4.8 Article

Mediator structure and conformation change

Journal

MOLECULAR CELL
Volume 81, Issue 8, Pages 1781-+

Publisher

CELL PRESS
DOI: 10.1016/j.molcel.2021.01.022

Keywords

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Funding

  1. US National Institutes of Health (NIH) [R01 GM049985]
  2. ShanghaiTech University, China
  3. NIH shared instrumentation grant [S10RR028096]

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Structural studies of Mediator reveal key amino acid residues and conformational changes that propagate across the entire protein, linking activator- and pol II-interacting regions. The structure provides insight into the role of Mediator as a universal adaptor for transcription control.
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.

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