Malopolska Centre of Biotechnology, Jagiellonian University, 30-387 Kraków, Poland.
Postgraduate School of Molecular Medicine, Medical University of Warsaw, 02-091 Warsaw, Poland.
Int J Mol Sci. 2020 Nov 3;21(21):8209. doi: 10.3390/ijms21218209.
Elp3, the catalytic subunit of the eukaryotic Elongator complex, is a lysine acetyltransferase that acetylates the C5 position of wobble-base uridines (U) 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.
elp3,真核延伸因子复合物的催化亚基,是一种赖氨酸乙酰转移酶,可乙酰化 tRNA(转移 RNA)中摆动碱基 U 的 C5 位置。这种延伸因子依赖性反密码子碱基的 RNA 乙酰化影响核糖体翻译延伸率,并将乙酰辅酶 A 代谢与蛋白质合成率和蛋白质组完整性直接联系起来。值得注意的是,包括各种癌症和神经退行性疾病在内的几种人类疾病与延伸因子的 tRNA 修饰活性失调有关。在这篇综述中,我们重点介绍了最近关于 elp3 结构和乙酰辅酶 A 在其独特修饰反应中的作用的发现。