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Crystal structure of a yeast TBP/TATA-box complex
1Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510.
Nature
|October 7, 1993
Summary
The crystal structure reveals how yeast TATA-binding protein (TBP) binds DNA. Yeast TBP severely bends TATA box DNA, creating a unique interface that alters DNA's normal structure.
Area of Science:
- Structural Biology
- Molecular Biology
- Biochemistry
Background:
- The TATA box is a crucial DNA sequence in gene promoters.
- TATA-binding protein (TBP) recognizes and binds the TATA box to initiate transcription.
- Understanding the TBP-TATA box interaction at the atomic level is key to deciphering gene regulation.
Purpose of the Study:
- To elucidate the atomic details of the TATA-box DNA complex with yeast TBP.
- To investigate the structural consequences of TBP binding on TATA box DNA conformation.
Main Methods:
- X-ray crystallography was used to determine the crystal structure of the complex.
- The structure was solved at a resolution of 2.5 Angstroms.
Main Results:
- The crystal structure reveals that yeast TBP binds the TATA box on its concave surface.
- TBP binding induces severe bending of the TATA box DNA towards the major groove.
- This severe bending results in an underwound DNA helix with a shallow minor groove, forming a hydrophobic interface with TBP.
- The DNA undergoes a positive writhe, significantly altering the trajectory of the flanking DNA.
Conclusions:
- Yeast TBP binding dramatically distorts the TATA box DNA structure.
- The observed DNA deformation creates a specific interface crucial for TBP recognition and potentially for downstream regulatory events.
- The findings provide critical insights into the mechanism of transcription initiation mediated by TBP.