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  5. Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ
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Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/23477
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dc.contributor.authorKourmouli, N.en
dc.contributor.authorDialynas, G.en
dc.contributor.authorPetraki, C.en
dc.contributor.authorPyrpasopoulou, A.en
dc.contributor.authorSingh, P. B.en
dc.contributor.authorGeorgatos, S. D.en
dc.contributor.authorTheodoropoulos, P. A.en
dc.date.accessioned2015-11-24T19:32:57Z-
dc.date.available2015-11-24T19:32:57Z-
dc.identifier.issn0021-9258-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/23477-
dc.rightsDefault Licence-
dc.subjectAmino Acid Sequenceen
dc.subjectAnimalsen
dc.subjectBrain/metabolismen
dc.subjectChromosomal Proteins, Non-Histone/chemistry/*metabolismen
dc.subjectEndometrial Neoplasmsen
dc.subjectFemaleen
dc.subjectHeLa Cellsen
dc.subjectHeterochromatin/*metabolismen
dc.subjectHumansen
dc.subjectKineticsen
dc.subjectMiceen
dc.subjectMolecular Sequence Dataen
dc.subjectMolecular Weighten
dc.subjectNuclear Envelope/*physiology/ultrastructureen
dc.subjectPeptide Fragments/chemistryen
dc.subjectProtein Bindingen
dc.subjectRecombinant Proteins/chemistry/metabolismen
dc.subjectTubulin/*metabolismen
dc.subjectTumor Cells, Cultureden
dc.titleBinding of heterochromatin protein 1 to the nuclear envelope is regulated by a soluble form of tubulinen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primary10.1074/jbc.M007135200-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/11278332-
heal.identifier.secondaryhttp://www.jbc.org/content/276/16/13007.full.pdf-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate2001-
heal.abstractWe have previously shown that the mouse heterochromatin protein 1 homologue M31 interacts dynamically with the nuclear envelope. Using quantitative in vitro assays, we now demonstrate that this interaction is potently inhibited by soluble factors present in mitotic and interphase cytosol. As indicated by depletion and order-of-addition experiments, the inhibitory activity co-isolates with a 55-kDa protein, which binds avidly to the nuclear envelope and presumably blocks M31-binding sites. Purification of this protein and microsequencing of tryptic peptides identify it as alpha2/6:beta2-tubulin. Consistent with this observation, bona fide tubulin, isolated from rat brain and maintained in a nonpolymerized state, abolishes binding of M31 to the nuclear envelope and aborts M31-mediated nuclear envelope reassembly in an in vitro system. These observations provide a new example of "moonlighting," a process whereby multimeric proteins switch function when their aggregation state or localization is altered.en
heal.journalNameJ Biol Chemen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
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