Structural plasticity of histones H3–H4 facilitates their allosteric exchange between RbAp48 and ASF1

Wei Zhang; Marek Yyl; Richard Ward; Frank Sobott; Joseph Maman; Andal Murthy; Aleksandra Watson; Oleg Fedorov; Andrew Bowman; Tom Owen-Hughes; Hassane El Mkami; Natalia Murzina; David G Norman; Ernest Laue

doi:10.1038/nsmb.2446

Structural plasticity of histones H3–H4 facilitates their allosteric exchange between RbAp48 and ASF1

Wei Zhang, Marek Yyl, Richard Ward, Frank Sobott, Joseph Maman, Andal Murthy, Aleksandra Watson, Oleg Fedorov, Andrew Bowman, Tom Owen-Hughes, Hassane El Mkami, Natalia Murzina, David G Norman, Ernest Laue (Lead / Corresponding author)

Research output: Contribution to journal › Article › peer-review

55 Citations (Scopus)

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.

Original language	English
Pages (from-to)	29-35
Number of pages	7
Journal	Nature Structural & Molecular Biology
Volume	20
Issue number	1
Early online date	25 Nov 2012
DOIs	https://doi.org/10.1038/nsmb.2446
Publication status	Published - Jan 2013

Keywords

RbAp48
ASF1
EPR spectroscopy
HISTONE CHAPERONE

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10.1038/nsmb.2446

Cite this

Zhang, W., Yyl, M., Ward, R., Sobott, F., Maman, J., Murthy, A., Watson, A., Fedorov, O., Bowman, A., Owen-Hughes, T., El Mkami, H., Murzina, N., Norman, D. G., & Laue, E. (2013). Structural plasticity of histones H3–H4 facilitates their allosteric exchange between RbAp48 and ASF1. Nature Structural & Molecular Biology, 20(1), 29-35. https://doi.org/10.1038/nsmb.2446

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title = "Structural plasticity of histones H3–H4 facilitates their allosteric exchange between RbAp48 and ASF1",

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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AU - Zhang, Wei

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AU - Ward, Richard

AU - Sobott, Frank

AU - Maman, Joseph

AU - Murthy, Andal

AU - Watson, Aleksandra

AU - Fedorov, Oleg

AU - Bowman, Andrew

AU - Owen-Hughes, Tom

AU - El Mkami, Hassane

AU - Murzina, Natalia

AU - Norman, David G

AU - Laue, Ernest

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AB - 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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Structural plasticity of histones H3–H4 facilitates their allosteric exchange between RbAp48 and ASF1

Abstract

Keywords

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Strategic Award: Wellcome Trust Technology Platform

Mechanisms for Remodelling Chromatin (Senior Fellowship Renewal)

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Structural plasticity of histones H3–H4 facilitates their allosteric exchange between RbAp48 and ASF1

Abstract

Keywords

Access to Document

Other files and links

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Projects

Strategic Award: Wellcome Trust Technology Platform

Mechanisms for Remodelling Chromatin (Senior Fellowship Renewal)

Cite this