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Badel C, Da Cunha V, Oberto J. Archaeal tyrosine recombinases. FEMS Microbiol Rev. 2021;45(4)doi: 10.1093/femsre/fuab004.
Badel, C., Da Cunha, V., & Oberto, J. (2021). Archaeal tyrosine recombinases. FEMS microbiology reviews, 45(4), . https://doi.org/10.1093/femsre/fuab004
Badel, Catherine, et al. "Archaeal tyrosine recombinases." FEMS microbiology reviews vol. 45,4 (2021). doi: https://doi.org/10.1093/femsre/fuab004
Badel C, Da Cunha V, Oberto J. Archaeal tyrosine recombinases. FEMS Microbiol Rev. 2021 Aug 17;45(4). doi: 10.1093/femsre/fuab004. PMID: 33524101; PMCID: PMC8371274.
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FEMS Microbiol Rev. 2021 Aug 17;45(4). doi: 10.1093/femsre/fuab004.

Archaeal tyrosine recombinases.

FEMS microbiology reviews

Catherine Badel, Violette Da Cunha, Jacques Oberto

Affiliations

  1. Université Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), 91198 Gif-sur-Yvette, France.

PMID: 33524101 PMCID: PMC8371274 DOI: 10.1093/femsre/fuab004

Abstract

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.

© The Author(s) 2021. Published by Oxford University Press on behalf of FEMS.

Keywords: Archaea; genome evolution; horizontal transfer; mobile genetic element; site-specific recombination; tyrosine recombinase

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