Journal article

Publication year: 2006

Pages: 895-901

Journal: Nature Structural & Molecular Biology

Volume number: 13

Issue number: 10

ISSN: 1545-9985

DOI Link: https://doi.org/10.1038/nsmb1143

Publisher: Nature Research

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.

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

APA Citation style: 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 & Molecular Biology. 13(10), 895-901. https://doi.org/10.1038/nsmb1143