Ernest Laue's goup and their collaborators have published a paper in Nature Structural and Molecular Biology "Structural plasticity of histones H3-H4 facilitates their allosteric exchange between RbAp48 and ASF1". The mechanisms by which histones are disassembled and reassembled into nucleosomes and chromatin structure during DNA replication, repair and transcription are poorly understood. A better understanding of the processes involved is vital to understanding how histone variants and post-translationally modified histones are inherited in an epigenetic manner. The researchers studied the interaction of the histone H3-H4 complex with the human retinoblastoma-associated protein RbAp48 and their exchange with a second histone chaperone, anti-silencing function protein 1 (ASF1). Exchange of histones H3-H4 between these two histone chaperones has a central role in the assembly of new nucleosomes. They showed that the H3-H4 complex has an unexpected structural plasticity, which is important for this exchange.