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Cysteine homeostasis under inhibition of protein synthesis in Escherichia coli cells

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Increased intracellular cysteine poses a potential danger to cells due to the high ability of cysteine to reduce free iron and promote the Fenton reaction. Here, we studied ways to maintain cysteine homeostasis in E. coli cells while inhibiting protein synthesis with valine or chloramphenicol. When growing wild-type bacteria on minimal medium with sulfate, an excess of cysteine resulting from the inhibition of protein synthesis is mainly incorporated into glutathione (up to 90%), which, therefore, can be considered as cysteine buffer. The share of hydrogen sulfide, which is the product of cysteine degradation by cysteine synthase B (CysM), does not exceed 1–3%, the rest falls on free cysteine, exported from cells. As a result, intracellular free cysteine is maintained at a low level (about 0.1 mM). The lack of glutathione in the gshA mutant increases H2S production and excretion of cysteine and leads to a threefold increase in the level of intracellular cysteine in response to valine and chloramphenicol. The relA mutants, exposed to valine, produce more H2S, dramatically accelerate the export of glutathione and accumulate more cysteine in the cytoplasm than their parent, which indicates that the regulatory nucleotide (p)ppGpp is involved in maintaining cysteine homeostasis. Disruption of cysteine homeostasis in gshA and relA mutants increases their sensitivity to peroxide stress.

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This work was performed according to state assignment 01201353249, and was also supported by a grant from the Program of the Ural Branch of the Russian Academy of Sciences AAAA-A18-118041890005-1 and by a grant from the Russian Foundation of Basic Research 19-04-00888.

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Correspondence to Galina V. Smirnova.

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 1S Changes in the color of lead acetate–soaked paper strips in untreated culture (control) and after treatment of E. coli with valine (a) and chloramphenicol (b). E. coli BW25113 (wt), JW2663 (ΔgshA), JW2755 (ΔrelA), and NM4861 (ΔrelAΔgshA) were grown in M9 medium with glucose to OD600 of 0.4, and then 4.3 mM valine or 77 µM chloramphenicol was added. Lead acetate–soaked paper strips, which were affixed in culture flasks above the level of the liquid culture, were successively replaced every 15 min and photographed. Representative samples from 3-6 independent experiments are shown

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Smirnova, G.V., Tyulenev, A.V., Bezmaternykh, K.V. et al. Cysteine homeostasis under inhibition of protein synthesis in Escherichia coli cells. Amino Acids 51, 1577–1592 (2019).

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