Aminoacylation of Proteins: New Targets for the Old ARSenal

Aminoacylation of Proteins: New Targets for the Old ARSenal

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: po...

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Veröffentlicht in:Cell metabolism 2018-01, Vol.27 (1), p.1-3
Hauptverfasser: Jafarnejad, Seyed Mehdi, Kim, Sung-Hoon, Sonenberg, Nahum
Format: Artikel
Sprache:eng
Schlagworte:
Amino Acids
Amino Acyl-tRNA Synthetases
Aminoacylation
Lysine
RNA, Transfer
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Zusammenfassung: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. 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.
ISSN:1550-4131
1932-7420
DOI:10.1016/j.cmet.2017.12.012