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

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

doi:10.1038/nsmb.2446

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

Wei Zhang, Marek Tyl, Richard Ward, Frank Sobott, Joseph Maman, Andal S. Murthy, Aleksandra A. Watson, Oleg Fedorov, Andrew Bowman, Tom Owen-Hughes, Hassane El Mkami, Natalia V. Murzina, David G. Norman, Ernest D. Laue^*

^*Corresponding author for this work

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 and Molecular Biology
Volume	20
Issue number	1
DOIs	https://doi.org/10.1038/nsmb.2446
Publication status	Published - Jan 2013

Keywords

DNA-REPLICATION
PULSED EPR
CHROMATIN
NUCLEOSOME
H4
COMPLEX
H3
METHYLATION
SUBUNIT
YEAST

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10.1038/nsmb.2446

EP/F0390034/1 The HIPER Project: Bringing the NMR Paradigm to ESR - The HIPER Project
Smith, G. M. (PI), El Mkami, H. (CoI) & Robertson, D. (CoI)
EPSRC
1/09/08 → 31/10/12
Project: Standard

Cite this

Zhang, W., Tyl, M., Ward, R., Sobott, F., Maman, J., Murthy, A. S., Watson, A. A., Fedorov, O., Bowman, A., Owen-Hughes, T., El Mkami, H., Murzina, N. V., Norman, D. G., & Laue, E. D. (2013). Structural plasticity of histones H3-H4 facilitates their allosteric exchange between RbAp48 and ASF1. Nature Structural and 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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author = "Wei Zhang and Marek Tyl and Richard Ward and Frank Sobott and Joseph Maman and Murthy, {Andal S.} and Watson, {Aleksandra A.} and Oleg Fedorov and Andrew Bowman and Tom Owen-Hughes and {El Mkami}, Hassane and Murzina, {Natalia V.} and Norman, {David G.} and Laue, {Ernest D.}",

year = "2013",

month = jan,

doi = "10.1038/nsmb.2446",

language = "English",

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Zhang, W, Tyl, M, Ward, R, Sobott, F, Maman, J, Murthy, AS, Watson, AA, Fedorov, O, Bowman, A, Owen-Hughes, T, El Mkami, H, Murzina, NV, Norman, DG & Laue, ED 2013, 'Structural plasticity of histones H3-H4 facilitates their allosteric exchange between RbAp48 and ASF1', Nature Structural and Molecular Biology, vol. 20, no. 1, pp. 29-35. https://doi.org/10.1038/nsmb.2446

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AU - Zhang, Wei

AU - Tyl, Marek

AU - Ward, Richard

AU - Sobott, Frank

AU - Maman, Joseph

AU - Murthy, Andal S.

AU - Watson, Aleksandra A.

AU - Fedorov, Oleg

AU - Bowman, Andrew

AU - Owen-Hughes, Tom

AU - El Mkami, Hassane

AU - Murzina, Natalia V.

AU - Norman, David G.

AU - Laue, Ernest D.

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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.

KW - DNA-REPLICATION

KW - PULSED EPR

KW - CHROMATIN

KW - NUCLEOSOME

KW - H4

KW - COMPLEX

KW - H3

KW - METHYLATION

KW - SUBUNIT

KW - YEAST

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DO - 10.1038/nsmb.2446

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JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

IS - 1

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

Abstract

Keywords

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Projects

EP/F0390034/1 The HIPER Project: Bringing the NMR Paradigm to ESR - The HIPER Project

Cite this