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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 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, and we show here that the H3-H4 complex has an unexpected structural plasticity, which is important for this exchange.

Original publication

DOI

10.1038/nsmb.2446

Type

Journal article

Journal

Nat Struct Mol Biol

Publication Date

01/2013

Volume

20

Pages

29 - 35

Keywords

Animals, Cell Cycle Proteins, Chromatin, Chromatin Assembly and Disassembly, DNA, DNA Replication, Histone Chaperones, Histones, Humans, Nucleosomes, Protein Binding, Protein Multimerization, Retinoblastoma-Binding Protein 4