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Identification and characterization of VapBC toxin–antitoxin system in Bosea sp. PAMC 26642 isolated from Arctic lichens

Toxin–antitoxin (TA) systems are genetic modules composed of a toxin interfering with cellular processes and its cognate antitoxin, which counteracts the activity of the toxin. TA modules are widespread in bacterial and archaeal genomes. It has been suggested that TA modules participate in the adapt...

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Autores principales: Jeon, Hyerin, Choi, Eunsil, Hwang, Jihwan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory Press 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8522696/
https://www.ncbi.nlm.nih.gov/pubmed/34429367
http://dx.doi.org/10.1261/rna.078786.121
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author Jeon, Hyerin
Choi, Eunsil
Hwang, Jihwan
author_facet Jeon, Hyerin
Choi, Eunsil
Hwang, Jihwan
author_sort Jeon, Hyerin
collection PubMed
description Toxin–antitoxin (TA) systems are genetic modules composed of a toxin interfering with cellular processes and its cognate antitoxin, which counteracts the activity of the toxin. TA modules are widespread in bacterial and archaeal genomes. It has been suggested that TA modules participate in the adaptation of prokaryotes to unfavorable conditions. The Bosea sp. PAMC 26642 used in this study was isolated from the Arctic lichen Stereocaulon sp. There are 12 putative type II TA loci in the genome of Bosea sp. PAMC 26642. Of these, nine functional TA systems have been shown to be toxic in Escherichia coli. The toxin inhibits growth, but this inhibition is reversed when the cognate antitoxin genes are coexpressed, indicating that these putative TA loci were bona fide TA modules. Only the BoVapC1 (AXW83_01405) toxin, a homolog of VapC, showed growth inhibition specific to low temperatures, which was recovered by the coexpression of BoVapB1 (AXW83_01400). Microscopic observation and growth monitoring revealed that the BoVapC1 toxin had bacteriostatic effects on the growth of E. coli and induced morphological changes. Quantitative real time polymerase chain reaction and northern blotting analyses showed that the BoVapC1 toxin had a ribonuclease activity on the initiator tRNA(fMet), implying that degradation of tRNA(fMet) might trigger growth arrest in E. coli. Furthermore, the BoVapBC1 system was found to contribute to survival against prolonged exposure at 4°C. This is the first study to identify the function of TA systems in cold adaptation.
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spelling pubmed-85226962021-11-01 Identification and characterization of VapBC toxin–antitoxin system in Bosea sp. PAMC 26642 isolated from Arctic lichens Jeon, Hyerin Choi, Eunsil Hwang, Jihwan RNA Article Toxin–antitoxin (TA) systems are genetic modules composed of a toxin interfering with cellular processes and its cognate antitoxin, which counteracts the activity of the toxin. TA modules are widespread in bacterial and archaeal genomes. It has been suggested that TA modules participate in the adaptation of prokaryotes to unfavorable conditions. The Bosea sp. PAMC 26642 used in this study was isolated from the Arctic lichen Stereocaulon sp. There are 12 putative type II TA loci in the genome of Bosea sp. PAMC 26642. Of these, nine functional TA systems have been shown to be toxic in Escherichia coli. The toxin inhibits growth, but this inhibition is reversed when the cognate antitoxin genes are coexpressed, indicating that these putative TA loci were bona fide TA modules. Only the BoVapC1 (AXW83_01405) toxin, a homolog of VapC, showed growth inhibition specific to low temperatures, which was recovered by the coexpression of BoVapB1 (AXW83_01400). Microscopic observation and growth monitoring revealed that the BoVapC1 toxin had bacteriostatic effects on the growth of E. coli and induced morphological changes. Quantitative real time polymerase chain reaction and northern blotting analyses showed that the BoVapC1 toxin had a ribonuclease activity on the initiator tRNA(fMet), implying that degradation of tRNA(fMet) might trigger growth arrest in E. coli. Furthermore, the BoVapBC1 system was found to contribute to survival against prolonged exposure at 4°C. This is the first study to identify the function of TA systems in cold adaptation. Cold Spring Harbor Laboratory Press 2021-11 /pmc/articles/PMC8522696/ /pubmed/34429367 http://dx.doi.org/10.1261/rna.078786.121 Text en © 2021 Jeon et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society https://creativecommons.org/licenses/by/4.0/This article, published in RNA, is available under a Creative Commons License (Attribution 4.0 International), as described at http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Jeon, Hyerin
Choi, Eunsil
Hwang, Jihwan
Identification and characterization of VapBC toxin–antitoxin system in Bosea sp. PAMC 26642 isolated from Arctic lichens
title Identification and characterization of VapBC toxin–antitoxin system in Bosea sp. PAMC 26642 isolated from Arctic lichens
title_full Identification and characterization of VapBC toxin–antitoxin system in Bosea sp. PAMC 26642 isolated from Arctic lichens
title_fullStr Identification and characterization of VapBC toxin–antitoxin system in Bosea sp. PAMC 26642 isolated from Arctic lichens
title_full_unstemmed Identification and characterization of VapBC toxin–antitoxin system in Bosea sp. PAMC 26642 isolated from Arctic lichens
title_short Identification and characterization of VapBC toxin–antitoxin system in Bosea sp. PAMC 26642 isolated from Arctic lichens
title_sort identification and characterization of vapbc toxin–antitoxin system in bosea sp. pamc 26642 isolated from arctic lichens
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8522696/
https://www.ncbi.nlm.nih.gov/pubmed/34429367
http://dx.doi.org/10.1261/rna.078786.121
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