%0 Journal Article
%A Bowman, A.
%A Hammond, C. M.
%A Stirling, A.
%A Ward, R.
%A Shang, W.
%A El-Mkami, H.
%A Robinson, D. A.
%A Svergun, Dmitri
%A Norman, D. G.
%A Owen-Hughes, T.
%T The Histone Chaperones Vps75 and Nap1 form Ring-like, Tetrameric Structures in Solution
%J Nucleic acids symposium series
%V 42
%N 9
%@ 1362-4962
%C Oxford
%I Oxford Univ. Press8619
%M PUBDB-2015-01364
%P 6038 - 6051
%D 2014
%Z OA
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000336495400060
%$ pmid:24688059
%R 10.1093/nar/gku232
%U https://bib-pubdb1.desy.de/record/207476