AI Article Synopsis
- TFIID is crucial for RNA polymerase II transcription but is complex and not well understood.
- The study focuses on the structure of TAF5, a key subunit of TFIID, revealing it has a distinct alpha-helical domain similar to factors that interact with RNA polymerase II.
- TAF5's N-terminal half can form a flexible dimer, which is important for assembling the larger TFIID complex.
Article 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-A resolution of the TAF5-NTD2 domain reveals an alpha-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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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1783120 | PMC |
| http://dx.doi.org/10.1073/pnas.0610297104 | DOI Listing |
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