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Science 10 December 1999:
Vol. 286. no. 5447, pp. 2153 - 2156
DOI: 10.1126/science.286.5447.2153
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Reports

Three-Dimensional Structure of the Human TFIID-IIA-IIB Complex

Frank Andel III, 1 Andreas G. Ladurner, 3 Carla Inouye, 3 Robert Tjian, 2 Eva Nogales 13*

The multisubunit transcription factor IID (TFIID) is an essential component of the eukaryotic RNA polymerase II machinery that works in concert with TFIIA (IIA) and TFIIB (IIB) to assemble initiation complexes at core eukaryotic promoters. Here the structures of human TFIID and the TFIID-IIA-IIB complex that were obtained by electron microscopy and image analysis to 35 angstrom resolution are presented. TFIID is a trilobed, horseshoe-shaped structure, with TFIIA and TFIIB bound on opposite lobes and flanking a central cavity. Antibody studies locate the TATA-binding protein (TBP) between TFIIA and TFIIB at the top of the cavity that most likely encompasses the TATA DNA binding region of the supramolecular complex.

1 Life Science Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
2 Howard Hughes Medical Institute,
3 Molecular and Cell Biology Department, University of California, Berkeley, CA 94720, USA.
*   To whom correspondence should be addressed. E-mail: enogales{at}lbl.gov

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