Structural basis of histone H4 recognition by p55
Ji-Joon Song1, Joseph D Garlick, Robert E Kingston
1Department of Molecular Biology, Massachusetts General Hospital, Boston, Massachusetts 02114, USA.
Genes & Development
|April 30, 2008
Summary
The crystal structure reveals how Drosophila p55, a WD40 repeat protein, binds histone H4 peptides. This binding pocket is crucial for the function of p55-containing chromatin-modifying complexes.
Area of Science:
- Biochemistry
- Structural Biology
- Genetics
Background:
- p55 is a component of chromatin-modifying complexes.
- p55 is known to bind histones.
Purpose of the Study:
- Determine the crystal structure of Drosophila p55 bound to a histone H4 peptide.
- Investigate the binding mechanism and functional importance of the p55-histone interaction.
Main Methods:
- X-ray crystallography to obtain the structure of p55 bound to histone H4 peptide.
- Biochemical reconstitution experiments to assess the functional importance of the binding pocket.
Main Results:
- The crystal structure reveals p55's WD40 beta-propeller domain binds the N-terminal helix of histone H4.
- The binding pocket on p55 requires an altered histone H4 fold for interaction.
- Reconstitution experiments confirm the binding pocket's importance for p55-containing complex function.
Conclusions:
- WD40 repeat proteins utilize diverse surfaces for histone binding and modification.
- The structure provides insights into the mechanism of histone recognition by p55.
- This study highlights the adaptability of histone modification complexes.
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