Skip to main content
Log in

Cysteine homeostasis under inhibition of protein synthesis in Escherichia coli cells

  • Original Article
  • Published:
Amino Acids Aims and scope Submit manuscript

Abstract

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.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Subscribe and save

Springer+ Basic
EUR 32.99 /Month
  • Get 10 units per month
  • Download Article/Chapter or Ebook
  • 1 Unit = 1 Article or 1 Chapter
  • Cancel anytime
Subscribe now

Buy Now

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6
Fig. 7
Fig. 8
Fig. 9
Fig. 10

Similar content being viewed by others

References

Download references

Acknowledgements

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.

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Galina V. Smirnova.

Ethics declarations

Conflict of interest

The authors declare that they have no conflict of interest.

Ethical approval

This article does not contain any studies with human participants or animals performed by any of the authors.

Additional information

Handling Editor: P. Fechter.

Publisher's Note

Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

Electronic supplementary material

Below is the link to the electronic supplementary material.

Fig.

 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

Supplementary material 2 (PDF 32 kb)

Supplementary material 3 (DOC 40 kb)

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

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). https://doi.org/10.1007/s00726-019-02795-2

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s00726-019-02795-2

Keywords

Navigation