Cdc123-mediated assembly of the translation factor eIF2: mechanism and significance (B10)

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To define the mechanism by which the ATP-grasp protein Cdc123 assembles the hetero-trimeric eIF2 complex we will continue the genetic and biochemical characterization of yeast Cdc123 mutants, employ advanced NMR methods to study protein associations and dynamics, search for a covalent eIF2 modification by SILAC mass spectrometry, and study the in vivo association of eIF2 with the initiator tRNA by RNA immunoprecipitation. To understand the anti-proliferative effect associated with chronic dysfunction of Cdc123 and eIF2, we will profile gene expression, specifically mRNA translation, by RNA-sequencing based methods.