Molecular Cell
Volume 81, Issue 8, 15 April 2021, Pages 1781-1788.e4
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Article
Mediator structure and conformation change

https://doi.org/10.1016/j.molcel.2021.01.022Get rights and content
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Highlights

  • A near atomic resolution cryo-EM structure of the Mediator complex was determined

  • The structure reveals the major activator-binding regions

  • Activator-binding and pol II-interacting regions are conformationally coupled

Summary

Mediator is a universal adaptor for transcription control. It serves as an interface between gene-specific activator or repressor proteins and the general RNA polymerase II (pol II) transcription machinery. Previous structural studies revealed a relatively small part of Mediator and none of the gene activator-binding regions. We have determined the cryo-EM structure of the Mediator at near-atomic resolution. The structure reveals almost all amino acid residues in ordered regions, including the major targets of activator proteins, the Tail module, and the Med1 subunit of the Middle module. Comparison of Mediator structures with and without pol II reveals conformational changes that propagate across the entire Mediator, from Head to Tail, coupling activator- and pol II-interacting regions.

Keywords

transcription
Mediator
activator
pol II
cryo-EM
structure
conformation change

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