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Cardenal Peralta, Cristina; Vandroux, Paul; Neumann-Arnold, Lea; Panvert, Michel; Fagart, Jérôme; Seufert, Wolfgang; Mechulam, Yves; Schmitt, Emmanuelle
Journal of structural biology, 09/2023, Letnik: 215, Številka: 3Journal Article
Display omitted •Crystal structure of human Cdc123 bound to domain 3 of eIF2γ.•ATP is required for human Cdc123 function in eIF2 assembly.•Model of the mechanism of action of human Cdc123.•Structural support for understanding eIF2γ mutations responsible for MEHMO diseases. Eukaryotic initiation factor 2 (eIF2) plays a key role in protein synthesis and in its regulation. The assembly of this heterotrimeric factor is facilitated by Cdc123, a member of the ATP grasp family that binds the γ subunit of eIF2. Notably, some mutations related to MEHMO syndrome, an X-linked intellectual disability, affect Cdc123-mediated eIF2 assembly. The mechanism of action of Cdc123 is unclear and structural information for the human protein is awaited. Here, the crystallographic structure of human Cdc123 (Hs-Cdc123) bound to domain 3 of human eIF2γ (Hs-eIF2γD3) was determined. The structure shows that the domain 3 of eIF2γ is bound to domain 1 of Cdc123. In addition, the long C-terminal region of Hs-Cdc123 provides a link between the ATP and Hs-eIF2γD3 binding sites. A thermal shift assay shows that ATP is tightly bound to Cdc123 whereas the affinity of ADP is much smaller. Yeast cell viability experiments, western blot analysis and two-hybrid assays show that ATP is important for the function of Hs-Cdc123 in eIF2 assembly. These data and recent findings allow us to propose a refined model to explain the mechanism of action of Cdc123 in eIF2 assembly.
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