Abstract
TFIID is an essential factor required for RNA polymerase II transcription but remains poorly understood because of its intrinsic complexity. Human TAF5, a 100-kDa subunit of general transcription factor TFIID, is an essential gene and plays a critical role in assembling the 1.2 MDa TFIID complex. We report here a structural analysis of the TAF5 protein. Our structure at 2.2-Å resolution of the TAF5-NTD2 domain reveals an α-helical domain with distant structural similarity to RNA polymerase II CTD interacting factors. The TAF5-NTD2 domain contains several conserved clefts likely to be critical for TFIID complex assembly. Our biochemical analysis of the human TAF5 protein demonstrates the ability of the N-terminal half of the TAF5 gene to form a flexible, extended dimer, a key property required for the assembly of the TFIID complex.
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Dates
Type | When |
---|---|
Created | 18 years, 7 months ago (Jan. 16, 2007, 10:18 p.m.) |
Deposited | 3 years, 4 months ago (April 12, 2022, 2:45 p.m.) |
Indexed | 2 months ago (June 28, 2025, 10:22 a.m.) |
Issued | 18 years, 7 months ago (Jan. 23, 2007) |
Published | 18 years, 7 months ago (Jan. 23, 2007) |
Published Online | 18 years, 7 months ago (Jan. 23, 2007) |
Published Print | 18 years, 7 months ago (Jan. 23, 2007) |
@article{Bhattacharya_2007, title={Structural analysis and dimerization potential of the human TAF5 subunit of TFIID}, volume={104}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.0610297104}, DOI={10.1073/pnas.0610297104}, number={4}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Bhattacharya, Suparna and Takada, Shinako and Jacobson, Raymond H.}, year={2007}, month=jan, pages={1189–1194} }