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@ARTICLE{Bowman:207476,
author = {Bowman, A. and Hammond, C. M. and Stirling, A. and Ward, R.
and Shang, W. and El-Mkami, H. and Robinson, D. A. and
Svergun, Dmitri and Norman, D. G. and Owen-Hughes, T.},
title = {{T}he {H}istone {C}haperones {V}ps75 and {N}ap1 form
{R}ing-like, {T}etrameric {S}tructures in {S}olution},
journal = {Nucleic acids symposium series},
volume = {42},
number = {9},
issn = {1362-4962},
address = {Oxford},
publisher = {Oxford Univ. Press8619},
reportid = {PUBDB-2015-01364},
pages = {6038 - 6051},
year = {2014},
note = {OA},
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.},
cin = {EMBL},
ddc = {540},
cid = {I:(DE-H253)EMBL-20120731},
pnm = {DORIS Beamline D1.2 (POF2-54G13)},
pid = {G:(DE-H253)POF2-D1.2-20130405},
experiment = {EXP:(DE-H253)D-D1.2-20150101},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000336495400060},
pubmed = {pmid:24688059},
doi = {10.1093/nar/gku232},
url = {https://bib-pubdb1.desy.de/record/207476},
}