Publication
Title
Structural plasticity of histones H3-H4 facilitates their allosteric exchange between RbAp48 and ASF1
Author
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.
Language
English
Source (journal)
Nature structural & molecular biology. - New York, N.Y., 2004, currens
Publication
New York, N.Y. : 2013
ISSN
1545-9993 [print]
1545-9985 [online]
Volume/pages
20:1(2013), p. 29-U43
ISI
000313072400007
Full text (Publishers DOI)
UAntwerpen
Faculty/Department
Research group
Publication type
Subject
Affiliation
Publications with a UAntwerp address
External links
Web of Science
Record
Identification
Creation 28.02.2013
Last edited 20.05.2017
To cite this reference