Mitotic silencing of human rRNA synthesis: inactivation of the promoter selectivity factor SL1 by cdc2 cyclin B-mediated phosphorylation

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dc.contributor.authorHeix, J.en
dc.contributor.authorVente, A.en
dc.contributor.authorVoit, R.en
dc.contributor.authorBudde, A.en
dc.contributor.authorMichaelidis, T. M.en
dc.contributor.authorGrummt, I.en
dc.date.accessioned2015-11-24T16:31:57Z
dc.date.available2015-11-24T16:31:57Z
dc.identifier.issn0261-4189-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/7500
dc.rightsDefault Licence-
dc.subjectcdc2en
dc.subjectcyclin ben
dc.subjectmitosisen
dc.subjectphosphopeptide mappingen
dc.subjectrna polymerase ien
dc.subjecttbpen
dc.subjecttbp-associated factorsen
dc.subjectrna-polymerase-ien
dc.subjecttata-binding-proteinen
dc.subjectribosomal gene-transcriptionen
dc.subjectcell-cycleen
dc.subjectnucleolar transcriptionen
dc.subjectdependent transcriptionen
dc.subjectspecies-specificityen
dc.subjectiiien
dc.titleMitotic silencing of human rRNA synthesis: inactivation of the promoter selectivity factor SL1 by cdc2 cyclin B-mediated phosphorylationen
heal.abstractWe have used a reconstituted cell-free transcription system to investigate the molecular basis of mitotic repression of RNA polymerase I (pol I) transcription. We demonstrate that SL1, the TBP-containing promoter-binding factor, is inactivated by cdc2/cyclin B-directed phosphorylation, and reactivated by dephosphorylation. Transcriptional inactivation in vitro is accompanied by phosphorylation of two subunits, e.g. TBP and hTAF(I)110. To distinguish whether transcriptional repression is due to phosphorylation of TBP, hTAFI110 or both, SL1 was purified from two HeLa cell lines that express either full-length or the core domain of TBP only. Both TBP-TAF(I) complexes exhibit similar activity and both are repressed at mitosis, indicating that the variable N-terminal domain which contains multiple target sites for cdc2/cyclin B phosphorylation is dispensable for mitotic repression. Protein-protein interaction studies reveal that mitotic phosphorylation impairs the interaction of SL1 with UBF, The results suggest that phosphorylation of SL1 is used as a molecular switch to prevent pre-initiation complex formation and to shut down rDNA transcription at mitosis.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.secondary<Go to ISI>://000077833700022-
heal.journalNameEmbo Journalen
heal.journalTypepeer reviewed-
heal.languageen-
heal.publicationDate1998-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιώνel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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