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 journalArticle

    37 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 languageEnglish
    Pages (from-to)29-35
    Number of pages7
    JournalNature Structural & Molecular Biology
    Volume20
    Issue number1
    Early online date25 Nov 2012
    DOIs
    Publication statusPublished - Jan 2013

    Fingerprint

    Histones
    Histone Chaperones
    Proteins
    Nucleosomes
    DNA Replication
    Epigenomics
    DNA Repair
    Chromatin

    Keywords

    • RbAp48
    • ASF1
    • EPR spectroscopy
    • HISTONE CHAPERONE

    Cite this

    Zhang, Wei ; Yyl, Marek ; Ward, Richard ; Sobott, Frank ; Maman, Joseph ; Murthy, Andal ; Watson, Aleksandra ; Fedorov, Oleg ; Bowman, Andrew ; Owen-Hughes, Tom ; El Mkami, Hassane ; Murzina, Natalia ; Norman, David G ; Laue, Ernest. / Structural plasticity of histones H3–H4 facilitates their allosteric exchange between RbAp48 and ASF1. In: Nature Structural & Molecular Biology. 2013 ; Vol. 20, No. 1. pp. 29-35.
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    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 Yyl and Richard Ward and Frank Sobott and Joseph Maman and Andal Murthy and Aleksandra Watson and Oleg Fedorov and Andrew Bowman and Tom Owen-Hughes and {El Mkami}, Hassane and Natalia Murzina and Norman, {David G} and Ernest Laue",
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    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, DG & Laue, E 2013, 'Structural plasticity of histones H3–H4 facilitates their allosteric exchange between RbAp48 and ASF1', Nature Structural & Molecular Biology, vol. 20, no. 1, pp. 29-35. https://doi.org/10.1038/nsmb.2446

    Structural plasticity of histones H3–H4 facilitates their allosteric exchange between RbAp48 and ASF1. / Zhang, Wei; Yyl, Marek; Ward, Richard; Sobott, Frank; Maman, Joseph; Murthy, Andal; Watson, Aleksandra; Fedorov, Oleg; Bowman, Andrew; Owen-Hughes, Tom; El Mkami, Hassane; Murzina, Natalia; Norman, David G; Laue, Ernest (Lead / Corresponding author).

    In: Nature Structural & Molecular Biology, Vol. 20, No. 1, 01.2013, p. 29-35.

    Research output: Contribution to journalArticle

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