Aminoacylation of Proteins: New Targets for the Old ARSenal

Seyed Mehdi Jafarnejad; Sung-Hoon Kim; Nahum Sonenberg

doi:10.1016/j.cmet.2017.12.012

Aminoacylation of Proteins: New Targets for the Old ARSenal

Cell Metab. 2018 Jan 9;27(1):1-3. doi: 10.1016/j.cmet.2017.12.012.

Authors

Seyed Mehdi Jafarnejad¹, Sung-Hoon Kim¹, Nahum Sonenberg²

Affiliations

¹ Goodman Cancer Research Center, McGill University, Montreal, QC H3A 1A3, Canada; Department of Biochemistry, McGill University, Montreal, QC H3A 1A3, Canada.
² Goodman Cancer Research Center, McGill University, Montreal, QC H3A 1A3, Canada; Department of Biochemistry, McGill University, Montreal, QC H3A 1A3, Canada. Electronic address: nahum.sonenberg@mcgill.ca.

PMID: 29320701
DOI: 10.1016/j.cmet.2017.12.012

Abstract

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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MeSH terms

Amino Acids
Amino Acyl-tRNA Synthetases
Aminoacylation*
Lysine*
RNA, Transfer

Substances

Amino Acids
RNA, Transfer
Amino Acyl-tRNA Synthetases
Lysine