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Functionality and cross-regulation of the four SprG/SprF type I toxin–antitoxin systems in Staphylococcus aureus
Toxin–antitoxin (TA) systems are ubiquitous among bacteria, frequently expressed in multiple copies, and important for functions such as antibiotic resistance and persistence. Type I TA systems are composed of a stable toxic peptide whose expression is repressed by an unstable RNA antitoxin. Here, w...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Oxford University Press
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6393307/ https://www.ncbi.nlm.nih.gov/pubmed/30551143 http://dx.doi.org/10.1093/nar/gky1256 |
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author | Riffaud, Camille Pinel-Marie, Marie-Laure Pascreau, Gaëtan Felden, Brice |
author_facet | Riffaud, Camille Pinel-Marie, Marie-Laure Pascreau, Gaëtan Felden, Brice |
author_sort | Riffaud, Camille |
collection | PubMed |
description | Toxin–antitoxin (TA) systems are ubiquitous among bacteria, frequently expressed in multiple copies, and important for functions such as antibiotic resistance and persistence. Type I TA systems are composed of a stable toxic peptide whose expression is repressed by an unstable RNA antitoxin. Here, we investigated the functionalities, regulation, and possible cross-talk between three core genome copies of the pathogenicity island-encoded ‘sprG1/sprF1’ type I TA system in the human pathogen Staphylococcus aureus. Except for SprG4, all RNA from these pairs, sprG2/sprF2, sprG3/sprF3, sprG4/sprF4, are expressed in the HG003 strain. SprG2 and SprG3 RNAs encode toxic peptides whose overexpression triggers bacteriostasis, which is counteracted at the RNA level by the overexpression of SprF2 and SprF3 antitoxins. Complex formation between each toxin and its cognate antitoxin involves their overlapping 3′ ends, and each SprF antitoxin specifically neutralizes the toxicity of its cognate SprG toxin without cross-talk. However, overexpression studies suggest cross-regulations occur at the RNA level between the SprG/SprF TA systems during growth. When subjected to H(2)O(2)-induced oxidative stress, almost all antitoxin levels dropped, while only SprG1 and SprF1 were reduced during phagocytosis-induced oxidative stress. SprG1, SprF1, SprF2, SprG3 and SprF3 levels also decrease during hyperosmotic stress. This suggests that novel SprG/SprF TA systems are involved in S. aureus persistence. |
format | Online Article Text |
id | pubmed-6393307 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-63933072019-03-05 Functionality and cross-regulation of the four SprG/SprF type I toxin–antitoxin systems in Staphylococcus aureus Riffaud, Camille Pinel-Marie, Marie-Laure Pascreau, Gaëtan Felden, Brice Nucleic Acids Res Gene regulation, Chromatin and Epigenetics Toxin–antitoxin (TA) systems are ubiquitous among bacteria, frequently expressed in multiple copies, and important for functions such as antibiotic resistance and persistence. Type I TA systems are composed of a stable toxic peptide whose expression is repressed by an unstable RNA antitoxin. Here, we investigated the functionalities, regulation, and possible cross-talk between three core genome copies of the pathogenicity island-encoded ‘sprG1/sprF1’ type I TA system in the human pathogen Staphylococcus aureus. Except for SprG4, all RNA from these pairs, sprG2/sprF2, sprG3/sprF3, sprG4/sprF4, are expressed in the HG003 strain. SprG2 and SprG3 RNAs encode toxic peptides whose overexpression triggers bacteriostasis, which is counteracted at the RNA level by the overexpression of SprF2 and SprF3 antitoxins. Complex formation between each toxin and its cognate antitoxin involves their overlapping 3′ ends, and each SprF antitoxin specifically neutralizes the toxicity of its cognate SprG toxin without cross-talk. However, overexpression studies suggest cross-regulations occur at the RNA level between the SprG/SprF TA systems during growth. When subjected to H(2)O(2)-induced oxidative stress, almost all antitoxin levels dropped, while only SprG1 and SprF1 were reduced during phagocytosis-induced oxidative stress. SprG1, SprF1, SprF2, SprG3 and SprF3 levels also decrease during hyperosmotic stress. This suggests that novel SprG/SprF TA systems are involved in S. aureus persistence. Oxford University Press 2019-02-28 2018-12-15 /pmc/articles/PMC6393307/ /pubmed/30551143 http://dx.doi.org/10.1093/nar/gky1256 Text en © The Author(s) 2018. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Gene regulation, Chromatin and Epigenetics Riffaud, Camille Pinel-Marie, Marie-Laure Pascreau, Gaëtan Felden, Brice Functionality and cross-regulation of the four SprG/SprF type I toxin–antitoxin systems in Staphylococcus aureus |
title | Functionality and cross-regulation of the four SprG/SprF type I toxin–antitoxin systems in Staphylococcus aureus |
title_full | Functionality and cross-regulation of the four SprG/SprF type I toxin–antitoxin systems in Staphylococcus aureus |
title_fullStr | Functionality and cross-regulation of the four SprG/SprF type I toxin–antitoxin systems in Staphylococcus aureus |
title_full_unstemmed | Functionality and cross-regulation of the four SprG/SprF type I toxin–antitoxin systems in Staphylococcus aureus |
title_short | Functionality and cross-regulation of the four SprG/SprF type I toxin–antitoxin systems in Staphylococcus aureus |
title_sort | functionality and cross-regulation of the four sprg/sprf type i toxin–antitoxin systems in staphylococcus aureus |
topic | Gene regulation, Chromatin and Epigenetics |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6393307/ https://www.ncbi.nlm.nih.gov/pubmed/30551143 http://dx.doi.org/10.1093/nar/gky1256 |
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