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Review

The aminoacyl-tRNA synthetases of Drosophila melanogaster

, , &
Pages 53-61 | Received 18 Aug 2015, Accepted 18 Sep 2015, Published online: 13 Jan 2016
 

Abstract

Aminoacyl-tRNA synthetases (aaRSs) ligate amino acids to their cognate tRNAs, allowing them to decode the triplet code during translation. Through different mechanisms aaRSs also perform several non-canonical functions in transcription, translation, apoptosis, angiogenesis and inflammation. Drosophila has become a preferred system to model human diseases caused by mutations in aaRS genes, to dissect effects of reduced translation or non-canonical activities, and to study aminoacylation and translational fidelity. However, the lack of a systematic annotation of this gene family has hampered such studies. Here, we report the identification of the entire set of aaRS genes in the fly genome and we predict their roles based on experimental evidence and/or orthology. Further, we propose a new, systematic and logical nomenclature for aaRSs. We also review the research conducted on Drosophila aaRSs to date. Together, our work provides the foundation for further research in the fly aaRS field.

Disclosure of Potential Conflicts of Interest

No potential conflicts of interest were disclosed.

Acknowledgments

We thank Rémy Bruggmann for his support on the bioinformatics side.

Supplemental Material

Supplemental data for this article can be accessed on the publisher's website.

Author Contributions

J.L. and S.J.M. performed the analysis, J.L. and W.H.G. constructed the phylogenetic trees, J.L. prepared the manuscript, S.J.M. and B.S. contributed to and edited the manuscript.

Funding

S.J.M. is supported by the FlyBase NIH/NHGRI grant U41HG000739 (W.M. Gelbart, Harvard University, PI; N.H. Brown, University of Cambridge, coPI). J.L. was supported by Cancer Research Switzerland and a SNF grant to B.S., and by a SNSF Early Postdoc Fellowship.