返回
Mediator Head module structure and functional interactions
DOI:10.1038/nsmb.1757.png)
摘要
En 中文
We used single-particle electron microscopy to characterize the structure and subunit organization of the Mediator Head module that controls Mediator-RNA polymerase II (RNAPII) and Mediator-promoter interactions. The Head module adopts several conformations differing in the position of a movable jaw formed by the Med18-Med20 subcomplex. We also characterized, by structural, biochemical and genetic means, the interactions of the Head module with TATA-binding protein (TBP) and RNAPII subunits Rpb4 and Rpb7. TBP binds near the Med18-Med20 attachment point and stabilizes an open conformation of the Head module. Rpb4 and Rpb7 bind between the Head jaws, establishing contacts essential for yeast-cell viability. These results, and consideration of the structure of the Mediator-RNAPII holoenzyme, shed light on the stabilization of the pre-initiation complex by Mediator and suggest how Mediator might influence initiation by modulating polymerase conformation and interaction with promoter DNA.
Keyword:
RNA-POLYMERASE-II
ELECTRON-MICROSCOPY
IN-VITRO
TRANSCRIPTION
INITIATION
COMPLEX
REQUIREMENT
SUBCOMPLEX
HOLOENZYME
SUBUNITS
AI总结
对已上传原文的论文进行重点信息的提取,主要内容包括:简要概述、研究摘要、背景介绍、关键亮点、图文解析、展望与总结。
期刊
N
IF:
10.1
论文数:
4.8K
被引数:
2.8W
机构
引用论文
Identification, structure, and functional requirement of the Mediator submodule Med7N/31
EMBO JOURNAL
IF8.3
Polymorphisms of the Endothelin-1 Gene Associate with Hypertension in Patients with Rheumatoid Arthritis
Endothelium
IF0
UCSF chimera - A visualization system for exploratory research and analysisUCSF chimera-用于探索性研究和分析的可视化系统

