Histone chaperone RbAp48 interacts with histones H3–H4 and delivers them to a second histone chaperone, ASF1, to be assembled into new nucleosomes. These interactions are now investigated, revealing that RbAp48 binds H3–H4 heterodimers (but not tetramers) and causes conformational changes in their core fold. Moreover, an allosteric mechanism facilitates exchange of H3–H4 between RbAp48 and ASF1.
- Wei Zhang
- Marek Tyl
- Ernest D Laue
