Expression of cadaverine biosynthesis genes under superoxide oxidative stress

Main Article Content

Anna V. Akhova
Polina A. Sekatskaya
Alexander G. Tkachenko

Abstract

The effect of redox-cycling methyl viologen, which causes the production of superoxide and formation of oxidative stress in bacterial cells, on the expression of the cadA and ldcC genes was studied. Gene expression was assessed using Escherichia coli strains bearing reporter gene fusions of the promoters of the studied genes with the structural part of the lacZ gene; expression values are given in Miller units. Bacteria were grown in batch cultures in LB broth without agitation or with agitation at 100 r.p.m. We have shown that exposure to methyl viologen, which leads to the induction of the nfo gene included in the soxRS regulon of oxidative defense (a long-term increase in the expression level by 10 times), led to a slight and short-term increase in the expression of the cadA and ldcC genes (by a maximum of 1.4 times, no longer than 1 h). An increase in the strength of oxidative stress due to elevated agitation/aeration had no effect on the expression of the cadA and ldcC genes. Methyl viologen at the concentrations used (1-100 μg/mL) did not affect the number of colony-forming units in the culture. Thus, non-lethal superoxide stress caused by exposure of bacteria to methyl viologen had little effect on the expression of the ldcC and cadA genes compared to the genes included in the soxRS regulon, which were strongly induced under these conditions.

Article Details

How to Cite
Akhova А. В., Sekatskaya П. А. ., & Tkachenko А. Г. . (2023). Expression of cadaverine biosynthesis genes under superoxide oxidative stress. Bulletin of Perm University. Biology, (1), 51–57. https://doi.org/10.17072/1994-9952-2023-1-51-57
Section
Микробиология
Author Biographies

Anna V. Akhova, Institute of Ecology and Genetics of Microorganisms UB RAS, Perm, Russia

Cand. Sc. (Biol), scientific researcher of the laboratory of microbial adaptation

Polina A. Sekatskaya, Institute of Ecology and Genetics of Microorganisms UB RAS, Perm, Russia

Laboratory assistant of the laboratory of microbial adaptation

Alexander G. Tkachenko, Institute of Ecology and Genetics of Microorganisms UB RAS, Perm, Russia

Doc. Sci. (Med), head of the laboratory of microbial adaptation

References

Akhova A. et al. Cadaverine biosynthesis contributes to decreased Escherichia coli susceptibility to anti-biotics // Research in Microbiology. 2021. Vol. 172. P. 103881. DOI: 10.1016/j.resmic.2021.103881.

Ding H., Demple B. Direct nitric oxide signal transduction via nitrosylation of iron-sulfur centers in the SoxR transcription activator // Proceeding of the National Academy of Sciences of the USA. 2000. Vol. 97. P. 5146–5150. DOI: 10.1073/pnas.97.10.5146.

Felix J. et al. Structural and functional analysis of the Francisella lysine decarboxylase as a key actor in oxidative stress resistance // Scientific Reports. 2021. Vol. 11. P. 972. DOI: 10.1038/s41598-020-79611-5.

Gu M., Imlay J.A. The SoxRS response of Escherichia coli is directly activated by redox-cycling drugs ra-ther than by superoxide // Molecular Microbiology. 2011. Vol. 79. P. 136–150. DOI: 10.1111/j.1365-2958.2010.07520.x.

Hidalgo E. et al. Binuclear [2Fe-2S] clusters in the Escherichia coli SoxR protein and role of the metal centers in transcription // Journal of Biological Chemistry. 1995. Vol. 270. P. 20908–20914. DOI: 10.1074/jbc.270.36.20908.

Kim J.S., Choi S.H., Lee J.K. Lysine decarboxylase expression by Vibrio vulnificus is induced by SoxR in response to superoxide stress // Journal of Bacteriology. 2006. Vol. 188. P. 8586–8592. DOI: 10.1128/JB.01084-06.

Kobayashi K., Tagawa S. Isolation of reductase for SoxR that governs an oxidative response regulon from Escherichia coli // FEBS Letters. 1999. Vol. 451. P. 227–230. DOI: 10.1016/s0014-5793(99)00565-7.

Krapp A.R., Humbert M.V., Carrillo N. The soxRS response of Escherichia coli can be induced in the ab-sence of oxidative stress and oxygen by modulation of NADPH content // Microbiology (Reading). 2011. Vol. 157. P. 957–965. DOI: 10.1099/mic.0.039461-0.

Liochev S.I. et al. Induction of the soxRS regulon of Escherichia coli by superoxide // Journal of Biologi-cal Chemistry. 1999. Vol. 274. P. 9479–9481. DOI: 10.1074/jbc.274.14.9479.

Martin R.G., Gillette W.K., Rosner J.L. Promoter discrimination by the related transcriptional activators MarA and SoxS: differential regulation by differential binding // Molecular Microbiology. 2000. Vol. 35. P. 623–634. DOI: 10.1046/j.1365-2958.2000.01732.x.

Michael A.J. Polyamines in Eukaryotes, Bacteria, and Archaea // Journal of Biological Chemistry. 2016. Vol. 291. P. 14896–14903. DOI: 10.1074/jbc.R116.734780.

Miller H.J. Experiments in molecular genetics. Cold Spring Harbor: Cold Spring Harbor Laboratory, 1972. 466 p.

Nunoshiba T. et al. Two-stage control of an oxidative stress regulon: the Escherichia coli SoxR protein triggers redox-inducible expression of the soxS regulatory gene // Journal of Bacteriology. 1992. Vol. 174. P. 6054–6060. DOI: 10.1128/jb.174.19.6054-6060.1992.

Rhee H.J., Kim E.J., Lee J.K. Physiological polyamines: simple primordial stress molecules // Journal of Cellular and Molecular Medicine. 2007. Vol. 11. P. 685–703. DOI: 10.1111/j.1582-4934.2007.00077.x.

Seixas A.F. et al. Bacterial response to oxidative stress and RNA oxidation // Frontiers in Genetics. 2022. Vol. 12. P. 821535. DOI: 10.3389/fgene.2021.821535.

Tkachenko A.G. Mechanisms of protective functions of Escherichia coli polyamines against toxic ef-fect of paraquat, which causes superoxide stress // Biochemistry (Mosc). 2004. Vol. 69. P. 188–194. DOI: 10.1023/b:biry.0000018950.30452.53.

Wu J., Weiss B. Two-stage induction of the soxRS (superoxide response) regulon of Escherichia coli // Journal of Bacteriology. 1992. Vol. 174. P. 3915–3920. DOI: 10.1128/jb.174.12.3915-3920.1992.

Yamamoto Y. et al. The Escherichia coli ldcC gene encodes another lysine decarboxylase, probably a constitutive enzyme // Genes and Genetic Systems. 1997. Vol. 72. P. 167–172. DOI: 10.1266/ggs.72.167.