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Journal Article

Structure and TBP binding of the Mediator head subcomplex Med8–Med18–Med20.

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Cramer,  P.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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1936510_Suppl_1.pdf
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1936510_Suppl_2.pdf
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(Supplementary material), 36KB

1936510_Suppl_5.pdf
(Supplementary material), 31KB

Citation

Larivière, L., Geiger, S., Hoeppner, S., Röther, S., Strässer, K., & Cramer, P. (2006). Structure and TBP binding of the Mediator head subcomplex Med8–Med18–Med20. Nature Structural and Molecular Biology, 13(10), 895-901. doi:10.1038/nsmb1143.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0015-8072-7
Abstract
The Mediator head module stimulates basal RNA polymerase II (Pol II) transcription and enables transcriptional regulation. Here we show that the head subunits Med8, Med18 and Med20 form a subcomplex (Med8/18/20) with two submodules. The highly conserved N-terminal domain of Med8 forms one submodule that binds the TATA box–binding protein (TBP) in vitro and is essential in vivo. The second submodule consists of the C-terminal region of Med8 (Med8C), Med18 and Med20. X-ray analysis of this submodule reveals that Med18 and Med20 form related beta-barrel folds. A conserved putative protein-interaction face on the Med8C/18/20 submodule includes sites altered by srb mutations, which counteract defects resulting from Pol II truncation. Our results and published data support a positive role of the Med8/18/20 subcomplex in initiation-complex formation and suggest that the Mediator head contains a multipartite TBP-binding site that can be modulated by transcriptional activators.