Mycolicibacterium smegmatis possesses operational agmatinase but contains no detectable polyamines

Int J Mycobacteriol. 2020 Apr-Jun;9(2):138-143. doi: 10.4103/ijmy.ijmy_48_20.

Abstract

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.

Keywords: Agmatine; Mycolicibacterium smegmatis; mycobacteria; polyamines; putrescine.

MeSH terms

  • Agmatine / metabolism
  • Gene Expression Profiling
  • Mycobacterium smegmatis / chemistry*
  • Mycobacterium smegmatis / enzymology*
  • Mycobacterium smegmatis / genetics
  • Polyamines / analysis*
  • Proteomics
  • Putrescine / metabolism
  • Ureohydrolases / genetics
  • Ureohydrolases / metabolism*

Substances

  • Polyamines
  • Agmatine
  • Ureohydrolases
  • agmatinase
  • Putrescine