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The histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4 complexes
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dc.contributor.author | Hammond, Colin M. | |
dc.contributor.author | Sundaramoorthy, Ramasubramanian | |
dc.contributor.author | Larance, Mark | |
dc.contributor.author | Lamond, Angus | |
dc.contributor.author | Stevens, Michael A. | |
dc.contributor.author | El-Mkami, Hassane | |
dc.contributor.author | Norman, David G. | |
dc.contributor.author | Owen-Hughes, Tom | |
dc.date.accessioned | 2016-08-19T10:30:16Z | |
dc.date.available | 2016-08-19T10:30:16Z | |
dc.date.issued | 2016-07-27 | |
dc.identifier | 245137864 | |
dc.identifier | 3b28d964-7c97-455c-ae8c-65b40981ade1 | |
dc.identifier | 84982809872 | |
dc.identifier | 000382999300017 | |
dc.identifier.citation | Hammond , C M , Sundaramoorthy , R , Larance , M , Lamond , A , Stevens , M A , El-Mkami , H , Norman , D G & Owen-Hughes , T 2016 , ' The histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4 complexes ' , Nucleic Acids Research , vol. 44 , no. 13 , pp. 6157-6172 . https://doi.org/10.1093/nar/gkw209 | en |
dc.identifier.issn | 0305-1048 | |
dc.identifier.other | ORCID: /0000-0002-0552-5784/work/60195407 | |
dc.identifier.uri | https://hdl.handle.net/10023/9336 | |
dc.description | Wellcome Trust [094090, 097945, 099149]; Medical Research Council [G1100021]. Funding for open access charge: Wellcome Trust. | en |
dc.description.abstract | Vps75 is a histone chaperone that has been historically characterized as homodimer by X-ray crystallography. In this study, we present a crystal structure containing two related tetrameric forms of Vps75 within the crystal lattice. We show Vps75 associates with histones in multiple oligomers. In the presence of equimolar H3-H4 and Vps75, the major species is a reconfigured Vps75 tetramer bound to a histone H3-H4 tetramer. However, in the presence of excess histones, a Vps75 dimer bound to a histone H3-H4 tetramer predominates. We show the Vps75-H3-H4 interaction is compatible with the histone chaperone Asf1 and deduce a structural model of the Vps75-Asf1-H3-H4 (VAH) co-chaperone complex using the Pulsed Electron-electron Double Resonance (PELDOR) technique and cross-linking MS/MS distance restraints. The model provides a molecular basis for the involvement of both Vps75 and Asf1 in Rtt109 catalysed histone H3 K9 acetylation. In the absence of Asf1 this model can be used to generate a complex consisting of a reconfigured Vps75 tetramer bound to a H3-H4 tetramer. This provides a structural explanation for many of the complexes detected biochemically and illustrates the ability of Vps75 to interact with dimeric or tetrameric H3-H4 using the same interaction surface. | |
dc.format.extent | 16 | |
dc.format.extent | 5220903 | |
dc.language.iso | eng | |
dc.relation.ispartof | Nucleic Acids Research | en |
dc.subject | QH426 Genetics | en |
dc.subject | Genetics | en |
dc.subject | DAS | en |
dc.subject.lcc | QH426 | en |
dc.title | The histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4 complexes | en |
dc.type | Journal article | en |
dc.contributor.sponsor | The Wellcome Trust | en |
dc.contributor.institution | University of St Andrews. School of Physics and Astronomy | en |
dc.identifier.doi | https://doi.org/10.1093/nar/gkw209 | |
dc.description.status | Peer reviewed | en |
dc.identifier.url | http://www.scopus.com/inward/record.url?scp=84980603903&partnerID=8YFLogxK | en |
dc.identifier.grantnumber | 099149/Z/12/Z | en |
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