Deciphering the Structures of the Tef3/eEF1Ba and Tef4/eEF1Ba complexes from yeast through Integrative Structural Biology

Protein translation is one of the most energy consuming process in cells. Although translation can be modulated at various steps—initiation, elongation, termination, and ribosome recycling—most studies focus on the initiation step. However, the elongation step is central to determining protein fate and regulating protein translation under stress. Among eukaryotes, fungi have the simplest elongation complex (eEF1), being composed of only 3 subunits in comparison to 4 and 5 respectively for plants and humans. These subunits are the guanidine nucleotide binding subunit eEF1A, and the two eEF1Bα and eEF1Bγ that compose the nucleotide exchange factor eEF1B. The main objectives of the project are to (i) identify the factors that destabilize the eEF1B complex, (ii) provide structural insights of the mechanism, and (iii) evaluate the impact of this dissociation in vivo in the model organism Saccharomyces cerevisiae.