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^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	6038-6051
Number of pages	14
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

Keywords

Nucleosome assembly protein-1
Angle scattering data
X-ray-scattering
Acetyltransferase Rtt109
Saccharomyces-cerevisiae
Transcription elongation
In-vitro
Complexes
Acetylation
Association

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10.1093/nar/gku232

ElMkami_2014_NAR_TheHistone
© The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research. 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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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.",

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author = "Andrew Bowman and Hammond, {Colin M.} and Andrew Stirling and Richard Ward and Weifeng Shang and {El Mkami}, Hassane and Robinson, {David A.} and Svergun, {Dmitri I.} and Norman, {David G.} and Tom Owen-Hughes",

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doi = "10.1093/nar/gku232",

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AU - Bowman, Andrew

AU - Hammond, Colin M.

AU - Stirling, Andrew

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

N1 - MRC [G1100021]; Wellcome Senior Fellowship [095062]. Source of open access funding: The Wellcome Trust [094090].

PY - 2014

Y1 - 2014

N2 - 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.

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.

KW - Nucleosome assembly protein-1

KW - Angle scattering data

KW - X-ray-scattering

KW - Acetyltransferase Rtt109

KW - Saccharomyces-cerevisiae

KW - Transcription elongation

KW - In-vitro

KW - Complexes

KW - Acetylation

KW - Association

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DO - 10.1093/nar/gku232

M3 - Article

SN - 0305-1048

VL - 42

SP - 6038

EP - 6051

JO - Nucleic Acids Research

JF - Nucleic Acids Research

IS - 9

ER -

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

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Keywords

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