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Analyzing and Building Nucleic Acid Structures with 3DNA
Published on: April 26, 2013
Solution structure of the first HMG box domain in human upstream binding factor
Yingqi Xu1, Wulin Yang, Jihui Wu
1Laboratory of Structural Biology, School of Life Science, University of Science and Technology of China, Hefei, Anhui 230026, Peoples Republic of China.
Biochemistry
|April 24, 2002
Summary
The first HMG box of human upstream binding factor (hUBF) adopts a specific L-shape structure. This structure is crucial for binding to ribosomal DNA promoters and understanding transcription regulation.
Area of Science:
- Molecular Biology
- Structural Biology
- Genetics
Background:
- Human upstream binding factor (hUBF) is a key transcription factor for RNA polymerase I.
- HMG box domains are DNA-binding motifs found in various proteins.
- The first HMG box of hUBF is critical for specific DNA binding to ribosomal promoters.
Purpose of the Study:
- To determine the three-dimensional structure of the first HMG box of hUBF.
- To understand the structural basis of hUBF's DNA binding specificity.
Main Methods:
- Multidimensional nuclear magnetic resonance (NMR) spectroscopy.
- (13)C,(15)N-labeled protein expression.
- Structural analysis of the hUBF HMG box 1 domain.
Main Results:
- The three-dimensional structure of hUBF HMG box 1 was determined in solution.
- The domain adopts a twisted L-shape comprising three alpha-helices.
- Conserved aromatic residues (F21, Y49, Y60) are vital for maintaining the protein's fold.
- The short arm of the domain is rigid, while the long arm is less rigid.
Conclusions:
- The determined structure provides insights into the specific DNA binding mechanism of hUBF.
- Structural flexibility of the long arm may play a role in DNA interaction.
- This study contributes to understanding the fundamental processes of ribosomal gene transcription.
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