Structural plasticity of histones H3-H4 facilitates their allosteric exchange between RbAp48 and ASF1 – Laue, Sobett and collaborator labs (2013)
Tuesday, January 1, 2013
Zhang, W., Tyl, M., Ward, R., Sobott, F., Maman, J., Murthy, A.S., Watson, A.A., Fedorov, O., Bowman, A., Owen-Hughes, T., El Mkami, H., Murzina, N.V., Norman, D.G., Laue, E.D.
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, however, crucial if we are to understand whether and how histone variants and post-translationally modified histones are inherited in an epigenetic manner. To this end we have studied the interaction of histones H3–H4 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 plays a central role in the assembly of new nucleosomes and we show here that the H3–H4 complex has a surprising structural plasticity, which is important for this exchange.
Nat Struct Mol Biol (2013) 20: 29-35. doi:10.1038/nsmb.2446