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<scp>tRNA</scp> synthetase: <scp>tRNA</scp> aminoacylation and beyond

Authors :
Kiranmai Poruri
Yan Ling Joy Pang
Susan A. Martinis
Source :
WIREs RNA. 5:461-480
Publication Year :
2014
Publisher :
Wiley, 2014.

Abstract

The aminoacyl-tRNA synthetases are prominently known for their classic function in the first step of protein synthesis, where they bear the responsibility of setting the genetic code. Each enzyme is exquisitely adapted to covalently link a single standard amino acid to its cognate set of tRNA isoacceptors. These ancient enzymes have evolved idiosyncratically to host alternate activities that go far beyond their aminoacylation role and impact a wide range of other metabolic pathways and cell signaling processes. The family of aminoacyl-tRNA synthetases have also been suggested as a remarkable scaffold to incorporate new domains that would drive evolution and the emergence of new organisms with more complex function. Because they are essential, the tRNA synthetases have served as pharmaceutical targets for drug and antibiotic development. The recent unfolding of novel important functions for this family of proteins offers new and promising pathways for therapeutic development to treat diverse human diseases.

Details

ISSN :
17577012 and 17577004
Volume :
5
Database :
OpenAIRE
Journal :
WIREs RNA
Accession number :
edsair.doi.dedup.....9a755878336be8d50f6ad42aa7fcc277
Full Text :
https://doi.org/10.1002/wrna.1224