Structural highlights
Publication Abstract from PubMed
Eukaryotic elongation factor 2 (eEF2) is an abundant and essential component of the translation machinery. The biogenesis of this 93 kDa multi-domain protein is assisted by the chaperonin TRiC/CCT. Here, we show in yeast cells that the highly conserved protein Hgh1 (FAM203 in humans) is a chaperone that cooperates with TRiC in eEF2 folding. In the absence of Hgh1, a substantial fraction of newly synthesized eEF2 is degraded or aggregates. We solved the crystal structure of Hgh1 and analyzed the interaction of wild-type and mutant Hgh1 with eEF2. These experiments revealed that Hgh1 is an armadillo repeat protein that binds to the dynamic central domain III of eEF2 via a bipartite interface. Hgh1 binding recruits TRiC to the C-terminal eEF2 module and prevents unproductive interactions of domain III, allowing efficient folding of the N-terminal GTPase module. eEF2 folding is completed upon dissociation of TRiC and Hgh1.
Chaperone Function of Hgh1 in the Biogenesis of Eukaryotic Elongation Factor 2.,Monkemeyer L, Klaips CL, Balchin D, Korner R, Hartl FU, Bracher A Mol Cell. 2019 Mar 6. pii: S1097-2765(19)30054-1. doi:, 10.1016/j.molcel.2019.01.034. PMID:30876804[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Monkemeyer L, Klaips CL, Balchin D, Korner R, Hartl FU, Bracher A. Chaperone Function of Hgh1 in the Biogenesis of Eukaryotic Elongation Factor 2. Mol Cell. 2019 Mar 6. pii: S1097-2765(19)30054-1. doi:, 10.1016/j.molcel.2019.01.034. PMID:30876804 doi:http://dx.doi.org/10.1016/j.molcel.2019.01.034
