首页    期刊浏览 2024年07月19日 星期五
登录注册

文章基本信息

  • 标题:Poly(ADP-ribosyl)ation directs recruitment and activation of an ATP-dependent chromatin remodeler
  • 本地全文:下载
  • 作者:Aaron J. Gottschalk ; Gyula Timinszky ; Stephanie E. Kong
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:2009
  • 卷号:106
  • 期号:33
  • 页码:13770-13774
  • DOI:10.1073/pnas.0906920106
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:Posttranslational modifications play a key role in recruiting chromatin remodeling and modifying enzymes to specific regions of chromosomes to modulate chromatin structure. Alc1 (amplified in liver cancer 1), a member of the SNF2 ATPase superfamily with a carboxy-terminal macrodomain, is encoded by an oncogene implicated in the pathogenesis of hepatocellular carcinoma. Here we show that Alc1 interacts transiently with chromatin-associated proteins, including histones and the poly(ADP-ribose) polymerase Parp1. Alc1 ATPase and chromatin remodeling activities are strongly activated by Parp1 and its substrate NAD and require an intact macrodomain capable of binding poly(ADP-ribose). Alc1 is rapidly recruited to nucleosomes in vitro and to chromatin in cells when Parp1 catalyzes PAR synthesis. We propose that poly(ADP-ribosyl)ation of chromatin-associated Parp1 serves as a mechanism for targeting a SNF2 family remodeler to chromatin.
  • 关键词:Alc1 ; chromatin remodeling enzyme ; macrodomain ; poly-(ADP-ribose) polymerase ; Snf2-like ATPase
国家哲学社会科学文献中心版权所有