TY  - JOUR
AU  - Bowman, A.
AU  - Hammond, C. M.
AU  - Stirling, A.
AU  - Ward, R.
AU  - Shang, W.
AU  - El-Mkami, H.
AU  - Robinson, D. A.
AU  - Svergun, Dmitri
AU  - Norman, D. G.
AU  - Owen-Hughes, T.
TI  - The Histone Chaperones Vps75 and Nap1 form Ring-like, Tetrameric Structures in Solution
JO  - Nucleic acids symposium series
VL  - 42
IS  - 9
SN  - 1362-4962
CY  - Oxford
PB  - Oxford Univ. Press8619
M1  - PUBDB-2015-01364
SP  - 6038 - 6051
PY  - 2014
N1  - OA
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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000336495400060
C6  - pmid:24688059
DO  - DOI:10.1093/nar/gku232
UR  - https://bib-pubdb1.desy.de/record/207476
ER  -