Resilience and proteome response of Escherichia coli to high levels of isoleucine mistranslation

Pranjic, Marija; Spät, Philipp; Semanjski Curkovic, Maja; Macek, Boris; Gruic-Sovulj, Ita; Mocibob, Marko

doi:10.1016/j.ijbiomac.2024.130068

Cited by 1 publication

(2 citation statements)

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“…We have also established that pre-incubation with Nva or 1.5 mmol/L Val before the addition of H 2 O 2 produced no beneficial effect of mistranslation against oxidative stress. Similar was reported by Pranjic et al ( 24 ), as their high-level isoleucine mistranslation in another IleRS editing-deficient strain lowered bacterial resilience and survival at elevated temperatures. However, when the editing-deficient strain IleRS(Ala 10 ) ED ─ in our study was pre-incubated with 0.75 mmol/L Val until it reached the early or mid-exponential growth and then was exposed to oxidative stress, it slightly outgrew the wild-type cultivated under the same conditions.…”

Section: Discussionsupporting

confidence: 87%

“…Aminoglycoside antibiotics, such as streptomycin and kanamycin, kill bacteria because they induce mistranslation and protein misfolding ( 23 ). In Escherichia coli mistranslation at isoleucine positions causes proteotoxic stress which provokes the SOS response and global proteome dysregulation and upregulates cellular apparatus to maintain proteostasis by increasing the levels of major chaperones, proteases, and disaggregase ClpB ( 24 ).…”

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Interplay between mistranslation and oxidative stress in Escherichia coli

Ević,

Rokov-Plavec

2024

Archives of Industrial Hygiene and Toxicology

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Mistakes in translation are mostly associated with toxic effects in the cell due to the production of functionally aberrant and misfolded proteins. However, under certain circumstances mistranslation can have beneficial effects and enable cells to preadapt to other stress conditions. Mistranslation may be caused by mistakes made by aminoacyl-tRNA synthetases, essential enzymes that link amino acids to cognate tRNAs. There is an Escherichia coli strain expressing isoleucyl-tRNA synthetase mutant variant with inactivated editing domain which produces mistranslated proteomes where valine (Val) and norvaline (Nva) are misincorporated into proteins instead of isoleucine. We compared this strain with the wild-type to determine the effects of such mistranslation on bacterial growth in oxidative stress conditions. When the cells were pre-incubated with 0.75 mmol/L Nva or 1.5 mmol/L Val or Nva and exposed to hydrogen peroxide, no beneficial effect of mistranslation was observed. However, when the editing-deficient strain was cultivated in medium supplemented with 0.75 mmol/L Val up to the early or mid-exponential phase of growth and then exposed to oxidative stress, it slightly outgrew the wild-type grown in the same conditions. Our results therefore show a modest adaptive effect of isoleucine mistranslation on bacterial growth in oxidative stress, but only in specific conditions. This points to a delicate balance between deleterious and beneficial effects of mistranslation.

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Section: Discussionsupporting

confidence: 87%

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confidence: 99%