Related Experiment Videos
Crystal structure of a TFIIB-TBP-TATA-element ternary complex
D B Nikolov1, H Chen, E D Halay
1Laboratories of Molecular Biophysics, Rockefeller University, New York, New York 10021, USA.
Nature
|September 14, 1995
Summary
The crystal structure of transcription factor IIB (TFIIB) bound to TBP and DNA reveals how TFIIB recognizes the TBP-DNA complex. This structure provides insights into fixing the transcription start site and interactions with other factors.
Area of Science:
- Molecular Biology
- Structural Biology
- Genetics
Background:
- Transcription factor IIB (TFIIB) and TATA box-binding protein (TBP) are essential for gene transcription initiation.
- Understanding the structural basis of their interaction with DNA is crucial for deciphering gene regulation.
Purpose of the Study:
- To determine the high-resolution crystal structure of the TFIIB/TBP/TATA-element ternary complex.
- To elucidate the molecular interactions governing the recognition of the TBP-DNA complex by TFIIB.
Main Methods:
- X-ray crystallography at 2.7 A resolution.
- Analysis of protein-protein and protein-DNA interactions within the ternary complex.
Main Results:
- The crystal structure of the TFIIB/TBP/TATA-element ternary complex was determined.
- Core TFIIB, structurally similar to cyclin A, interacts with the preformed TBP-DNA complex via specific protein-protein and protein-DNA contacts.
- The amino-terminal domain of TFIIB is positioned to define the transcription start site.
Conclusions:
- The TFIIB/TBP/TATA complex structure reveals key interactions for transcription initiation.
- TFIIB plays a critical role in stabilizing the pre-initiation complex and positioning the transcription start site.
- The structure suggests potential interaction sites for other transcription factors and coactivators.