UNIVERSITY OF MALTA LIFE SCIENCE RESEARCH SEMINARS Web: http://www.um.edu.mt/events/scisem/ Email: [email protected] Abstract form Title: Presenter: Contact address: Tel: Fax: Email: Presentation date: Isolation of a novel GABPα interactor Byron Baron [email protected] 21 November 2011 Abstract GA-binding protein α (GABPα), which is also known as NRF-2 or E4TF-1, is the only ETS factor that forms obligate heteromeric protein complexes due to the lack of a transactivation domain. It forms heterodimers with GABPγ or heterotetramers with GABPβ and can also recruit other co-factors. This allows GABP to cover a multitude of roles in transcription control. A methyltranserase (called E4TF1-binding methyltransferase - EBM) was isolated as a physical interactor of GABPα using a Yeast-Two Hybrid Assay and verified by co-IP. In a luciferase assay using the Target of Methylation-induced Silencing (TMS1) and Thrombopoietin (TPO) promoters, which are regulated by the GABP complex, EBM was shown to generally increase the promoter activity in the presence of over-expressed GABPα. This interaction offers a window into understanding and modulating GABPα-implicated pathogenesis such breast cancer, Acute Megakaryoblastic Leukemia (AMKL), Adenylosuccinate Lyase (ADSL) disease and Congenital Myasthenic Syndrome.