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Three-dimensional structures of the TAFII-containing complexes TFIID and TFTC

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Brand, Marjorie | Leurent, Claire | Mallouh, Véronique | Tora, Laszlo | Schultz, Patrick

Edité par CCSD ; American Association for the Advancement of Science (AAAS) -

International audience. TBP (TATA-binding protein)-associated factors (TAF(II)s) are components of large multiprotein complexes such as TFIID, TFTC, STAGA, PCAF/GCN5, and SAGA, which play a key role in the regulation of gene expression by RNA polymerase II. The structures of TFIID and TFTC have been determined at 3.5-nanometer resolution by electron microscopy and digital image analysis of single particles. Human TFIID resembles a macromolecular clamp that contains four globular domains organized around a solvent-accessible groove of a size suitable to bind DNA. TFTC is larger and contains five domains, four of which are similar to TFIID.

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