Three-dimensional structures of the TAFII-containing complexes TFIID and TFTC |
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Authors: | Brand M Leurent C Mallouh V Tora L Schultz P |
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Institution: | Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/Université Louis Pasteur, Boite Postale 163, F-67404 Illkirch cedex, Communauté Urbaine de Strasbourg, France. |
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Abstract: | 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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