首页    期刊浏览 2024年11月08日 星期五
登录注册

文章基本信息

  • 标题:Functional architecture of the Reb1-Ter complex of Schizosaccharomyces pombe
  • 本地全文:下载
  • 作者:Rahul Jaiswal ; Malay Choudhury ; Shamsu Zaman
  • 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:2016
  • 卷号:113
  • 期号:16
  • 页码:E2267-E2276
  • DOI:10.1073/pnas.1525465113
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:Reb1 of Schizosaccharomyces pombe represents a family of multifunctional proteins that bind to specific terminator sites (Ter) and cause polar termination of transcription catalyzed by RNA polymerase I (pol I) and arrest of replication forks approaching the Ter sites from the opposite direction. However, it remains to be investigated whether the same mechanism causes arrest of both DNA transactions. Here, we present the structure of Reb1 as a complex with a Ter site at a resolution of 2.7 Å. Structure-guided molecular genetic analyses revealed that it has distinct and well-defined DNA binding and transcription termination (TTD) domains. The region of the protein involved in replication termination is distinct from the TTD. Mechanistically, the data support the conclusion that transcription termination is not caused by just high affinity Reb1-Ter protein–DNA interactions. Rather, protein–protein interactions between the TTD with the Rpa12 subunit of RNA pol I seem to be an integral part of the mechanism. This conclusion is further supported by the observation that double mutations in TTD that abolished its interaction with Rpa12 also greatly reduced transcription termination thereby revealing a conduit for functional communications between RNA pol I and the terminator protein.
  • 关键词:crystal structure ; RNA polymerase I ; transcription termination ; protein–DNA interaction ; replication termination
国家哲学社会科学文献中心版权所有