The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution
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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.
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 . DOI: 10.1093/nar/gku232
Nucleic Acids Research
© 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.
DescriptionMRC [G1100021]; Wellcome Senior Fellowship . Source of open access funding: The Wellcome Trust .
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