Abstract
The translation elongation factor-1 (EF-1) contains of four different subunits. They are designated EF-1α, EF-1β, EF-1β' and EF-1γ in plants. EF-1α catalyzes GTP-dependent binding of aa-tRNA to the ribosome, and both EF-1β and EF-1β' catalyzes the GDP/GTP exchange on EF-1α. However, the function of EF-1γ in protein biosynthesis remains unknown. In this study, we analyzed the binding between EF-1γ and other EF-1 subunits to know the subunit composition in plant. In addition, a yeast two-hybrid library was screened to identify novel candidates that interact to EF-1γ.
A yeast two-hybrid assay showed the interaction of EF-1γ with EF-1α, EF-1β and EF-1γ. This result suggests that EF-1γ can form homodimers in the cells. Furthermore, we identified a ribosomal protein L30 as a novel EF-1γ interactor. The interactions between both proteins were also confirmed by other binding assays.
