Journal Article

PUBDB-2015-01364

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png The Histone Chaperones Vps75 and Nap1 form Ring-like, Tetrameric Structures in Solution

Bowman, A. (Corresponding Author) ; Hammond, C. M. ; Stirling, A. ; Ward, R. ; Shang, W. ; El-Mkami, H. ; Robinson, D. A. ; Svergun, D.>Extern*EMBL* ; Norman, D. G. ; Owen-Hughes, T.

2014
Oxford Univ. Press8619 Oxford

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Please use a persistent id in citations: doi:10.1093/nar/gku232

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.

Note: OA

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Contributing Institute(s):

1. EMBL (EMBL)

Research Program(s):

1. DORIS Beamline D1.2 (POF2-54G13) (POF2-54G13)

Experiment(s):

1. DORIS Beamline D1.2 (DORIS III)

Appears in the scientific report 2014

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Database coverage:
; ; ; Allianz-Lizenz / DFG ; BIOSIS Previews ; Current Contents - Life Sciences ; IF >= 5 ; JCR ; NCBI Molecular Biology Database ; Nationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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