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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...

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Detalles Bibliográficos
Autores principales: Badel, Catherine, Da Cunha, Violette, Oberto, Jacques
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2021
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.
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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
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