The Aminoacyl-tRNA Synthetases and Their Protein–Protein Interactions
- 1Department of Chemistry, Wayne State University, 5101 Cass Avenue, Detroit, MI 48201, USA
Abstract
The canonical role of each aminoacyl-tRNA synthetase (ARS) is to correctly aminoacylate its cognate tRNA(s) with its corresponding amino acid; the resultant aminoacyl-tRNAs drive protein translation. However, decades of work, particularly in eukaryotes, have led to the elucidation of a variety of non-translational roles for these ubiquitous enzymes. Many canonical and non-canonical ARS activities rely on protein–protein interactions, and mutations are known that either disrupt these interactions or enable new ones in disease states. Fewer ARS–protein interactions are known in archaea and bacteria; these are mostly focused on connections that occur during translation but also include other interesting, multimeric complexes. This review focuses on physical ARS–protein interactions from all three domains of life. The functional impacts of many of these interactions, when known, are discussed.
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BibTeX
@article{hendrickson2026aminoacyltrna,
title = {{The Aminoacyl-tRNA Synthetases and Their Protein–Protein Interactions}},
author = {Tamara L. Hendrickson and Neal P. Bachert and Gabriella F. Mack and Nathaniel W. Buzenski and Brian C. Lee},
journal = {Biomolecules},
year = {2026},
month = oct,
doi = {10.3390/biom16111544},
url = {https://www.mdpi.com/2218-273X/16/11/1544},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - The Aminoacyl-tRNA Synthetases and Their Protein–Protein Interactions
AU - Tamara L. Hendrickson
AU - Neal P. Bachert
AU - Gabriella F. Mack
AU - Nathaniel W. Buzenski
AU - Brian C. Lee
PY - 2026
DA - 2026/10/23
JO - Biomolecules
DO - 10.3390/biom16111544
UR - https://www.mdpi.com/2218-273X/16/11/1544
AB - The canonical role of each aminoacyl-tRNA synthetase (ARS) is to correctly aminoacylate its cognate tRNA(s) with its corresponding amino acid; the resultant aminoacyl-tRNAs drive protein translation. However, decades of work, particularly in eukaryotes, have led to the elucidation of a variety of non-translational roles for these ubiquitous enzymes. Many canonical and non-canonical ARS activities rely on protein–protein interactions, and mutations are known that either disrupt these interactions or enable new ones in disease states. Fewer ARS–protein interactions are known in archaea and bacteria; these are mostly focused on connections that occur during translation but also include other interesting, multimeric complexes. This review focuses on physical ARS–protein interactions from all three domains of life. The functional impacts of many of these interactions, when known, are discussed.
SN - 2218-273X
ER -