NAD(+)-dependent modulation of chromatin structure and transcription by nucleosome binding properties of PARP-1

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PARP-1 is the most abundantly expressed member of a family of proteins that catalyze the transfer of ADPribose units from NAD(+) to target proteins. Herein, we describe previously uncharacterized nucleosome binding properties of PARP-1 that promote the formation of compact, transcriptionally repressed chromatin structures. PARP-1 binds in a specific manner to nucleosomes and modulates chromatin structure through NAD(+)-dependent automodification, without modifying core histories or promoting the disassembly of nucleosomes. The automodification activity of PARP-1 is potently stimulated by nucleosomes, causing the release of PARP-1 from chromatin. The NAD+-dependent activities of PARP-1 are reversed by PARG, a poly(ADPribose) glycohydrolase, and are inhibited by ATP. In vivo, PARP-1 incorporation is associated with transcriptionally repressed chromatin domains that are spatially distinct from both histone H1-repressed domains and actively transcribed regions. Thus, PARP-1 functions both as a structural component of chromatin and a modulator of chromatin structure through its intrinsic enzymatic activity.
Publisher
Cell Press
Issue Date
2004-12
Language
English
Article Type
Article
Keywords

POLY(ADP-RIBOSE) POLYMERASE; HISTONE; ATP; DNA; COMPLEX; CORE; METABOLISM; INITIATION; CATALYSIS; DOMAINS

Citation

CELL, v.119, no.6, pp.803 - 814

ISSN
0092-8674
DOI
10.1016/j.cell.2004.11.002
URI
http://hdl.handle.net/10203/83002
Appears in Collection
BS-Journal Papers(저널논문)
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