Next Article in Journal
Comparative Ubiquitome Analysis under Heat Stress Reveals Diverse Functions of Ubiquitination in Saccharina japonica
Next Article in Special Issue
Stearoyl-CoA Desaturase-2 in Murine Development, Metabolism, and Disease
Previous Article in Journal
SEIPIN: A Key Factor for Nuclear Lipid Droplet Generation and Lipid Homeostasis
Previous Article in Special Issue
Stearoyl-CoA Desaturase 1 Activity Determines the Maintenance of DNMT1-Mediated DNA Methylation Patterns in Pancreatic β-Cells
Review

How Elongator Acetylates tRNA Bases

1
Malopolska Centre of Biotechnology, Jagiellonian University, 30-387 Kraków, Poland
2
Postgraduate School of Molecular Medicine, Medical University of Warsaw, 02-091 Warsaw, Poland
*
Authors to whom correspondence should be addressed.
Int. J. Mol. Sci. 2020, 21(21), 8209; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21218209
Received: 19 October 2020 / Revised: 29 October 2020 / Accepted: 30 October 2020 / Published: 3 November 2020
(This article belongs to the Special Issue CoA in Health and Disease)
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. View Full-Text
Keywords: Elongator; Elp3; tRNA modification; acetyl-CoA; proteome balance; cancers; neurodegenerative diseases Elongator; Elp3; tRNA modification; acetyl-CoA; proteome balance; cancers; neurodegenerative diseases
Show Figures

Figure 1

MDPI and ACS Style

Abbassi, N.-e.-H.; Biela, A.; Glatt, S.; Lin, T.-Y. How Elongator Acetylates tRNA Bases. Int. J. Mol. Sci. 2020, 21, 8209. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21218209

AMA Style

Abbassi N-e-H, Biela A, Glatt S, Lin T-Y. How Elongator Acetylates tRNA Bases. International Journal of Molecular Sciences. 2020; 21(21):8209. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21218209

Chicago/Turabian Style

Abbassi, Nour-el-Hana, Anna Biela, Sebastian Glatt, and Ting-Yu Lin. 2020. "How Elongator Acetylates tRNA Bases" International Journal of Molecular Sciences 21, no. 21: 8209. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21218209

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop