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Nucleic Acids Research 2006 34(8):2398-2407; doi:10.1093/nar/gkl241
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Published online 8 May 2006

© The Author 2006. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions@oxfordjournals.org

Article

Modulation of nucleosome-binding activity of FACT by poly(ADP-ribosyl)ation

Jing-Yi Huang, Wei-Hao Chen1,4, Ya-Ling Chang, Hsiao-Ting Wang, Wan-ting Chuang and Sheng-Chung Lee1,2,3,*

1 Institute of Molecular Medicine, College of Medicine, National Taiwan University Taipei, Taiwan 2 Institute of Clinical Medicine, College of Medicine, National Taiwan University Taipei, Taiwan 3 Institute of Biological Chemistry, Academia Sinica Taipei, Taiwan 4 Institute of Atomic and Molecular Sciences, Academia Sinica Taipei, Taiwan

*To whom correspondence should be addressed. Tel: 886 2 2312 3456, ext. 2982; Fax: 886 2 2321 0977; Email: slee{at}ntu.edu.tw

Received December 16, 2005. Revised January 12, 2006. Accepted March 29, 2006.

Chromatin-modifying factors play key roles in transcription, DNA replication and DNA repair. Post-translational modification of these proteins is largely responsible for regulating their activity. The FACT (facilitates chromatin transcription) complex, a heterodimer of hSpt16 and SSRP1, is a chromatin structure modulator whose involvement in transcription and DNA replication has been reported. Here we show that nucleosome binding activity of FACT complex is regulated by poly(ADP-ribosyl)ation. hSpt16, the large subunit of FACT, is poly(ADP-ribosyl)ated by poly(ADP-ribose) polymerase-1 (PARP-1) resulting from physical interaction between these two proteins. The level of hSpt16 poly(ADP-ribosyl)ation is elevated after genotoxic treatment and coincides with the activation of PARP-1. The enhanced hSpt16 poly(ADP-ribosyl)ation level correlates with the dissociation of FACT from chromatin in response to DNA damage. Our findings suggest that poly(ADP-ribosyl)ation of hSpt16 by PARP-1 play regulatory roles for FACT-mediated chromatin remodeling.


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