Aminoacylation of Proteins: New Targets for the Old ARSenal

Publication date: 9 January 2018
Source:Cell Metabolism, Volume 27, Issue 1
Author(s): Seyed Mehdi Jafarnejad, Sung-Hoon Kim, Nahum Sonenberg
Besides charging tRNAs with their cognate amino acids, aminoacyl-tRNA synthetases (ARSs) are involved in a plethora of non-canonical functions, including development, immune response, and angiogenesis. In this issue of Cell Metabolism, He et al. (2018) report a novel biochemical function of ARSs: posttranslational addition of amino acids to lysine residues in proteins.

Teaser

Besides charging tRNAs with their cognate amino acids, aminoacyl-tRNA synthetases (ARSs) are involved in a plethora of non-canonical functions, including development, immune response, and angiogenesis. In this issue of Cell Metabolism, He et al. (2018) report a novel biochemical function of ARSs: posttranslational addition of amino acids to lysine residues in proteins.


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