Identification of distinct SET/TAF-Ibeta domains required for core histone binding and quantitative characterisation of the interaction

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dc.contributor.authorKaretsou, Z.en
dc.contributor.authorEmmanouilidou, A.en
dc.contributor.authorSanidas, I.en
dc.contributor.authorLiokatis, S.en
dc.contributor.authorNikolakaki, E.en
dc.contributor.authorPolitou, A. S.en
dc.contributor.authorPapamarcaki, T.en
dc.date.accessioned2015-11-24T19:12:20Z
dc.date.available2015-11-24T19:12:20Z
dc.identifier.issn1471-2091-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/21058
dc.rightsDefault Licence-
dc.subjectAmino Acid Sequenceen
dc.subjectChromatin/metabolismen
dc.subjectChromosomal Proteins, Non-Histone/chemistry/*metabolismen
dc.subjectCircular Dichroismen
dc.subjectHistone Chaperonesen
dc.subjectHistones/*metabolismen
dc.subjectMolecular Chaperones/metabolismen
dc.subjectMolecular Sequence Dataen
dc.subjectMutant Proteins/metabolismen
dc.subjectProtein Bindingen
dc.subjectProtein Structure, Tertiaryen
dc.subjectRecombinant Proteins/metabolismen
dc.subjectSpectrometry, Fluorescenceen
dc.subjectTranscription Factors/chemistry/*metabolismen
dc.titleIdentification of distinct SET/TAF-Ibeta domains required for core histone binding and quantitative characterisation of the interactionen
heal.abstractBACKGROUND: The assembly of nucleosomes to higher-order chromatin structures is finely tuned by the relative affinities of histones for chaperones and nucleosomal binding sites. The myeloid leukaemia protein SET/TAF-Ibeta belongs to the NAP1 family of histone chaperones and participates in several chromatin-based mechanisms, such as chromatin assembly, nucleosome reorganisation and transcriptional activation. To better understand the histone chaperone function of SET/TAF-Ibeta, we designed several SET/TAF-Ibeta truncations, examined their structural integrity by circular Dichroism and assessed qualitatively and quantitatively the histone binding properties of wild-type protein and mutant forms using GST-pull down experiments and fluorescence spectroscopy-based binding assays. RESULTS: Wild type SET/TAF-Ibeta binds to histones H2B and H3 with Kd values of 2.87 and 0.15 microM, respectively. The preferential binding of SET/TAF-Ibeta to histone H3 is mediated by its central region and the globular part of H3. On the contrary, the acidic C-terminal tail and the amino-terminal dimerisation domain of SET/TAF-Ibeta, as well as the H3 amino-terminal tail, are dispensable for this interaction. CONCLUSION: This type of analysis allowed us to assess the relative affinities of SET/TAF-Ibeta for different histones and identify the domains of the protein required for effective histone recognition. Our findings are consistent with recent structural studies of SET/TAF-Ibeta and can be valuable to understand the role of SET/TAF-Ibeta in chromatin function.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.primary10.1186/1471-2091-10-10-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/19358706-
heal.identifier.secondaryhttp://www.biomedcentral.com/1471-2091/10/10-
heal.journalNameBMC Biochemen
heal.journalTypepeer-reviewed-
heal.languageen-
heal.publicationDate2009-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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