Aminoacylation of Proteins: New Targets for the Old ARSenal

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Aminoacylation of Proteins: New Targets for the Old ARSenal Seyed Mehdi Jafarnejad, Sung-Hoon Kim, Nahum Sonenberg Cell Metabolism Volume 27, Issue 1, Pages 1-3 (January 2018) DOI: 10.1016/j.cmet.2017.12.012 Copyright © 2017 Elsevier Inc. Terms and Conditions

Figure 1 Dual Role of ARSs in Aminoacylation of tRNAs and Proteins Left: aminoacylation of tRNA by ARSs. The 3′ end of tRNAs are charged with amino acids using activated aminoacyl-adenylate intermediates by ARSs. The aminoacylated tRNA is recruited to the ribosome during mRNA translation. Right: aminoacylation of lysine residues in proteins by ARSs. The high-energy aminoacyl-adenylate intermediate is charged onto lysine residues in proteins by ARSs. Lysine aminoacylation impacts substrate-specific functions in diverse physiological processes. Lysine aminoacylation is reversible by removing the aminoacyl group from the lysine by NAD+-dependent deacetylases. Cell Metabolism 2018 27, 1-3DOI: (10.1016/j.cmet.2017.12.012) Copyright © 2017 Elsevier Inc. Terms and Conditions