Decoding the impact of disease-causing mutations in an essential aminoacyl-tRNA synthetase.
J Biol Chem
; 297(6): 101386, 2021 12.
Article
in En
| MEDLINE
| ID: mdl-34752820
ABSTRACT
Aminoacyl-tRNA synthetases are housekeeping enzymes that catalyze the specific attachment of amino acids onto cognate tRNAs, providing building blocks for ribosomal protein synthesis. Owing to the absolutely essential nature of these enzymes, the possibility that mutations in their sequence could be the underlying cause of diseases had not been foreseen. However, we are learning of patients bearing familial mutations in aminoacyl-tRNA synthetases at an exponential rate. In a recent issue of JBC, Jin et al. analyzed the impact of two such mutations in the very special bifunctional human glutamyl-prolyl-tRNA synthetase and convincingly decode how these mutations elicit the integrated stress response.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Amino Acyl-tRNA Synthetases
Limits:
Humans
Language:
En
Journal:
J Biol Chem
Year:
2021
Document type:
Article