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- Title
Structural plasticity of histones H3-H4 facilitates their allosteric exchange between RbAp48 and ASF1.
- Authors
Zhang, Wei; Tyl, Marek; Ward, Richard; Sobott, Frank; Maman, Joseph; Murthy, Andal S; Watson, Aleksandra A; Fedorov, Oleg; Bowman, Andrew; Owen-Hughes, Tom; El Mkami, Hassane; Murzina, Natalia V; Norman, David G; Laue, Ernest D
- Abstract
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.
- Subjects
HISTONES; ALLOSTERIC enzymes; RETINOBLASTOMA; DNA replication; MATERIAL plasticity
- Publication
Nature Structural & Molecular Biology, 2013, Vol 20, Issue 1, p29
- ISSN
1545-9993
- Publication type
Article
- DOI
10.1038/nsmb.2446