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Conservation and diversity of radiation and oxidative stress resistance mechanisms in Deinococcus species
Deinococcus bacteria are famous for their extreme resistance to ionising radiation and other DNA damage- and oxidative stress-generating agents. More than a hundred genes have been reported to contribute to resistance to radiation, desiccation and/or oxidative stress in Deinococcus radiodurans. Thes...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6300522/ https://www.ncbi.nlm.nih.gov/pubmed/30339218 http://dx.doi.org/10.1093/femsre/fuy037 |
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author | Lim, Sangyong Jung, Jong-Hyun Blanchard, Laurence de Groot, Arjan |
author_facet | Lim, Sangyong Jung, Jong-Hyun Blanchard, Laurence de Groot, Arjan |
author_sort | Lim, Sangyong |
collection | PubMed |
description | Deinococcus bacteria are famous for their extreme resistance to ionising radiation and other DNA damage- and oxidative stress-generating agents. More than a hundred genes have been reported to contribute to resistance to radiation, desiccation and/or oxidative stress in Deinococcus radiodurans. These encode proteins involved in DNA repair, oxidative stress defence, regulation and proteins of yet unknown function or with an extracytoplasmic location. Here, we analysed the conservation of radiation resistance-associated proteins in other radiation-resistant Deinococcus species. Strikingly, homologues of dozens of these proteins are absent in one or more Deinococcus species. For example, only a few Deinococcus-specific proteins and radiation resistance-associated regulatory proteins are present in each Deinococcus, notably the metallopeptidase/repressor pair IrrE/DdrO that controls the radiation/desiccation response regulon. Inversely, some Deinococcus species possess proteins that D. radiodurans lacks, including DNA repair proteins consisting of novel domain combinations, translesion polymerases, additional metalloregulators, redox-sensitive regulator SoxR and manganese-containing catalase. Moreover, the comparisons improved the characterisation of several proteins regarding important conserved residues, cellular location and possible protein–protein interactions. This comprehensive analysis indicates not only conservation but also large diversity in the molecular mechanisms involved in radiation resistance even within the Deinococcus genus. |
format | Online Article Text |
id | pubmed-6300522 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-63005222018-12-27 Conservation and diversity of radiation and oxidative stress resistance mechanisms in Deinococcus species Lim, Sangyong Jung, Jong-Hyun Blanchard, Laurence de Groot, Arjan FEMS Microbiol Rev Review Article Deinococcus bacteria are famous for their extreme resistance to ionising radiation and other DNA damage- and oxidative stress-generating agents. More than a hundred genes have been reported to contribute to resistance to radiation, desiccation and/or oxidative stress in Deinococcus radiodurans. These encode proteins involved in DNA repair, oxidative stress defence, regulation and proteins of yet unknown function or with an extracytoplasmic location. Here, we analysed the conservation of radiation resistance-associated proteins in other radiation-resistant Deinococcus species. Strikingly, homologues of dozens of these proteins are absent in one or more Deinococcus species. For example, only a few Deinococcus-specific proteins and radiation resistance-associated regulatory proteins are present in each Deinococcus, notably the metallopeptidase/repressor pair IrrE/DdrO that controls the radiation/desiccation response regulon. Inversely, some Deinococcus species possess proteins that D. radiodurans lacks, including DNA repair proteins consisting of novel domain combinations, translesion polymerases, additional metalloregulators, redox-sensitive regulator SoxR and manganese-containing catalase. Moreover, the comparisons improved the characterisation of several proteins regarding important conserved residues, cellular location and possible protein–protein interactions. This comprehensive analysis indicates not only conservation but also large diversity in the molecular mechanisms involved in radiation resistance even within the Deinococcus genus. Oxford University Press 2018-10-18 /pmc/articles/PMC6300522/ /pubmed/30339218 http://dx.doi.org/10.1093/femsre/fuy037 Text en © FEMS 2018. 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 | Review Article Lim, Sangyong Jung, Jong-Hyun Blanchard, Laurence de Groot, Arjan Conservation and diversity of radiation and oxidative stress resistance mechanisms in Deinococcus species |
title | Conservation and diversity of radiation and oxidative stress resistance mechanisms in Deinococcus species |
title_full | Conservation and diversity of radiation and oxidative stress resistance mechanisms in Deinococcus species |
title_fullStr | Conservation and diversity of radiation and oxidative stress resistance mechanisms in Deinococcus species |
title_full_unstemmed | Conservation and diversity of radiation and oxidative stress resistance mechanisms in Deinococcus species |
title_short | Conservation and diversity of radiation and oxidative stress resistance mechanisms in Deinococcus species |
title_sort | conservation and diversity of radiation and oxidative stress resistance mechanisms in deinococcus species |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6300522/ https://www.ncbi.nlm.nih.gov/pubmed/30339218 http://dx.doi.org/10.1093/femsre/fuy037 |
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