Nature structural & molecular biology, 2006-10, Vol.13 (10), p.895-901
2006
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- Autor(en) / Beteiligte
- Titel
- Structure and TBP binding of the Mediator head subcomplex Med8-Med18-Med20
- Ist Teil von
- Nature structural & molecular biology, 2006-10, Vol.13 (10), p.895-901
- Ort / Verlag
- United States: Nature Publishing Group
- Erscheinungsjahr
- 2006
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- 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.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 1545-9993eISSN: 1545-9985DOI: 10.1038/nsmb1143Titel-ID: cdi_proquest_miscellaneous_68933301
- Format
- –
- Schlagworte
- Amino Acid Sequence, Binding Sites, Cellular proteins, Dimerization, Gene expression, Mediator Complex, Models, Molecular, Molecular biology, Molecular Sequence Data, Mutation, Physiological aspects, Protein Binding, Protein Folding, Protein Structure, Tertiary, Ribonucleic acid, RNA, RNA Polymerase II - chemistry, RNA Polymerase II - metabolism, RNA polymerases, Saccharomyces cerevisiae Proteins - chemistry, Saccharomyces cerevisiae Proteins - metabolism, Sequence Homology, Amino Acid, Structure, Structure-Activity Relationship, TATA-Box Binding Protein - chemistry, TATA-Box Binding Protein - metabolism, Transcription Factors - chemistry, Transcription Factors - metabolism, Transcription, Genetic