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

27 Citationer (Scopus)

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.

Originalsprog	Engelsk
Tidsskrift	Nucleic Acids Research
Vol/bind	42
Udgave nummer	9
Sider (fra-til)	6038-51
Antal sider	14
ISSN	0305-1048
DOI	https://doi.org/10.1093/nar/gku232
Status	Udgivet - maj 2014
Udgivet eksternt	Ja

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10.1093/nar/gku232

gku232.pdfForlagets udgivne version, 3,62 MBLicens: CC BY-NC

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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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year = "2014",

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T1 - The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution

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

PY - 2014/5

Y1 - 2014/5

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 - Models, Molecular

KW - Molecular Chaperones

KW - Nucleosome Assembly Protein 1

KW - Protein Binding

KW - Protein Interaction Domains and Motifs

KW - Protein Structure, Quaternary

KW - Saccharomyces cerevisiae

KW - Saccharomyces cerevisiae Proteins

KW - Scattering, Small Angle

KW - Solutions

KW - X-Ray Diffraction

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1093/nar/gku232

DO - 10.1093/nar/gku232

M3 - Journal article

C2 - 24688059

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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