Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2020 Mar;11(2):e1564.
doi: 10.1002/wrna.1564. Epub 2019 Aug 15.

RNA mimicry in post-transcriptional regulation by aminoacyl tRNA synthetases

Ofri Levi  1 , Shahar Garin  1 , Yoav Arava  1
Affiliations
Review

RNA mimicry in post-transcriptional regulation by aminoacyl tRNA synthetases

Ofri Levi et al. Wiley Interdiscip Rev RNA. 2020 Mar.

Abstract

Aminoacyl tRNA synthetases (aaRS) are well studied for their roles in tRNA charging with cognate amino acid. Nevertheless, numerous lines of evidence indicate that these proteins have roles other than tRNA charging. These include coordination of cellular signaling cascades, induction of cytokines outside the cell and transcription regulation. Herein, we focus on their roles in post-transcriptional regulation of mRNA expression. We describe functions that are related to antitermination of transcription, RNA splicing and mRNA translation. Cases were recognition of mRNA by the aaRS involves recognition of tRNA-like structures are described. Such recognition may be achieved by repurposing tRNA-binding domains or through domains added to the aaRS later in evolution. Furthermore, we describe cases in which binding by aaRS is implicated in autogenous regulation of expression. Overall, we propose RNA-mimicry as a common mode of interaction between aaRS and mRNA which allows efficient expression regulation. This article is categorized under: RNA Processing > tRNA Processing RNA Interactions with Proteins and Other Molecules > Protein-RNA Recognition RNA Interactions with Proteins and Other Molecules > Protein-RNA Interactions: Functional Implications Translation > Translation Regulation.

Keywords: RNA-mimicry; aminoacyl tRNA synthetase; autogenous regulation; post-transcriptional regulation; tRNA.

PubMed Disclaimer

References

REFERENCES

    1. Akins, R. A., & Lambowitz, A. M. (1987). A protein required for splicing group I introns in Neurospora mitochondria is mitochondrial tyrosyl-tRNA synthetase or a derivative thereof. Cell, 50(3), 331-345.
    1. Ames, B. N., Tsang, T. H., Buck, M., & Christman, M. F. (1983). The leader mRNA of the histidine attenuator region resembles tRNAHis: Possible general regulatory implications. Proceedings of the National Academy of Sciences of the United States of America, 80(17), 5240-5242.
    1. Andreev, D. E., Hirnet, J., Terenin, I. M., Dmitriev, S. E., Niepmann, M., & Shatsky, I. N. (2012). Glycyl-tRNA synthetase specifically binds to the poliovirus IRES to activate translation initiation. Nucleic Acids Research, 40(12), 5602-5614. https://doi.org/10.1093/nar/gks182
    1. Archibold, E. R., & Williams, L. S. (1972). Regulation of synthesis of methionyl-, prolyl-, and threonyl-transfer ribonucleic acid synthetases of Escherichia coli. Journal of Bacteriology, 109(3), 1020-1026.
    1. Arnez, J. G., & Moras, D. (1997). Structural and functional considerations of the aminoacylation reaction. Trends in Biochemical Sciences, 22(6), 211-216.

Publication types

LinkOut - more resources