期刊
CELL
卷 119, 期 6, 页码 803-814出版社
CELL PRESS
DOI: 10.1016/j.cell.2004.11.002
关键词
-
资金
- NIDDK NIH HHS [R01 DK069710, DK069710, DK58110] Funding Source: Medline
- NIGMS NIH HHS [GM25232] Funding Source: Medline
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据