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tRNA synthetase: tRNA aminoacylation and beyond
Author(s) -
Pang Yan Ling Joy,
Poruri Kiranmai,
Martinis Susan A.
Publication year - 2014
Publication title -
wiley interdisciplinary reviews: rna
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.225
H-Index - 71
eISSN - 1757-7012
pISSN - 1757-7004
DOI - 10.1002/wrna.1224
Subject(s) - aminoacylation , transfer rna , aminoacyl trna synthetase , rna , translation (biology) , amino acyl trna synthetases , protein biosynthesis , biology , genetic code , function (biology) , biochemistry , amino acid , computational biology , genetics , messenger rna , gene
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 has 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. WIREs RNA 2014, 5:461–480. doi: 10.1002/wrna.1224 This article is categorized under: RNA Structure and Dynamics > Influence of RNA Structure in Biological Systems RNA Interactions with Proteins and Other Molecules > RNA–Protein Complexes Translation > Translation Mechanisms RNA Processing > tRNA Processing