The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution

Andrew Bowman, Colin M. Hammond, Andrew Stirling, Richard Ward, Weifeng Shang, Hassane El-Mkami, David A. Robinson, Dmitri I. Svergun, David G. Norman, Tom Owen-Hughes (Lead / Corresponding author)

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    27 Citations (Scopus)
    183 Downloads (Pure)

    Abstract

    NAP-1 fold histone chaperones play an important role in escorting histones to and from sites of nucleosome assembly and disassembly. The two NAP-1 fold histone chaperones in budding yeast, Vps75 and Nap1, have previously been crystalized in a characteristic homodimeric conformation. In this study, a combination of small angle X-ray scattering, multi angle light scattering and pulsed electron-electron double resonance approaches were used to show that both Vps75 and Nap1 adopt ring-shaped tetrameric conformations in solution. This suggests that the formation of homotetramers is a common feature of NAP-1 fold histone chaperones. The tetramerisation of NAP-1 fold histone chaperones may act to shield acidic surfaces in the absence of histone cargo thus providing a 'self-chaperoning' type mechanism.
    © The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research.
    Original languageEnglish
    Pages (from-to)6038-6051
    Number of pages13
    JournalNucleic Acids Research
    Volume42
    Issue number9
    Early online date31 Mar 2014
    DOIs
    Publication statusPublished - 2014

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