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Archaeal tyrosine recombinases
The integration of mobile genetic elements into their host chromosome influences the immediate fate of cellular organisms and gradually shapes their evolution. Site-specific recombinases catalyzing this integration have been extensively characterized both in bacteria and eukarya. More recently, a nu...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8371274/ https://www.ncbi.nlm.nih.gov/pubmed/33524101 http://dx.doi.org/10.1093/femsre/fuab004 |
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author | Badel, Catherine Da Cunha, Violette Oberto, Jacques |
author_facet | Badel, Catherine Da Cunha, Violette Oberto, Jacques |
author_sort | Badel, Catherine |
collection | PubMed |
description | The integration of mobile genetic elements into their host chromosome influences the immediate fate of cellular organisms and gradually shapes their evolution. Site-specific recombinases catalyzing this integration have been extensively characterized both in bacteria and eukarya. More recently, a number of reports provided the in-depth characterization of archaeal tyrosine recombinases and highlighted new particular features not observed in the other two domains. In addition to being active in extreme environments, archaeal integrases catalyze reactions beyond site-specific recombination. Some of these integrases can catalyze low-sequence specificity recombination reactions with the same outcome as homologous recombination events generating deep rearrangements of their host genome. A large proportion of archaeal integrases are termed suicidal due to the presence of a specific recombination target within their own gene. The paradoxical maintenance of integrases that disrupt their gene upon integration implies novel mechanisms for their evolution. In this review, we assess the diversity of the archaeal tyrosine recombinases using a phylogenomic analysis based on an exhaustive similarity network. We outline the biochemical, ecological and evolutionary properties of these enzymes in the context of the families we identified and emphasize similarities and differences between archaeal recombinases and their bacterial and eukaryal counterparts. |
format | Online Article Text |
id | pubmed-8371274 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-83712742021-08-18 Archaeal tyrosine recombinases Badel, Catherine Da Cunha, Violette Oberto, Jacques FEMS Microbiol Rev Review Article The integration of mobile genetic elements into their host chromosome influences the immediate fate of cellular organisms and gradually shapes their evolution. Site-specific recombinases catalyzing this integration have been extensively characterized both in bacteria and eukarya. More recently, a number of reports provided the in-depth characterization of archaeal tyrosine recombinases and highlighted new particular features not observed in the other two domains. In addition to being active in extreme environments, archaeal integrases catalyze reactions beyond site-specific recombination. Some of these integrases can catalyze low-sequence specificity recombination reactions with the same outcome as homologous recombination events generating deep rearrangements of their host genome. A large proportion of archaeal integrases are termed suicidal due to the presence of a specific recombination target within their own gene. The paradoxical maintenance of integrases that disrupt their gene upon integration implies novel mechanisms for their evolution. In this review, we assess the diversity of the archaeal tyrosine recombinases using a phylogenomic analysis based on an exhaustive similarity network. We outline the biochemical, ecological and evolutionary properties of these enzymes in the context of the families we identified and emphasize similarities and differences between archaeal recombinases and their bacterial and eukaryal counterparts. Oxford University Press 2021-02-01 /pmc/articles/PMC8371274/ /pubmed/33524101 http://dx.doi.org/10.1093/femsre/fuab004 Text en © The Author(s) 2021. Published by Oxford University Press on behalf of FEMS. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) ), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Article Badel, Catherine Da Cunha, Violette Oberto, Jacques Archaeal tyrosine recombinases |
title | Archaeal tyrosine recombinases |
title_full | Archaeal tyrosine recombinases |
title_fullStr | Archaeal tyrosine recombinases |
title_full_unstemmed | Archaeal tyrosine recombinases |
title_short | Archaeal tyrosine recombinases |
title_sort | archaeal tyrosine recombinases |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8371274/ https://www.ncbi.nlm.nih.gov/pubmed/33524101 http://dx.doi.org/10.1093/femsre/fuab004 |
work_keys_str_mv | AT badelcatherine archaealtyrosinerecombinases AT dacunhaviolette archaealtyrosinerecombinases AT obertojacques archaealtyrosinerecombinases |