Projects per year
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.
© The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research.
© The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research.
Original language | English |
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Pages (from-to) | 6038-6051 |
Number of pages | 13 |
Journal | Nucleic Acids Research |
Volume | 42 |
Issue number | 9 |
Early online date | 31 Mar 2014 |
DOIs | |
Publication status | Published - 2014 |
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Dive into the research topics of 'The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution'. Together they form a unique fingerprint.Projects
- 3 Finished
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Strategic Award: Wellcome Trust Technology Platform
Blow, J., Lamond, A. & Owen-Hughes, T.
1/01/13 → 30/09/18
Project: Research
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State-of-the-Art Facilities for Structural Biology at the University of Dundee
Hunter, B., Lilley, D., Owen-Hughes, T., Wyatt, P. & van Aalten, D.
1/03/12 → 28/02/17
Project: Research
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Profiles
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Owen-Hughes, Tom
- Molecular Cell and Developmental Biology - Professor of Chromatin Structure and Dynamics
Person: Academic