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.
Citation
Bowman , A , Hammond , C M , Stirling , A , Ward , R , Shang , W , El Mkami , H , Robinson , D A , Svergun , D I , Norman , D G & 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
Publication
Nucleic Acids Research
Status
Peer reviewed
ISSN
0305-1048Type
Journal article
Description
MRC [G1100021]; Wellcome Senior Fellowship [095062]. Source of open access funding: The Wellcome Trust [094090].Collections
Items in the St Andrews Research Repository are protected by copyright, with all rights reserved, unless otherwise indicated.