Results 1 to 10 of about 362,571 (177)

Sequence analysis of tyrosine recombinases allows annotation of mobile genetic elements in prokaryotic genomes [PDF]

open access: yesMolecular Systems Biology, 2021
Mobile genetic elements (MGEs) sequester and mobilize antibiotic resistance genes across bacterial genomes. Efficient and reliable identification of such elements is necessary to follow resistance spreading.
Orsolya Barabás   +2 more
exaly   +6 more sources

Archaeal tyrosine recombinases [PDF]

open access: yesFEMS Microbiology Reviews, 2021
The integration of mobile genetic elements into their host chromosome influences the immediate fate of cellular organisms and gradually shapes their evolution.
Catherine Badel   +2 more
exaly   +5 more sources

Genome engineering in Bacillus anthracis using tyrosine site-specific recombinases [PDF]

open access: yesPLoS ONE, 2017
Tyrosine site-specific recombinases (T-SSR) are polynucleotidyltransferases that catalyze cutting and joining reactions between short specific DNA sequences. We developed three systems for performing genetic modifications in Bacillus anthracis that use T-
Stephen Leppla   +2 more
exaly   +6 more sources

Starships are active eukaryotic transposable elements mobilized by a new family of tyrosine recombinases. [PDF]

open access: yesProc Natl Acad Sci U S A, 2023
Transposable elements in eukaryotic organisms have historically been considered ‘selfish’, at best conferring indirect benefits to their host organisms.
Urquhart AS   +3 more
europepmc   +6 more sources

Interaction of the putative tyrosine recombinases RipX (UU145), XerC (UU222), and CodV (UU529) ofUreaplasma parvumserovar 3 with specific DNA [PDF]

open access: yesFEMS Microbiology Letters, 2013
Phase variation of two loci (‘mba locus’ and ‘UU172 phase-variable element’) in Ureaplasma parvum serovar 3 has been suggested as result of site-specific DNA inversion occurring at short inverted repeats. Three potential tyrosine recombinases (RipX, XerC,
Joachim Spergser   +2 more
exaly   +3 more sources

Structure of Yeast Kinetochore Ndc10 DNA-binding Domain Reveals Unexpected Evolutionary Relationship to Tyrosine Recombinases [PDF]

open access: yesJournal of Biological Chemistry, 2012
Background: Ndc10 is a DNA-binding protein in yeast that is responsible for centromere formation. Results: The structure of the protein unexpectedly shows that it contains a type IB topoisomerase/λ-integrase fold.
Martin Singleton
exaly   +3 more sources

In vitro DNA Inversions Mediated by the PsrA Site-Specific Tyrosine Recombinase of Streptococcus pneumoniae [PDF]

open access: yesFrontiers in Molecular Biosciences, 2020
Site-specific recombination is a DNA breaking and reconstructing process that plays important roles in various cellular pathways for both prokaryotes and eukaryotes. This process requires a site-specific recombinase and direct or inverted repeats.
Jingwen Li   +5 more
doaj   +5 more sources

The integrase family of tyrosine recombinases: evolution of a conserved active site domain [PDF]

open access: yesNucleic Acids Research, 1997
The integrases are a diverse family of tyrosine recombinases which rearrange DNA duplexes by means of conservative site-specific recombination reactions.
Dominic Esposito, J J Scocca
exaly   +4 more sources

Towards a more accurate annotation of tyrosine-based site-specific recombinases in bacterial genomes [PDF]

open access: yesMobile DNA, 2012
Background Tyrosine-based site-specific recombinases (TBSSRs) are DNA breaking-rejoining enzymes. In bacterial genomes, they play a major role in the comings and goings of mobile genetic elements (MGEs), such as temperate phage genomes, integrated ...
Van Houdt Rob   +4 more
doaj   +5 more sources

Discovery and characterization of novel Cre-type tyrosine site-specific recombinases for advanced genome engineering

open access: yesNucleic Acids Research, 2023
Tyrosine-type site-specific recombinases (Y-SSRs) are versatile tools for genome engineering due to their ability to mediate excision, integration, inversion and exchange of genomic DNA with single nucleotide precision.
Frank Buchholz   +2 more
exaly   +5 more sources

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