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

http://www.ncbi.nlm.nih.gov/pubmed/16964259

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.

Pubmed ID: 16964259 RIS Download

Mesh terms: Amino Acid Sequence | Binding Sites | Dimerization | Mediator Complex | Models, Molecular | Molecular Sequence Data | Protein Binding | Protein Folding | Protein Structure, Tertiary | RNA Polymerase II | Saccharomyces cerevisiae Proteins | Sequence Homology, Amino Acid | Structure-Activity Relationship | TATA-Box Binding Protein | Transcription Factors | Transcription, Genetic

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