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How Elongator Acetylates tRNA Bases

Nour-el-Hana Abbassi, Anna Biela, Sebastian Glatt, Ting‐Yu Lin

2020International Journal of Molecular Sciences39 citationsDOIOpen Access PDF

Abstract

Elp3, the catalytic subunit of the eukaryotic Elongator complex, is a lysine acetyltransferase that acetylates the C5 position of wobble-base uridines (U34) in transfer RNAs (tRNAs). This Elongator-dependent RNA acetylation of anticodon bases affects the ribosomal translation elongation rates and directly links acetyl-CoA metabolism to both protein synthesis rates and the proteome integrity. Of note, several human diseases, including various cancers and neurodegenerative disorders, correlate with the dysregulation of Elongator’s tRNA modification activity. In this review, we focus on recent findings regarding the structure of Elp3 and the role of acetyl-CoA during its unique modification reaction.

Topics & Concepts

Transfer RNAAcetylationWobble base pairTranslation (biology)Protein biosynthesisRNALysineRibosomal RNAProtein subunitAcetyltransferaseBiologyBiochemistryChemistryAmino acidMessenger RNAGeneRNA modifications and cancerRNA and protein synthesis mechanismsPeptidase Inhibition and Analysis
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