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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    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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    Histone Chaperones
    Histones
    Electrons
    Saccharomycetales
    Nucleosomes
    Nucleic Acids
    X-Rays
    Light
    1-nitro-2-acetylpyrrole
    Research

    Cite this

    Bowman, Andrew ; Hammond, Colin M. ; Stirling, Andrew ; Ward, Richard ; Shang, Weifeng ; El-Mkami, Hassane ; Robinson, David A. ; Svergun, Dmitri I. ; Norman, David G. ; Owen-Hughes, Tom. / The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution. In: Nucleic Acids Research. 2014 ; Vol. 42, No. 9. pp. 6038-6051.
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    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.{\circledC} The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research.",
    author = "Andrew Bowman and Hammond, {Colin M.} and Andrew Stirling and Richard Ward and Weifeng Shang and Hassane El-Mkami and Robinson, {David A.} and Svergun, {Dmitri I.} and Norman, {David G.} and Tom Owen-Hughes",
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    Bowman, A, Hammond, CM, Stirling, A, Ward, R, Shang, W, El-Mkami, H, Robinson, DA, Svergun, DI, Norman, DG & Owen-Hughes, T 2014, 'The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution', Nucleic Acids Research, vol. 42, no. 9, pp. 6038-6051. https://doi.org/10.1093/nar/gku232

    The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution. / Bowman, Andrew; Hammond, Colin M.; Stirling, Andrew; Ward, Richard; Shang, Weifeng; El-Mkami, Hassane; Robinson, David A.; Svergun, Dmitri I.; Norman, David G.; Owen-Hughes, Tom (Lead / Corresponding author).

    In: Nucleic Acids Research, Vol. 42, No. 9, 2014, p. 6038-6051.

    Research output: Contribution to journalArticle

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    AU - El-Mkami, Hassane

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