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The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution
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dc.contributor.author | Bowman, Andrew | |
dc.contributor.author | Hammond, Colin M. | |
dc.contributor.author | Stirling, Andrew | |
dc.contributor.author | Ward, Richard | |
dc.contributor.author | Shang, Weifeng | |
dc.contributor.author | El Mkami, Hassane | |
dc.contributor.author | Robinson, David A. | |
dc.contributor.author | Svergun, Dmitri I. | |
dc.contributor.author | Norman, David G. | |
dc.contributor.author | Owen-Hughes, Tom | |
dc.date.accessioned | 2014-07-09T15:01:05Z | |
dc.date.available | 2014-07-09T15:01:05Z | |
dc.date.issued | 2014 | |
dc.identifier | 130816526 | |
dc.identifier | b25a5920-d261-4868-b087-842d5e80d081 | |
dc.identifier | 000336495400060 | |
dc.identifier | 84901332832 | |
dc.identifier | 000336495400060 | |
dc.identifier.citation | Bowman , A , Hammond , C M , Stirling , A , Ward , R , Shang , W , El Mkami , H , Robinson , D A , Svergun , D I , Norman , D G & Owen-Hughes , T 2014 , ' The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution ' , Nucleic Acids Research , vol. 42 , no. 9 , pp. 6038-6051 . https://doi.org/10.1093/nar/gku232 | en |
dc.identifier.issn | 0305-1048 | |
dc.identifier.other | ORCID: /0000-0002-0552-5784/work/60195401 | |
dc.identifier.uri | https://hdl.handle.net/10023/4995 | |
dc.description | MRC [G1100021]; Wellcome Senior Fellowship [095062]. Source of open access funding: The Wellcome Trust [094090]. | en |
dc.description.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. | |
dc.format.extent | 14 | |
dc.format.extent | 3675031 | |
dc.language.iso | eng | |
dc.relation.ispartof | Nucleic Acids Research | en |
dc.subject | Nucleosome assembly protein-1 | en |
dc.subject | Angle scattering data | en |
dc.subject | X-ray-scattering | en |
dc.subject | Acetyltransferase Rtt109 | en |
dc.subject | Saccharomyces-cerevisiae | en |
dc.subject | Transcription elongation | en |
dc.subject | In-vitro | en |
dc.subject | Complexes | en |
dc.subject | Acetylation | en |
dc.subject | Association | en |
dc.subject | QD Chemistry | en |
dc.subject.lcc | QD | en |
dc.title | The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution | en |
dc.type | Journal article | en |
dc.contributor.institution | University of St Andrews. School of Biology | en |
dc.contributor.institution | University of St Andrews. School of Physics and Astronomy | en |
dc.identifier.doi | https://doi.org/10.1093/nar/gku232 | |
dc.description.status | Peer reviewed | en |
dc.identifier.url | http://nar.oxfordjournals.org/content/42/9/6038/suppl/DC1 | en |
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