Structural Plasticity of Histones H3-H4 Facilitates Their Allosteric Exchange Between RbAp48 and ASF1

Zhang, W, et al., 20(1), 29-35, Nat Struct Mol Biol, 2013

Interactions of the Histone H3-H4 complex with the histone chaperone proteins RbAp48 and ASF-1 were studied. RbAp48 was shown to bind the histone H3-H4 complex as a heterodimer, not a heterotetramer. Major conformational changes were shown to take place in the core fold of H3-H4 complex upon binding to RpAp48, indicating an allosteric mechanism facilitating the exchange of H3-H4 complex between the two chaperones. The Octet RED384 system and Streptavidin biosensors were used to characterize RbAp48 and ASF1 binding to acetylated histone H4.

Read More