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

doi:10.1093/nar/gku232

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 language	English
Pages (from-to)	6038-6051
Number of pages	13
Journal	Nucleic Acids Research
Volume	42
Issue number	9
Early online date	31 Mar 2014
DOIs	https://doi.org/10.1093/nar/gku232
Publication status	Published - 2014

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10.1093/nar/gku232

Nucl. Acids Res.-2014-Bowman-6038-51
This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
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http://nar.oxfordjournals.org/content/42/9/6038

Strategic Award: Wellcome Trust Technology Platform
Blow, J., Lamond, A. & Owen-Hughes, T.
Wellcome Trust
1/01/13 → 30/09/18
Project: Research
State-of-the-Art Facilities for Structural Biology at the University of Dundee
Hunter, B., Lilley, D., Owen-Hughes, T., Wyatt, P. & van Aalten, D.
Wellcome Trust
1/03/12 → 28/02/17
Project: Research
Mechanisms for Remodelling Chromatin (Senior Fellowship Renewal)
Owen-Hughes, T.
Wellcome Trust
1/01/12 → 31/05/19
Project: Research

Owen-Hughes, Tom
- Molecular Cell and Developmental Biology - Professor of Chromatin Structure and Dynamics
Person: Academic

Cite this

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

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.{\textcopyright} The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research.",

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doi = "10.1093/nar/gku232",

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AU - Ward, Richard

AU - Shang, Weifeng

AU - El-Mkami, Hassane

AU - Robinson, David A.

AU - Svergun, Dmitri I.

AU - Norman, David G.

AU - Owen-Hughes, Tom

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AB - 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.

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JO - Nucleic Acids Research

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

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Projects

Strategic Award: Wellcome Trust Technology Platform

State-of-the-Art Facilities for Structural Biology at the University of Dundee

Mechanisms for Remodelling Chromatin (Senior Fellowship Renewal)

Profiles

Owen-Hughes, Tom

Cite this