BMB Section Seminar: "A novel lysine specific methyltransferase that induces dynamic methylation in human eukaryotic elongation factor 1 alpha (eEF1A)"
Dr. Jedrzej Mieczyslaw Malecki, Falnes Group, BMB, Department of Biosciences, University of Oslo
Lysine methylation is abundant on histone proteins, representing a dynamic regulator of chromatin state and gene activity, but is also frequent on many non-histone proteins, including eukaryotic elongation factor 1 alpha (eEF1A). However, the functional significance of eEF1A methylation remains obscure, and it has remained unclear whether eEF1A methylation is dynamic and subject to active regulation. We demonstrated, using a wide range of in vitro and in vivo approaches, that the previously uncharacterized human methyltransferase (METTLN) specifically targets one of the lysine residues in eEF1A. Interestingly, eEF1A methylation at this residue showed strong variation across different tissues and cell lines, and was induced by altering growth conditions or by treatment with certain stress-inducing drugs. In summary, we characterized a novel lysine-specific methyltransferase responsible for methylation of a particular lysine residue in eEF1A, and showed that this modification is dynamic, inducible, and likely of regulatory importance.