Structural Basis for the Recognition of Histone H4 by the Histone-Chaperone RbAp46
2008
How RbAp46 Recognizes Histone H4
publication
10 minutes
Evidence: high
Author Information
Author(s): Murzina Natalia V., Pei Xue-Yuan, Zhang Wei, Sparkes Mike, Vicente-Garcia Jose, Pratap J. Venkatesh, McLaughlin Stephen H., Ben-Shahar Tom Rolef, Verreault Alain, Luisi Ben F., Laue Ernest D.
Primary Institution: Department of Biochemistry, University of Cambridge
Hypothesis
How does RbAp46 interact with histone H4?
Conclusion
RbAp46 binds to histone H4 in a unique conformation that differs from its structure in nucleosomes.
Supporting Evidence
- RbAp46 and RbAp48 are essential for chromatin structure.
- The crystal structure shows how histone H4 binds to RbAp46.
- Histone H4 adopts a different conformation when bound to RbAp46.
- Mutations in RbAp46 disrupt its interaction with histone H4.
- RbAp46 can bind to histone H3/H4 complexes.
- Binding studies show RbAp46 interacts with histones H3 and H4.
- Histone H4 must unfold to interact with RbAp46.
Takeaway
RbAp46 is like a helper that grabs onto a part of histone H4, changing its shape so it can work better with other proteins.
Methodology
The study used crystallography to determine the structure of RbAp46 bound to histone H4.
Digital Object Identifier (DOI)
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