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Analysis on the Interacting Domain of Human eRF3a with Survivin
Li Fang, Xiao Ruilin, Chai Baofeng*
Key Laboratory of Chemical Biology and Molecular Engineering, Ministry of Education, China;Institute of Biotechnology, Shanxi University, Taiyuan 030006, China
Abstract: In mammals, two genes, GSPT1 and GSPT2, encode two distinct forms of Class II polypeptide release factor eRF3, eRF3a and eRF3b, respectively. eRF3 is a GTPase associated with eRF1 in a complex that mediates the release of nascent polypeptides. Some studies indicated that eRF3 was involved in cell cycle regulation, cytoskeleton, apoptosis, and tumorigenesis. Survivin is the most powerful inhibitor of apoptosis gene ever found. In additional, survivin is involved in cell mitosis and angiogenesis etc. Both eRF3 and survivin are associated with the regulation of cell cycle and apoptosis. Our previous studies demonstrated that eRF3 interacted with survivin in vivo and in vitro. In this study, we have truncated eRF3a, and verified the interaction between eRF3a(1-72aa)/eRF3a(1-36aa) and survivin by using the yeast two-hybrid and pull-down assay, respectively. The results suggested that both eRF3a(1-72aa) and eRF3a(1-36aa) could interact with survivin, therefore, we concluded that their minimal interaction domain located amongst 1-36aa of eRF3a. Accordingly, the results provided the data supporting for further confirmation of the N terminal domain of eRF3 cooperating with survivin involved in cell cycle and apoptosis regulation.