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Mapping histone fold TAFs within yeast TFIID.
Claire Leurent1, Steven Sanders, Christine Ruhlmann
1Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, 1, rue Laurent Fries, BP163, 67400 Illkirch, France.
The EMBO Journal
|July 3, 2002
Summary
The TFIID complex
Area of Science:
- Molecular Biology
- Structural Biology
- Genetics
Background:
- TFIID is a crucial transcription factor regulating gene expression by RNA polymerase II.
- It comprises the TATA box-binding protein (TBP) and 14 TBP-associated factors (TAFs).
Purpose of the Study:
- To determine the three-dimensional structure of yeast TFIID (yTFIID).
- To investigate the molecular organization and TAF distribution within yTFIID.
Main Methods:
- Electron microscopy and image analysis were used to determine yTFIID structure at ~3 nm resolution.
- Immunolabelling experiments mapped the locations of histone fold domain (HFD)-containing TAFs.
Main Results:
- Yeast TFIID adopts a molecular clamp-like structure with three lobes.
- Nine HFD-containing TAFs are localized in three distinct substructures, with most in two lobes.
- This reveals a novel molecular organization of TFIID.
Conclusions:
- The determined structure provides insights into TFIID's role in gene regulation.
- The findings suggest that pairwise interactions between HFD-TAFs occur within the native complex.
- A novel organization of TFIID, with HFD-TAFs clustered in specific lobes, was uncovered.