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dc.contributor.authorGal, Cen_US
dc.contributor.authorMurton, HEen_US
dc.contributor.authorSubramanian, Len_US
dc.contributor.authorWhale, AJen_US
dc.contributor.authorMoore, KMen_US
dc.contributor.authorPaszkiewicz, Ken_US
dc.contributor.authorCodlin, Sen_US
dc.contributor.authorBähler, Jen_US
dc.contributor.authorCreamer, KMen_US
dc.contributor.authorPartridge, JFen_US
dc.contributor.authorAllshire, RCen_US
dc.contributor.authorKent, NAen_US
dc.contributor.authorWhitehall, SKen_US
dc.date.accessioned2017-03-24T15:04:57Z
dc.date.available2015-10-26en_US
dc.date.issued2016-01en_US
dc.date.submitted2017-03-01T08:45:45.522Z
dc.identifier.urihttp://qmro.qmul.ac.uk/xmlui/handle/123456789/22220
dc.description.abstractMaintenance of the correct level and organisation of nucleosomes is crucial for genome function. Here, we uncover a role for a conserved bromodomain AAA-ATPase, Abo1, in the maintenance of nucleosome architecture in fission yeast. Cells lacking abo1(+) experience both a reduction and mis-positioning of nucleosomes at transcribed sequences in addition to increased intragenic transcription, phenotypes that are hallmarks of defective chromatin re-establishment behind RNA polymerase II. Abo1 is recruited to gene sequences and associates with histone H3 and the histone chaperone FACT. Furthermore, the distribution of Abo1 on chromatin is disturbed by impaired FACT function. The role of Abo1 extends to some promoters and also to silent heterochromatin. Abo1 is recruited to pericentromeric heterochromatin independently of the HP1 ortholog, Swi6, where it enforces proper nucleosome occupancy. Consequently, loss of Abo1 alleviates silencing and causes elevated chromosome mis-segregation. We suggest that Abo1 provides a histone chaperone function that maintains nucleosome architecture genome-wide.en_US
dc.description.sponsorshipBBSRC (Doctoral Training Grants) Medical Research Council National Institute for Health Research (NIHR) Newcastle Biomedical Research Centre based at Newcastle Upon Tyne Hospitals NHS Foundation Trust and Newcastle University Marie Curie International Incoming FellowshipIIF275280 EMBO Long Term FellowshipALTF 1491‐2010 The Wellcome Trust095021 Wellcome Trust core funding092076 NIA fellowshipNRSA F31‐AG038153 NIH R01GM084045 Cancer CenterCCSG 2 P30 CA21765; American Lebanese Syrian Associated Charities of St. Jude Children's Research Hospital; Wellcome Trust Senior Investigator Award; Wellcome Trust Institutional Strategic Support FundWT097835MF; Newcastle UniversityWT 097823/Z/11/Zen_US
dc.format.extent79 - 93en_US
dc.languageengen_US
dc.relation.ispartofEMBO Repen_US
dc.rightsThis is an open access article under the terms of the Creative Commons Attribution 4.0 License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
dc.subjectAbo1en_US
dc.subjectSchizosaccharomyces pombeen_US
dc.subjectbromodomain AAA‐ATPasesen_US
dc.subjectchromatinen_US
dc.subjectnucleosome mappingen_US
dc.subjectAdenosine Triphosphatasesen_US
dc.subjectChromatinen_US
dc.subjectChromatin Assembly and Disassemblyen_US
dc.subjectChromosomal Proteins, Non-Histoneen_US
dc.subjectChromosome Segregationen_US
dc.subjectDNA, Intergenicen_US
dc.subjectGene Silencingen_US
dc.subjectHistone Chaperonesen_US
dc.subjectHistonesen_US
dc.subjectNucleosomesen_US
dc.subjectPromoter Regions, Geneticen_US
dc.subjectRNA Polymerase IIen_US
dc.subjectSchizosaccharomycesen_US
dc.subjectSchizosaccharomyces pombe Proteinsen_US
dc.subjectTranscription Factorsen_US
dc.subjectTranscription, Geneticen_US
dc.titleAbo1, a conserved bromodomain AAA-ATPase, maintains global nucleosome occupancy and organisation.en_US
dc.typeArticle
dc.rights.holder© 2015 The Authors
dc.identifier.doi10.15252/embr.201540476en_US
pubs.author-urlhttps://www.ncbi.nlm.nih.gov/pubmed/26582768en_US
pubs.issue1en_US
pubs.notesNot knownen_US
pubs.publication-statusPublisheden_US
pubs.volume17en_US
dcterms.dateAccepted2015-10-26en_US


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