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ORIGINAL ARTICLE
Year : 2020  |  Volume : 9  |  Issue : 2  |  Page : 138-143

Mycolicibacterium smegmatis possesses operational agmatinase but contains no detectable polyamines


1 Research Center of Biotechnology of the Russian Academy of Sciences, Bach Institute of Biochemistry, Moscow, Russia
2 Perm State University, Biology Faculty; Perm Federal Research Center of the Ural Branch of the Russian Academy of Sciences, Institute of Ecology and Genetics of Microorganisms, Perm, Russia
3 Perm Federal Research Center of the Ural Branch of the Russian Academy of Sciences, Institute of Ecology and Genetics of Microorganisms, Perm, Russia
4 Shemyakin and Ovchinnikov, Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Department of Genomics and Postgenomic Technologies, Moscow, Russia
5 Federal Research and Clinical Centre of Physical-Chemical Medicine of Federal Medical Biological Agency, Moscow, Russia

Correspondence Address:
Mikhail Shumkov
Leninsky prospect 33, build 3, Moscow 119071
Russia
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Source of Support: None, Conflict of Interest: None


DOI: 10.4103/ijmy.ijmy_48_20

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Background: Polyamines are widespread intracellular molecules able to influence antibiotic susceptibility, but almost nothing is known on their occurrence and physiological role in mycobacteria. Methods: here, we analyzed transcriptomic, proteomic and biochemical data and obtained the first evidence for the post-transcriptional expression of some genes attributed to polyamine metabolism and polyamine transport in Mycolicibacterium smegmatis (basionym Mycobacterium smegmatis). Results: in our experiments, exponentially growing cells demonstrated transcription of 21 polyamine-associated genes and possessed 7 enzymes of polyamine metabolism and 2 polyamine transport proteins. Conclusion: Mycolicibacterium smegmatis putrescine synthesizing enzyme agmatinase SpeB was originally shown to catalyze agmatine conversion to putrescine in vitro. Nevertheless, we have not found any polyamines in mycobacterial cells.


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