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Related Concept Videos

Conservative Site-specific Recombination and Phase Variation02:53

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Because the DNA segments are cut and reorganized in a direction-specific manner, site-specific recombination has emerged as an efficient genetic engineering technique. Flippase and Cyclization recombinases or Flp and Cre, respectively, are two members of the tyrosine recombinase family derived from bacteriophages, that are used to mediate site-specific DNA insertions, deletions, and targeted expression of proteins in mammalian cell lines.
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Translesion (TLS) polymerases rescue stalled DNA polymerases at sites of damaged bases by replacing the replicative polymerase and installing a nucleotide across the damaged site. Doing so, TLS allows additional time for the cell to repair the damage before resuming regular DNA replication.
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The basic reaction of homologous recombination (HR) involves two chromatids that contain DNA sequences sharing a significant stretch of identity. One of these sequences uses a strand from another as a template to synthesize DNA in an enzyme-catalyzed reaction. The final product is a novel amalgamation of the two substrates. To ensure an accurate recombination of sequences, HR is restricted to the S and G2 phases of the cell cycle. At these stages, the DNA has been replicated already and the...
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The evolution of new genes is critical for speciation. Exon recombination, also known as exon shuffling or domain shuffling, is an important means of new gene formation. It is observed across vertebrates, invertebrates, and in some plants such as potatoes and sunflowers. During exon recombination, exons from the same or different genes recombine and produce new exon-intron combinations, which might evolve into new genes. 
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Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...
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Related Experiment Video

Updated: Nov 19, 2025

Preparation of the Mgm101 Recombination Protein by MBP-based Tagging Strategy
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Archaeal tyrosine recombinases.

Catherine Badel1, Violette Da Cunha1, Jacques Oberto1

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

FEMS Microbiology Reviews
|February 1, 2021
PubMed
Summary

Archaeal tyrosine recombinases are unique enzymes that can cause large genome rearrangements and even disrupt their own genes. Their diverse biochemical and evolutionary properties are distinct from bacterial and eukaryotic counterparts.

Keywords:
Archaeagenome evolutionhorizontal transfermobile genetic elementsite-specific recombinationtyrosine recombinase

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Area of Science:

  • Microbiology
  • Genetics
  • Evolutionary Biology

Background:

  • Mobile genetic elements integrate into host chromosomes, influencing organismal fate and evolution.
  • Site-specific recombinases are key to this integration, with extensive characterization in bacteria and eukarya.
  • Recent studies reveal unique features of archaeal tyrosine recombinases.

Purpose of the Study:

  • To assess the diversity of archaeal tyrosine recombinases.
  • To outline their biochemical, ecological, and evolutionary properties.
  • To compare archaeal recombinases with their bacterial and eukaryotic counterparts.

Main Methods:

  • Phylogenomic analysis using an exhaustive similarity network.
  • Review of existing literature on archaeal tyrosine recombinases.

Main Results:

  • Archaeal integrases exhibit unique features, including activity in extreme environments and catalysis of reactions beyond site-specific recombination.
  • Some archaeal integrases can mediate low-sequence specificity recombination, leading to significant genome rearrangements.
  • A notable proportion of archaeal integrases are 'suicidal,' possessing recombination targets within their own genes.

Conclusions:

  • Archaeal tyrosine recombinases display remarkable diversity and unique functional capabilities.
  • The 'suicidal' nature of some integrases suggests novel evolutionary mechanisms.
  • Understanding these enzymes provides insights into genome evolution across different domains of life.