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dc.contributor.authorSundaramoorthy, Ramasubramanian
dc.contributor.authorHughes, Amanda L.
dc.contributor.authorSingh, Vijender
dc.contributor.authorWiechens, Nicola
dc.contributor.authorRyan, Daniel P.
dc.contributor.authorEl-Mkami, Hassane
dc.contributor.authorPetoukhov, Maxim
dc.contributor.authorSvergun, Dmitri I.
dc.contributor.authorTreutlein, Barbara
dc.contributor.authorQuack, Salina
dc.contributor.authorFischer, Monika
dc.contributor.authorMichaelis, Jens
dc.contributor.authorBöttcher, Bettina
dc.contributor.authorNorman, David G.
dc.contributor.authorOwen-Hughes, Tom
dc.date.accessioned2017-04-28T09:30:13Z
dc.date.available2017-04-28T09:30:13Z
dc.date.issued2017-03-23
dc.identifier.citationSundaramoorthy , R , Hughes , A L , Singh , V , Wiechens , N , Ryan , D P , El-Mkami , H , Petoukhov , M , Svergun , D I , Treutlein , B , Quack , S , Fischer , M , Michaelis , J , Böttcher , B , Norman , D G & Owen-Hughes , T 2017 , ' Structural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomes ' , eLife , vol. 6 , e22510 . https://doi.org/10.7554/eLife.22510en
dc.identifier.issn2050-084X
dc.identifier.otherPURE: 249879303
dc.identifier.otherPURE UUID: d1625dd9-5b09-482f-aaca-30f806840a7c
dc.identifier.otherRIS: urn:A805CE685C68236CF2E50979C9337E75
dc.identifier.otherScopus: 85017511461
dc.identifier.otherORCID: /0000-0002-0552-5784/work/60195399
dc.identifier.otherWOS: 000399016000001
dc.identifier.urihttps://hdl.handle.net/10023/10676
dc.descriptionThis work was funded by Wellcome Senior Fellowship 095062, Wellcome Trust grants 094090, 099149 and 097945. ALH was funded by and EMBO long-term fellowship ALTF 380–2015 co-funded by the European Commission (LTFCOFUND2013, GA-2013–609409).en
dc.description.abstractThe yeast Chd1 protein acts to position nucleosomes across genomes. Here, we model the structure of the Chd1 protein in solution and when bound to nucleosomes. In the apo state, the DNA-binding domain contacts the edge of the nucleosome while in the presence of the non-hydrolyzable ATP analog, ADP-beryllium fluoride, we observe additional interactions between the ATPase domain and the adjacent DNA gyre 1.5 helical turns from the dyad axis of symmetry. Binding in this conformation involves unravelling the outer turn of nucleosomal DNA and requires substantial reorientation of the DNA-binding domain with respect to the ATPase domains. The orientation of the DNA-binding domain is mediated by sequences in the N-terminus and mutations to this part of the protein have positive and negative effects on Chd1 activity. These observations indicate that the unfavorable alignment of C-terminal DNA-binding region in solution contributes to an auto-inhibited state.
dc.format.extent28
dc.language.isoeng
dc.relation.ispartofeLifeen
dc.rights© 2017, Sundaramoorthy et al. This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited.en
dc.subjectChd1en
dc.subjectNucleosomeen
dc.subjectChromatin remodelingen
dc.subjectATPaseen
dc.subjectQH426 Geneticsen
dc.subjectQH301 Biologyen
dc.subjectQD Chemistryen
dc.subjectDASen
dc.subject.lccQH426en
dc.subject.lccQH301en
dc.subject.lccQDen
dc.titleStructural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomesen
dc.typeJournal articleen
dc.contributor.sponsorThe Wellcome Trusten
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews. School of Physics and Astronomyen
dc.identifier.doihttps://doi.org/10.7554/eLife.22510
dc.description.statusPeer revieweden
dc.identifier.grantnumber099149/Z/12/Zen


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