Document Type
Article
Publication Date
6-2-2014
Abstract
Aminoacyl-tRNA synthetases use a variety of mechanisms to ensure fidelity of the genetic code and ultimately select the correct amino acids to be used in protein synthesis. The physiological necessity of these quality control mechanisms in different environments remains unclear, as the cost vs benefit of accurate protein synthesis is difficult to predict. We show that in Escherichia coli, a non-coded amino acid produced through oxidative damage is a significant threat to the accuracy of protein synthesis and must be cleared by phenylalanine-tRNA synthetase in order to prevent cellular toxicity caused by mis-synthesized proteins. These findings demonstrate how stress can lead to the accumulation of non-canonical amino acids that must be excluded from the proteome in order to maintain cellular viability.
Recommended Citation
Bullwinkle, T. J., Reynolds, N. M., Raina, M. Moghal, A. Matsa, E., Rajkovic, A., Kayadibi, H., Fazlollahi, F., Ryan, C., Howitz, N., Faull, K., Lazazzera, B. A. and Ibba, M. (2014) Oxidation of cellular amino acid pools leads to cytotoxic mistranslation of the genetic code. eLife 3:e02501. https://doi.org/10.7554/eLife.02501
Copyright
The authors
Creative Commons License
This work is licensed under a Creative Commons Attribution 3.0 License.
Included in
Amino Acids, Peptides, and Proteins Commons, Biochemistry Commons, Cellular and Molecular Physiology Commons, Molecular Biology Commons, Nucleic Acids, Nucleotides, and Nucleosides Commons, Other Biochemistry, Biophysics, and Structural Biology Commons
Comments
This article was originally published in eLife, volume 3, in 2014. https://doi.org/10.7554/eLife.02501