A bromodomain-DNA interaction facilitates acetylation-dependent bivalent nucleosome recognition by the BET protein BRDT

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dc.identifier.uri http://dx.doi.org/10.15488/1167
dc.identifier.uri http://www.repo.uni-hannover.de/handle/123456789/1191
dc.contributor.author Miller, Thomas C.R.
dc.contributor.author Simon, Bernd
dc.contributor.author Rybin, Vladimir
dc.contributor.author Grötsch, Helga
dc.contributor.author Curtet, Sandrine
dc.contributor.author Khochbin, Saadi
dc.contributor.author Carlomagno, Teresa
dc.contributor.author Müller, Christoph W.
dc.date.accessioned 2017-02-24T08:49:29Z
dc.date.available 2017-02-24T08:49:29Z
dc.date.issued 2016
dc.identifier.citation Miller, T.C.R.; Simon, B.; Rybin, V.; Grötsch, H.; Curtet, S. et al.: A bromodomain-DNA interaction facilitates acetylation-dependent bivalent nucleosome recognition by the BET protein BRDT. In: Nature Communications 7 (2016), 13855. DOI: https://doi.org/10.1038/ncomms13855
dc.description.abstract Bromodomains are critical components of many chromatin modifying/remodelling proteins and are emerging therapeutic targets, yet how they interact with nucleosomes, rather than acetylated peptides, remains unclear. Using BRDT as a model, we characterized how the BET family of bromodomains interacts with site-specifically acetylated nucleosomes. Here we report that BRDT interacts with nucleosomes through its first (BD1), but not second (BD2) bromodomain, and that acetylated histone recognition by BD1 is complemented by a bromodomain-DNA interaction. Simultaneous DNA and histone recognition enhances BRDT's nucleosome binding affinity and specificity, and its ability to localize to acetylated chromatin in cells. Conservation of DNA binding in bromodomains of BRD2, BRD3 and BRD4, indicates that bivalent nucleosome recognition is a key feature of these bromodomains and possibly others. Our results elucidate the molecular mechanism of BRDT association with nucleosomes and identify structural features of the BET bromodomains that may be targeted for therapeutic inhibition. eng
dc.description.sponsorship EMBL Interdisciplinary Postdoc Programme (EIPOD)
dc.description.sponsorship Marie Curie COFUND Actions
dc.description.sponsorship Foundation pour la Recherche Medicale (FRM)
dc.description.sponsorship ANR Episperm3
dc.description.sponsorship INCa libre
dc.description.sponsorship Plan Cancer
dc.description.sponsorship Fondation ARC
dc.language.iso eng
dc.publisher London : Nature Publishing Group
dc.relation.ispartofseries Nature Communications 7 (2016)
dc.rights CC BY 4.0
dc.rights.uri https://creativecommons.org/licenses/by/4.0/
dc.subject bromodomain–DNA eng
dc.subject protein eng
dc.subject BRDT eng
dc.subject infection research eng
dc.subject.ddc 500 | Naturwissenschaften ger
dc.title A bromodomain-DNA interaction facilitates acetylation-dependent bivalent nucleosome recognition by the BET protein BRDT
dc.type article
dc.type Text
dc.relation.issn 2041-1723
dc.relation.doi https://doi.org/10.1038/ncomms13855
dc.bibliographicCitation.volume 7
dc.bibliographicCitation.firstPage 13855
dc.description.version publishedVersion
tib.accessRights frei zug�nglich


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