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...
Main Authors: | , , , , , , , , |
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Format: | Article |
Language: | English |
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Wolters Kluwer Medknow Publications
2020-01-01
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Series: | International Journal of Mycobacteriology |
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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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format | Article |
id | doaj.art-e815c63d536c46f2b2e5dfacab7759a5 |
institution | Directory Open Access Journal |
issn | 2212-5531 2212-554X |
language | English |
last_indexed | 2024-12-10T04:25:34Z |
publishDate | 2020-01-01 |
publisher | Wolters Kluwer Medknow Publications |
record_format | Article |
series | International Journal of Mycobacteriology |
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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