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Title
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Structural plasticity of histones H3-H4 facilitates their allosteric exchange between RbAp48 and ASF1
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Author
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Abstract
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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. |
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Language
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English
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Source (journal)
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Nature structural & molecular biology. - New York, N.Y., 2004, currens
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Publication
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New York, N.Y.
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2013
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ISSN
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1545-9993
[print]
1545-9985
[online]
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DOI
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10.1038/NSMB.2446
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Volume/pages
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20
:1
(2013)
, p. 29-U43
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ISI
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000313072400007
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Full text (Publisher's DOI)
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