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Spark Plasma Sintering Apparatus Used for the Formation of Strontium Titanate Bicrystals
Published on: February 9, 2017
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Crystal structure of a transcription factor IIIB core interface ternary complex
Z Sean Juo1, George A Kassavetis, Jimin Wang
1Department of Molecular Biophysics & Biochemistry, Yale University, 266 Whitney Avenue, New Haven, Connecticut 06520-8114, USA. juo@csb.yale.edu
Nature
|March 28, 2003
Summary
Transcription factor IIIB (TFIIIB) assembly was structurally characterized. The study reveals the Brf1 domain
Area of Science:
- Molecular Biology
- Structural Biology
- Biochemistry
Background:
- Transcription factor IIIB (TFIIIB) is crucial for RNA polymerase III transcription.
- TFIIIB comprises TATA-binding protein (TBP), TFIIB-related factor (Brf1), and Bdp1.
- TFIIIB mediates polymerase recruitment and open complex formation at promoters.
Purpose of the Study:
- To elucidate the structural basis of TFIIIB assembly.
- To understand the interaction between Brf1, TBP, and promoter DNA.
Main Methods:
- X-ray crystallography
- Determination of a 2.95 Å resolution crystal structure of a ternary complex.
Main Results:
- The crystal structure reveals the core interface for TFIIIB assembly.
- The Brf1 homology domain II (residues 435–545) is key for TBP binding and Bdp1 incorporation.
- Specific interactions between Brf1 and TBP explain the complex's stability.
Conclusions:
- The structure provides atomic-level insights into TFIIIB complex formation.
- Understanding TFIIIB structure is vital for deciphering RNA polymerase III regulation.
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