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Information × Registration Number 0120U104519, ( 0220U104283 0221U106019 0221U106564 ) R & D request Title Study on the structural features of human translation elongation complex eEF1B Head Negrutskyii Borys S., Доктор біологічних наук Registration Date 23-10-2020 Organization Institute of Molecular Biology and Genetics of NAS of Ukraine popup.description1 The aim of our project is to disclose for the first time a spatial organization of the human translation elongation complex eEF1B. eEF1B is a key protein complex participating in the ribosomal polypeptide elongation step. It comprises three different subunits (eEF1Bα, eEF1Bβ and eEF1Bγ), all of them are predicted to belong to the partially disordered proteins family Information about the spatial organization of the eEF1B complex is indispensable for understanding the fundamental translation mechanisms. In addition, mutations in the human genes encoding eEF1Bα and eEF1Bβ subunits of eEF1B have now been identified as causes of neurodevelopmental disorders. Despite the high priority of understanding the structural details of eEF1B organization, the spatial organization of neither the full eEF1B complex nor its subunits is known. This failure might be explained by the presence of long disordered regions in these structures, leading to significant instability and aggregation of the subunits in vitro. We established this aim as we have developed the procedures for gentle isolation of non-aggregated individual eEF1B subunits overexpressed in E.coli that should greatly facilitate biophysical measurements. To achieve the goal we will use a combination of molecular biology, biophysical and computational methods. They will provide solid data on the multimeric state and stoichiometry of subunits in the complexes as well as clear and detailed identification of the protein regions involved into maintaining the protein structure or protected by other protein in the case of protein-protein interaction. Using all obtained experimental and literature data to computationally arrange all subunits inside the eEF1B complex, with subsequent verification of the structure by HDX-MS measurements, will permit to create first atomistic model of the eEF1B complex. popup.nrat_date 2024-12-10 Close
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Head: Negrutskyii Borys S.. Study on the structural features of human translation elongation complex eEF1B.
Institute of Molecular Biology and Genetics of NAS of Ukraine. № 0120U104519
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