Title
Structural plasticity of histones H3-H4 facilitates their allosteric exchange between RbAp48 and ASF1
Author
Faculty/Department
Faculty of Sciences. Chemistry
Publication type
article
Publication
New York, N.Y. ,
Subject
Physics
Chemistry
Biology
Human medicine
Source (journal)
Nature structural & molecular biology. - New York, N.Y., 2004, currens
Volume/pages
20(2013) :1 , p. 29-U43
ISSN
1545-9993
1545-9985
ISI
000313072400007
Carrier
E
Target language
English (eng)
Full text (Publishers DOI)
Affiliation
University of Antwerp
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.
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