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000207476 1001_ $$0P:(DE-HGF)0$$aBowman, A.$$b0$$eCorresponding Author
000207476 245__ $$aThe Histone Chaperones Vps75 and Nap1 form Ring-like, Tetrameric Structures in Solution
000207476 260__ $$aOxford$$bOxford Univ. Press8619$$c2014
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000207476 520__ $$aNAP-1 fold histone chaperones play an important role in escorting histones to and from sites of nucleosome assembly and disassembly. The two NAP-1 fold histone chaperones in budding yeast, Vps75 and Nap1, have previously been crystalized in a characteristic homodimeric conformation. In this study, a combination of small angle X-ray scattering, multi angle light scattering and pulsed electron–electron double resonance approaches were used to show that both Vps75 and Nap1 adopt ring-shaped tetrameric conformations in solution. This suggests that the formation of homotetramers is a common feature of NAP-1 fold histone chaperones. The tetramerisation of NAP-1 fold histone chaperones may act to shield acidic surfaces in the absence of histone cargo thus providing a ‘self-chaperoning’ type mechanism.
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000207476 7001_ $$0P:(DE-HGF)0$$aHammond, C. M.$$b1
000207476 7001_ $$0P:(DE-HGF)0$$aStirling, A.$$b2
000207476 7001_ $$0P:(DE-HGF)0$$aWard, R.$$b3
000207476 7001_ $$0P:(DE-HGF)0$$aShang, W.$$b4
000207476 7001_ $$0P:(DE-HGF)0$$aEl-Mkami, H.$$b5
000207476 7001_ $$0P:(DE-HGF)0$$aRobinson, D. A.$$b6
000207476 7001_ $$0P:(DE-H253)PIP1001422$$aSvergun, Dmitri$$b7
000207476 7001_ $$0P:(DE-HGF)0$$aNorman, D. G.$$b8
000207476 7001_ $$0P:(DE-HGF)0$$aOwen-Hughes, T.$$b9
000207476 773__ $$0PERI:(DE-600)2205588-5$$a10.1093/nar/gku232$$gVol. 42, no. 9, p. 6038 - 6051$$n9$$p6038 - 6051$$tNucleic acids symposium series$$v42$$x1362-4962$$y2014
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