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A Protocol for Computer-Based Protein Structure and Function Prediction
Published on: November 3, 2011
Three-dimensional structure of the human TFIID-IIA-IIB complex
F Andel1, A G Ladurner, C Inouye
1Life Science Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
Science (New York, N.Y.)
|December 11, 1999
Summary
Researchers visualized the structure of human transcription factor IID (TFIID) and its complex with TFIIA and TFIIB. This reveals the TFIID-IIA-IIB complex
Area of Science:
- Molecular Biology
- Structural Biology
- Biochemistry
Background:
- Transcription factor IID (TFIID) is crucial for eukaryotic RNA polymerase II transcription initiation.
- TFIID interacts with TFIIA and TFIIB to form pre-initiation complexes at core promoters.
Purpose of the Study:
- To determine the high-resolution structure of human TFIID and the TFIID-TFIIA-TFIIB complex.
- To elucidate the spatial arrangement of these transcription factors within the initiation complex.
Main Methods:
- Electron microscopy (EM) for structural determination.
- Image analysis techniques to achieve 35 angstrom resolution.
- Antibody studies for protein localization within the complex.
Main Results:
- Human TFIID exhibits a trilobed, horseshoe-shaped structure.
- TFIIA and TFIIB bind to opposite lobes of TFIID, flanking a central cavity.
- The TATA-binding protein (TBP) is located centrally, between TFIIA and TFIIB, within the cavity likely involved in TATA DNA binding.
Conclusions:
- The study provides a detailed structural model of the TFIID-TFIIA-TFIIB complex.
- This structural information clarifies the organization of key components involved in eukaryotic transcription initiation.
- The findings offer insights into the mechanism of TATA DNA recognition by the transcription machinery.
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