Che1/AATF interacts with subunits of the histone acetyltransferase core module of SAGA complexes

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dc.contributor.authorCaliskan, Gizem
dc.contributor.authorBaris, Ikbal C.
dc.contributor.authorAyaydin, Ferhan
dc.contributor.authorDobson, Melanie J.
dc.contributor.authorSenarisoy, Muge
dc.contributor.authorBoros, Imre M.
dc.contributor.authorTopcu, Zeki
dc.contributor.authorZencir, Sevil
dc.date.accessioned2019-10-27T10:47:08Z
dc.date.available2019-10-27T10:47:08Z
dc.date.issued2017
dc.departmentEge Üniversitesien_US
dc.description.abstractGeneral Control Non-derepressible 5 (GCN5) and Alteration/Deficiency in Activation 2 and 3 proteins (ADA2 and ADA3, respectively) are subunits of the Histone AcetylTransferase (HAT) module of SAGA-and ATAC-type co-activators. We previously reported four new interacting partners of human ADA3 identified by screening a human fetal brain cDNA library using yeast two hybrid technology. One of these partners was Apoptosis-Antagonizing Transcription Factor (AATF), also known as Che-1, an RNA polymerase II-binding protein with a number of roles in different cellular processes including regulation of transcription, cell proliferation, cell cycle control, DNA damage responses and apoptosis. Che-1/AATF is a potential therapeutic target for cancer treatments. In this study, we aimed to identify whether besides ADA3, other components of the HAT modules of SAGA and ATAC complexes, human ADA2 and GCN5 also interact with Che-1/AATF. Co-immunoprecipitation and co-localization experiments were used to demonstrate association of AATF both with two ADA2 isoforms, ADA2A and ADA2B and with GCN5 proteins in human cells and yeast two-hybrid assays to delineate domains in the ADA2 and GCN5 proteins required for these interactions. These findings provide new insights into the pathways regulated by ADA-containing protein complexes.en_US
dc.description.sponsorshipTurkish Scientific and Technological Research Assembly [112T429]; Hungarian NRDIO [GINOP-2.3.2-15-2016-00020]en_US
dc.description.sponsorshipThis work was supported by the Turkish Scientific and Technological Research Assembly (112T429) (Dr. Sevil Zencir), and Hungarian NRDIO-GINOP-2.3.2-15-2016-00020 (Prof Imre M. Boros). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.en_US
dc.identifier.doi10.1371/journal.pone.0189193en_US
dc.identifier.issn1932-6203
dc.identifier.issue12en_US
dc.identifier.pmid29232376en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.urihttps://doi.org/10.1371/journal.pone.0189193
dc.identifier.urihttps://hdl.handle.net/11454/31385
dc.identifier.volume12en_US
dc.identifier.wosWOS:000417698200025en_US
dc.identifier.wosqualityQ1en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.publisherPublic Library Scienceen_US
dc.relation.ispartofPlos Oneen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.titleChe1/AATF interacts with subunits of the histone acetyltransferase core module of SAGA complexesen_US
dc.typeArticleen_US

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