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dc.contributor.authorBracken, Adrianen
dc.date.accessioned2021-03-08T14:30:46Z
dc.date.available2021-03-08T14:30:46Z
dc.date.issued2020en
dc.date.submitted2020en
dc.identifier.citationGlancy, E. and Ciferri, C. and Bracken, A.P., Structural basis for PRC2 engagement with chromatin, Current Opinion in Structural Biology, 67, 2020, 135-144en
dc.identifier.otherYen
dc.identifier.urihttp://hdl.handle.net/2262/95582
dc.descriptionPUBLISHEDen
dc.description.abstractThe polycomb repressive complex 2 (PRC2) is a conservedmultiprotein, repressive chromatin complex essential fordevelopment and maintenance of eukaryotic cellular identity.PRC2 comprises a trimeric core of SUZ12, EED and EZH1/2,which together with RBBP4/7 is sufficient to catalyse mono-methylation, di-methylation and tri-methylation of histone H3 atlysine 27 (H3K27me1/2/3). These histone methyltransferaseactivities of PRC2 are deregulated in several human cancers and certain developmental disorders, such as WeaverSyndrome. Core PRC2 associates with several accessoryproteins, which organise to define two main subassemblies,PRC2.1 and PRC2.2. Here we review new biochemical andstructural studies that are providing critical insights into howcore and accessory PRC2 subunits coordinate the faithfuldeposition of H3K27 methylations genome-wide.en
dc.format.extent135-144en
dc.language.isoenen
dc.relation.ispartofseriesCurrent Opinion in Structural Biologyen
dc.relation.ispartofseries67en
dc.rightsYen
dc.subjecthistone methyltransferaseactivities of PRC2en
dc.subjecthuman cancersen
dc.subjectpolycomb repressive complex 2 (PRC2)en
dc.subject.lcshhistone methyltransferaseactivities of PRC2en
dc.subject.lcshhuman cancersen
dc.subject.lcshpolycomb repressive complex 2 (PRC2)en
dc.titleStructural basis for PRC2 engagement with chromatinen
dc.typeJournal Articleen
dc.type.supercollectionscholarly_publicationsen
dc.type.supercollectionrefereed_publicationsen
dc.identifier.peoplefinderurlhttp://people.tcd.ie/brackeaen
dc.identifier.rssinternalid224441en
dc.identifier.doihttp://dx.doi.org/10.1016/j.sbi.2020.10.017en
dc.rights.ecaccessrightsopenAccess
dc.contributor.sponsorGrantNumberSFI/16/IA/4562en
dc.contributor.sponsorGrantNumberSFI/17/BBSRC/3415en
dc.contributor.sponsorGrantNumber15/IA/3104en
dc.identifier.orcid_id0000-0002-1547-9443en


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