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dc.contributor.authorBuchanan, Luke
dc.contributor.authorDurand-Dubief, Mickaël
dc.contributor.authorRoguev, Assen
dc.contributor.authorCagri, Sakalar
dc.contributor.authorWilhelm, Brian
dc.contributor.authorStålfors, Annelie
dc.contributor.authorShevchenko, Anna
dc.contributor.authorAasland, Rein
dc.contributor.authorShevchenko, Andrej
dc.contributor.authorEkwall, Karl
dc.contributor.authorStewart, Francis
dc.date.accessioned2016-08-05T07:52:33Z
dc.date.available2016-08-05T07:52:33Z
dc.date.issued2009-11-13
dc.PublishedPLoS Genetics 2009, 5(11):e1000726eng
dc.identifier.issn1553-7404en_US
dc.identifier.urihttps://hdl.handle.net/1956/12459
dc.description.abstractEukaryotic genomes are repetitively packaged into chromatin by nucleosomes, however they are regulated by the differences between nucleosomes, which establish various chromatin states. Local chromatin cues direct the inheritance and propagation of chromatin status via self-reinforcing epigenetic mechanisms. Replication-independent histone exchange could potentially perturb chromatin status if histone exchange chaperones, such as Swr1C, loaded histone variants into wrong sites. Here we show that in Schizosaccharomyces pombe, like Saccharomyces cerevisiae, Swr1C is required for loading H2A.Z into specific sites, including the promoters of lowly expressed genes. However S. pombe Swr1C has an extra subunit, Msc1, which is a JumonjiC-domain protein of the Lid/Jarid1 family. Deletion of Msc1 did not disrupt the S. pombe Swr1C or its ability to bind and load H2A.Z into euchromatin, however H2A.Z was ectopically found in the inner centromere and in subtelomeric chromatin. Normally this subtelomeric region not only lacks H2A.Z but also shows uniformly lower levels of H3K4me2, H4K5, and K12 acetylation than euchromatin and disproportionately contains the most lowly expressed genes during vegetative growth, including many meiotic-specific genes. Genes within and adjacent to subtelomeric chromatin become overexpressed in the absence of either Msc1, Swr1, or paradoxically H2A.Z itself. We also show that H2A.Z is N-terminally acetylated before, and lysine acetylated after, loading into chromatin and that it physically associates with the Nap1 histone chaperone. However, we find a negative correlation between the genomic distributions of H2A.Z and Nap1/Hrp1/Hrp3, suggesting that the Nap1 chaperones remove H2A.Z from chromatin. These data describe H2A.Z action in S. pombe and identify a new mode of chromatin surveillance and maintenance based on negative regulation of histone variant misincorporation.en_US
dc.language.isoengeng
dc.publisherPLoSen_US
dc.rightsAttribution CC BYeng
dc.rights.urihttp://creativecommons.org/licenses/by/4.0eng
dc.titleThe Schizosaccharomyces pombe JmjC-protein, Msc1, prevents H2A.Z localization in centromeric and subtelomeric chromatin domainsen_US
dc.typePeer reviewed
dc.typeJournal article
dc.date.updated2016-04-08T08:15:41Z
dc.description.versionpublishedVersionen_US
dc.rights.holderCopyright 2009 The Authorsen_US
dc.identifier.doihttps://doi.org/10.1371/journal.pgen.1000726
dc.identifier.cristin346228
dc.subject.nsiVDP::Matematikk og naturvitenskap: 400::Basale biofag: 470
dc.subject.nsiVDP::Mathematics and natural scienses: 400::Basic biosciences: 470


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