The histone chaperones Nap1 and Vps75 bind histones H3 and H4 in a tetrameric conformation

A. Bowman, Richard Ward, Nicola Wiechens, Vijender Singh, Hassane El-Mkami, David George Norman, Tom Owen-Hughes (Lead / Corresponding author)

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    57 Citations (Scopus)
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    Abstract

    Histone chaperones physically interact with histones to direct proper assembly and disassembly of nucleosomes regulating diverse nuclear processes such as DNA replication, promoter remodeling, transcription elongation, DNA damage, and histone variant exchange. Currently, the best-characterized chaperone-histone interaction is that between the ubiquitous chaperone Asf1 and a dimer of H3 and H4. Nucleosome assembly proteins (Nap proteins) represent a distinct class of histone chaperone. Using pulsed electron double resonance (PELDOR) measurements and protein crosslinking, we show that two members of this class, Nap1 and Vps75, bind histones in the tetrameric conformation also observed when they are sequestered within the nucleosome. Furthermore, H3 and H4 trapped in their tetrameric state can be used as substrates in nucleosome assembly and chaperone-mediated lysine acetylation. This alternate mode of histone interaction provides a potential means of maintaining the integrity of the histone tetramer during cycles of nucleosome reassembly.

    Original languageEnglish
    Pages (from-to)398-408
    Number of pages11
    JournalMolecular Cell
    Volume41
    Issue number4
    DOIs
    Publication statusPublished - 18 Feb 2011

    Keywords

    • NUCLEOSOME ASSEMBLY PROTEIN-1
    • DNA-REPLICATION
    • ACETYLTRANSFERASE RTT109
    • CRYSTAL-STRUCTURE
    • STRUCTURAL BASIS
    • COMPLEXES
    • CORE
    • CHROMATIN
    • ACETYLATION
    • ASF1

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