4.5 Review

Translational Fidelity during Bacterial Stresses and Host Interactions

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Summary: Editing mechanisms are crucial for correct amino acid incorporation during protein synthesis. Editing-deficient aaRSs have been found in host-dependent organisms. In this study, a previously unknown hyperaccurate mutation, L287F, was identified in the amino acid activation site of MmPheRS. It was also discovered that m-Tyr, a toxic oxidation byproduct of Phe, is poorly discriminated by MmPheRS activation and is not subjected to editing. Furthermore, expressing MmPheRS and the hyperaccurate variants makes E. coli susceptible to m-Tyr stress.

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Summary: This study reveals a previously unknown linkage between translational fidelity and bacterial fitness under bile stress, showing that increased translational fidelity contributes to the fitness of Salmonella upon bile salt exposure, and the improved fitness depends on an increased level of intracellular ATP.
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Escherichia coli alanyl-tRNA synthetase maintains proofreading activity and translational accuracy under oxidative stress

Arundhati Kavoor et al.

Summary: Aminoacyl-tRNA synthetases (aaRSs) are enzymes that maintain translational accuracy and cellular viability. Recent studies show that oxidation can affect aaRS functions, but has minimal impact on alanyl-tRNA synthetase (AlaRS).

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Oxidation alters the architecture of the phenylalanyl-tRNA synthetase editing domain to confer hyperaccuracy

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Hong Zhang et al.

Summary: Aminoacyl-tRNA synthetases are crucial enzymes for protein synthesis, and mutations in these enzymes can lead to neurological disorders. Editing defects in alanyl-tRNA synthetase (AlaRS) cause neurodegeneration in mice and microcephaly in humans, but the cellular impact in eukaryotes is not well understood. This study reveals that AlaRS editing defects activate the general amino acid control pathway, attenuate the heatshock response, downregulate carbon metabolism, and inhibit protein synthesis in yeast cells, contrasting with effects seen in other aaRSs editing deficiencies. Supplying extra carbon source partially rescues the heat sensitivity caused by AlaRS editing deficiency.

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