Article
A critical role in structure-specific DNA binding for the acetylatable lysine residues in HMGB1.
The Biochemical journal - 1 May 2008
Assenberg René, Webb Michelle, Connolly Edward, Stott Katherine, Watson Matthew, Hobbs Josie, Thomas Jean O
Abstract excerpt
The structure-specific DNA-binding protein HMGB1 (high-mobility group protein B1) which comprises two tandem HMG boxes (A and B) and an acidic C-terminal tail, is acetylated in vivo at Lys(2) and Lys(11) in the A box. Mutation to alanine of both residues in the isolated A domain, which has a strong preference for pre-bent DNA, abolishes binding to four-way junctions and 88 bp DNA minicircles. The same mutations...
Topics
- Acetylation
- Amino Acid Motifs
- Amino Acid Sequence
- CREB-Binding Protein
- Circular Dichroism
- DNA
- HMGB1 Protein
- Lysine
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Nuclear Magnetic Resonance, Biomolecular
- Nucleic Acid Conformation
- Protein Binding