Modulation of nucleosome-binding activity of FACT by poly(ADP-ribosyl)ation.
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.
Mesh Terms:
Cell Cycle Proteins, Chromatin, Chromatin Assembly and Disassembly, DNA Damage, DNA-Binding Proteins, Hela Cells, High Mobility Group Proteins, Humans, Nucleosomes, Poly(ADP-ribose) Polymerases, Transcription Factors, Transcriptional Elongation Factors
Cell Cycle Proteins, Chromatin, Chromatin Assembly and Disassembly, DNA Damage, DNA-Binding Proteins, Hela Cells, High Mobility Group Proteins, Humans, Nucleosomes, Poly(ADP-ribose) Polymerases, Transcription Factors, Transcriptional Elongation Factors
Nucleic Acids Res.
Date: May. 10, 2006
PubMed ID: 16682447
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