title: Modulation of nucleosome-binding activity of FACT by poly(ADP-ribosyl)ation.
abstract: 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.
authors: Institute of Molecular Medicine, College of Medicine, National Taiwan University, Taipei, Taiwan.
authors: Jing-Yi
authors: JY
authors: Huang
authors: Wei-Hao
authors: WH
authors: Chen
authors: Ya-Ling
authors: YL
authors: Chang
authors: Hsiao-Ting
authors: HT
authors: Wang
authors: Wan-ting
authors: WT
authors: Chuang
authors: Sheng-Chung
authors: SC
authors: Lee