Mycolicibacterium smegmatis possesses operational agmatinase but contains no detectable polyamines

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...

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Main Authors: Mikhail Zamakhaev, Ivan Tsyganov, Larisa Nesterova, Anna Akhova, Artem Grigorov, Julia Bespyatykh, Tatyana Azhikina, Alexander Tkachenko, Mikhail Shumkov
Format: Article
Language:English
Published: Wolters Kluwer Medknow Publications 2020-01-01
Series:International Journal of Mycobacteriology
Subjects:
Online Access:http://www.ijmyco.org/article.asp?issn=2212-5531;year=2020;volume=9;issue=2;spage=138;epage=143;aulast=Zamakhaev
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author Mikhail Zamakhaev
Ivan Tsyganov
Larisa Nesterova
Anna Akhova
Artem Grigorov
Julia Bespyatykh
Tatyana Azhikina
Alexander Tkachenko
Mikhail Shumkov
author_facet Mikhail Zamakhaev
Ivan Tsyganov
Larisa Nesterova
Anna Akhova
Artem Grigorov
Julia Bespyatykh
Tatyana Azhikina
Alexander Tkachenko
Mikhail Shumkov
author_sort Mikhail Zamakhaev
collection DOAJ
description 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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spelling doaj.art-e815c63d536c46f2b2e5dfacab7759a52022-12-22T02:02:17ZengWolters Kluwer Medknow PublicationsInternational Journal of Mycobacteriology2212-55312212-554X2020-01-019213814310.4103/ijmy.ijmy_48_20Mycolicibacterium smegmatis possesses operational agmatinase but contains no detectable polyaminesMikhail ZamakhaevIvan TsyganovLarisa NesterovaAnna AkhovaArtem GrigorovJulia BespyatykhTatyana AzhikinaAlexander TkachenkoMikhail ShumkovBackground: 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.http://www.ijmyco.org/article.asp?issn=2212-5531;year=2020;volume=9;issue=2;spage=138;epage=143;aulast=Zamakhaevagmatinemycobacteriamycolicibacterium smegmatis polyaminesputrescine
spellingShingle Mikhail Zamakhaev
Ivan Tsyganov
Larisa Nesterova
Anna Akhova
Artem Grigorov
Julia Bespyatykh
Tatyana Azhikina
Alexander Tkachenko
Mikhail Shumkov
Mycolicibacterium smegmatis possesses operational agmatinase but contains no detectable polyamines
International Journal of Mycobacteriology
agmatine
mycobacteria
mycolicibacterium smegmatis
polyamines
putrescine
title Mycolicibacterium smegmatis possesses operational agmatinase but contains no detectable polyamines
title_full Mycolicibacterium smegmatis possesses operational agmatinase but contains no detectable polyamines
title_fullStr Mycolicibacterium smegmatis possesses operational agmatinase but contains no detectable polyamines
title_full_unstemmed Mycolicibacterium smegmatis possesses operational agmatinase but contains no detectable polyamines
title_short Mycolicibacterium smegmatis possesses operational agmatinase but contains no detectable polyamines
title_sort mycolicibacterium smegmatis possesses operational agmatinase but contains no detectable polyamines
topic agmatine
mycobacteria
mycolicibacterium smegmatis
polyamines
putrescine
url http://www.ijmyco.org/article.asp?issn=2212-5531;year=2020;volume=9;issue=2;spage=138;epage=143;aulast=Zamakhaev
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