How Elongator Acetylates tRNA Bases

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

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.

Citation

Abbassi, N., Biela, A., Glatt, S., & Lin, T. (2020). How Elongator Acetylates tRNA Bases. International Journal of Molecular Sciences, 21(21), 8209. https://doi.org/10.3390/ijms21218209

• Journal Article Type: Article
• Acceptance Date: Oct 30, 2020
• Online Publication Date: Nov 3, 2020
• Publication Date: Nov 3, 2020
• Deposit Date: Nov 2, 2023
• Journal: International Journal of Molecular Sciences
• Print ISSN: 1661-6596
• Publisher: MDPI
• Peer Reviewed: Peer Reviewed
• Volume: 21
• Issue: 21
• Pages: 8209
• DOI: https://doi.org/10.3390/ijms21218209
• Keywords: Inorganic Chemistry; Organic Chemistry; Physical and Theoretical Chemistry; Computer Science Applications; Spectroscopy; Molecular Biology; General Medicine; Catalysis
• Public URL: https://durham-repository.worktribe.com/output/1875030
• Additional Information: This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).