEDGF (p75) promotes DNA-end resection and homologous recombination Nature Structural & Molecular Biology. ,vol. 19, pp. 803- 810 ,(2012) , 10.1038/NSMB.2314
Peter J. Cook, Bong Gun Ju, Francesca Telese, Xiangting Wang, Christopher K. Glass, Michael G. Rosenfeld, Tyrosine dephosphorylation of H2AX modulates apoptosis and survival decisions Nature. ,vol. 458, pp. 591- 596 ,(2009) , 10.1038/NATURE07849
Harihar Basnet, Xue B. Su, Yuliang Tan, Jill Meisenhelder, Daria Merkurjev, Kenneth A. Ohgi, Tony Hunter, Lorraine Pillus, Michael G. Rosenfeld, Tyrosine phosphorylation of histone H2A by CK2 regulates transcriptional elongation Nature. ,vol. 516, pp. 267- 271 ,(2014) , 10.1038/NATURE13736
Jiri Lukas, Claudia Lukas, Jiri Bartek, More than just a focus: The chromatin response to DNA damage and its role in genome integrity maintenance Nature Cell Biology. ,vol. 13, pp. 1161- 1169 ,(2011) , 10.1038/NCB2344
Davide F.V. Corona, John W. Tamkun, Multiple roles for ISWI in transcription, chromosome organization and DNA replication. Biochimica et Biophysica Acta. ,vol. 1677, pp. 113- 119 ,(2004) , 10.1016/J.BBAEXP.2003.09.018
Sara S Dirscherl, Jocelyn E Krebs, Functional diversity of ISWI complexes Biochemistry and Cell Biology. ,vol. 82, pp. 482- 489 ,(2004) , 10.1139/O04-044
William M. Bonner, Christophe E. Redon, Jennifer S. Dickey, Asako J. Nakamura, Olga A. Sedelnikova, Stéphanie Solier, Yves Pommier, γH2AX and cancer Nature Reviews Cancer. ,vol. 8, pp. 957- 967 ,(2008) , 10.1038/NRC2523
Andrew Xiao, Haitao Li, David Shechter, Sung Hee Ahn, Laura A. Fabrizio, Hediye Erdjument-Bromage, Satoko Ishibe-Murakami, Bin Wang, Paul Tempst, Kay Hofmann, Dinshaw J. Patel, Stephen J. Elledge, C. David Allis, WSTF regulates the H2A.X DNA damage response via a novel tyrosine kinase activity Nature. ,vol. 457, pp. 57- 62 ,(2009) , 10.1038/NATURE07668
Li Lan, Ayako Ui, Satoshi Nakajima, Kotomi Hatakeyama, Mikiko Hoshi, Reiko Watanabe, Susan M. Janicki, Hideaki Ogiwara, Takashi Kohno, Shin-ichiro Kanno, Akira Yasui, The ACF1 Complex Is Required for DNA Double-Strand Break Repair in Human Cells Molecular Cell. ,vol. 40, pp. 976- 987 ,(2010) , 10.1016/J.MOLCEL.2010.12.003