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dc.contributor.authorTurcu, Diana Cornelia
dc.contributor.authorLillehaug, Johan R.
dc.contributor.authorSeo, Hee-Chan
dc.date.accessioned2020-05-03T16:07:47Z
dc.date.available2020-05-03T16:07:47Z
dc.date.issued2019-12
dc.PublishedTurcu D, Lillehaug JR, Seo H. SIX3 and SIX6 interact with GEMININ via C-terminal regions. Biochemistry and Biophysics Reports. 2019;20eng
dc.identifier.issn2405-5808en_US
dc.identifier.urihttp://hdl.handle.net/1956/22068
dc.description.abstractThe histoarchitecture and function of eye and forebrain depend on a well-controlled balance between cell proliferation and differentiation. For example, the binding of the cell cycle regulator GEMININ to CDT1, which is a part of the pre-replication complex, promotes cell differentiation. Homeodomain transcription factors SIX3 and SIX6 also interact with GEMININ of which SIX3-GEMININ interaction promotes cell proliferation, whereas the nature of SIX6-GEMININ interaction has not been studied to date. We investigated SIX3/SIX6 and GEMININ interactions using bimolecular fluorescence complementation, surface plasmon resonance and isothermal titration calorimetry. Interactions between SIX3/SIX6 and GEMININ were detected in mammalian cells in culture. The presence of the C-terminal regions of SIX3 and SIX6 proteins, but not their SIX domains or homeodomains as previously thought, were required for interaction with GEMININ. Interestingly, the disordered C- and N- terminal regions of GEMININ were involved in binding to SIX3/SIX6. The coiled-coil region of GEMININ, which is the known protein-binding domain and also interacts with CDT1, was not involved in GEMININ-SIX3/SIX6 interaction. Using SPR and ITC, SIX3 bound GEMININ with a micromolar affinity and the binding stoichiometry was 1:2 (SIX3 - GEMININ). The present study gives new insights into the binding properties of SIX proteins, especially the role of their variable and disordered C-terminal regions.en_US
dc.language.isoengeng
dc.publisherElsevieren_US
dc.rightsAttribution CC BYeng
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/eng
dc.subjectSIX3eng
dc.subjectSIX6eng
dc.subjectGEMININCell-cycle regulationeng
dc.subjectBimolecular fluorescence complementation (BiFC)eng
dc.subjectSurface plasmon resonance (SPR)eng
dc.subjectIsothermal titration calorimetry (ITC)eng
dc.subjectProtein interactioneng
dc.titleSIX3 and SIX6 interact with GEMININ via C-terminal regionsen_US
dc.typePeer reviewed
dc.typeJournal article
dc.date.updated2020-01-10T13:25:08Z
dc.description.versionpublishedVersionen_US
dc.rights.holderCopyright 2019 The Authorsen_US
dc.identifier.doihttps://doi.org/10.1016/j.bbrep.2019.100695
dc.identifier.cristin1764561
dc.source.journalBiochemistry and Biophysics Reports


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