Mediator Head module structure and functional interactions View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2010-03

AUTHORS

Gang Cai, Tsuyoshi Imasaki, Kentaro Yamada, Francesco Cardelli, Yuichiro Takagi, Francisco J Asturias

ABSTRACT

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. More... »

PAGES

273

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsmb.1757

DOI

http://dx.doi.org/10.1038/nsmb.1757

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1034423139

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/20154708


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