Abstract
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.
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Dates
Type | When |
---|---|
Created | 23 years ago (July 27, 2002, 5:42 a.m.) |
Deposited | 1 year, 7 months ago (Jan. 13, 2024, 5:32 a.m.) |
Indexed | 3 weeks, 1 day ago (July 30, 2025, 10:06 a.m.) |
Issued | 25 years, 8 months ago (Dec. 10, 1999) |
Published | 25 years, 8 months ago (Dec. 10, 1999) |
Published Print | 25 years, 8 months ago (Dec. 10, 1999) |
@article{Andel_1999, title={Three-Dimensional Structure of the Human TFIID-IIA-IIB Complex}, volume={286}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.286.5447.2153}, DOI={10.1126/science.286.5447.2153}, number={5447}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Andel, Frank and Ladurner, Andreas G. and Inouye, Carla and Tjian, Robert and Nogales, Eva}, year={1999}, month=dec, pages={2153–2156} }