.png){kind=icon}
Return
Mediator Head module structure and functional interactions
.png){kind=icon}
OA
AI
DOI：10.1038/nsmb.1757.png)
.png){kind=icon}
.png){kind=icon}
Share.png){kind=icon}
Save
Abstract
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.
Keywords:
RNA-POLYMERASE-II
ELECTRON-MICROSCOPY
IN-VITRO
TRANSCRIPTION
INITIATION
COMPLEX
REQUIREMENT
SUBCOMPLEX
HOLOENZYME
SUBUNITS
AI Summary
Key information extracted from the uploaded paper, including a brief overview, abstract, background, key highlights, visual analysis, and future outlook.
Journal
N
IF:
10.1
Papers:
4.8K
Citations:
2.8W
Organization
Cited Papers
ShareSaveIdentification, structure, and functional requirement of the Mediator submodule Med7N/31.png)
EMBO JOURNALOAAI
EMBO JOURNALIF8.3
OAAIShareSavePolymorphisms of the Endothelin-1 Gene Associate with Hypertension in Patients with Rheumatoid ArthritisEndothelium
EndotheliumIF0
PREAI
ShareSaveAn electrophysiological and immunohistochemical study of the hippocampus of the reeler mutant mouse
PREAI
ShareSaveShareSaveShareSave
View more