Methylation-independent binding to histone H3 and cell cycle-dependent incorporation of HP1beta into heterochromatin

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dc.contributor.authorDialynas, G. K.en
dc.contributor.authorMakatsori, D.en
dc.contributor.authorKourmouli, N.en
dc.contributor.authorTheodoropoulos, P. A.en
dc.contributor.authorMcLean, K.en
dc.contributor.authorTerjung, S.en
dc.contributor.authorSingh, P. B.en
dc.contributor.authorGeorgatos, S. D.en
dc.date.accessioned2015-11-24T19:04:30Z
dc.date.available2015-11-24T19:04:30Z
dc.identifier.issn0021-9258-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/20052
dc.rightsDefault Licence-
dc.subjectAmino Acid Sequenceen
dc.subjectAnimalsen
dc.subjectCell Cycleen
dc.subjectCell Nucleus/metabolismen
dc.subjectChromosomal Proteins, Non-Histone/*chemistryen
dc.subjectDogsen
dc.subjectHeLa Cellsen
dc.subjectHeterochromatin/*chemistryen
dc.subjectHistones/*chemistryen
dc.subjectHumansen
dc.subjectMethylationen
dc.subjectMolecular Sequence Dataen
dc.subjectProtein Bindingen
dc.subjectRatsen
dc.titleMethylation-independent binding to histone H3 and cell cycle-dependent incorporation of HP1beta into heterochromatinen
heal.abstractWe have examined HP1beta-chromatin interactions in different molecular contexts in vitro and in vivo. Employing purified components we show that HP1beta exhibits selective, stoichiometric, and salt-resistant binding to recombinant histone H3, associating primarily with the helical "histone fold" domain. Furthermore, using "bulk" nucleosomes released by MNase digestion, S-phase extracts, and fragments of peripheral heterochromatin, we demonstrate that HP1beta associates more tightly with destabilized or disrupted nucleosomes (H3/H4 subcomplexes) than with intact particles. Western blotting and mass spectrometry data indicate that HP1beta-selected H3/H4 particles and subparticles possess a complex pattern of posttranslational modifications but are not particularly enriched in me3K9-H3. Consistent with these results, mapping of HP1beta and me3K9-H3 sites in vivo reveals overlapping, yet spatially distinct patterns, while transient transfection assays with synchronized cells show that stable incorporation of HP1beta-gfp into heterochromatin requires passage through the S-phase. The data amassed challenge the dogma that me3K9H3 is necessary and sufficient for HP1 binding and unveil a new mode of HP1-chromatin interactions.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.primary10.1074/jbc.M600558200-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/16547356-
heal.identifier.secondaryhttp://www.jbc.org/content/281/20/14350.full.pdf-
heal.journalNameJ Biol Chemen
heal.journalTypepeer-reviewed-
heal.languageen-
heal.publicationDate2006-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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