Cre Recombinase and Other Tyrosine Recombinases
Chemical Reviews, 2016Tyrosine-type site-specific recombinases (T-SSRs) have opened new avenues for the predictable modification of genomes as they enable precise genome editing in heterologous hosts. These enzymes are ubiquitous in eubacteria, prevalent in archaea and temperate phages, present in certain yeast strains, but barely found in higher eukaryotes.
Joachim Hauber +2 more
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Identification of a Potential General Acid/Base in the Reversible Phosphoryl Transfer Reactions Catalyzed by Tyrosine Recombinases: Flp H305 [PDF]
SummaryFlp provides a unique opportunity to apply the tools of chemical biology to phosphoryl transfer reactions. Flp and other tyrosine recombinases catalyze site-specific DNA rearrangements via a phosphotyrosine intermediate.
Phoebe A Rice, Katrine Whiteson
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Strand Selection by the Tyrosine Recombinases
Progress in Molecular Biology and Translational Science, 2005Publisher Summary This chapter focuses on four tyrosine recombinases for which there is a wealth of biochemical and structural data. This chapter reviews the biochemical and structural findings for each of these enzymes. This chapter also examines the factors that influence strand selection and consider the possible function of strand selection in ...
Paul D Sadowski
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Dual Recombinase-Mediated Cassette Exchange by Tyrosine Site-Specific Recombinases
Methods in Molecular Biology, 2017Recombinase-mediated cassette exchange, or RMCE, is a genome engineering tool that can be used to swap DNA fragments of interest between two DNA molecules. In a variation of RMCE, called dual RMCE, the exchange of DNA fragments is mediated by two recombinases in contrast to one recombinase in the classic RMCE reaction.
Rachelle P Anderson
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The integrase family of tyrosine recombinases: evolution of a conserved active site domain. [PDF]
The integrases are a diverse family of tyrosine recombinases which rearrange DNA duplexes by means of conservative site-specific recombination reactions. Members of this family, of which the well-studied lambda Int protein is the prototype, were previously found to share four strongly conserved residues, including an active site tyrosine directly ...
Dominic Esposito, J J Scocca
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DIRS-1 and the other tyrosine recombinase retrotransposons
Cytogenetic and Genome Research, 2005DIRS-1 is a retroelement from the slime mold <i>Dictyostelium discoideum</i>. Until recently only two related retrotransposons had been described: PAT from the nematode <i>Panagrellus redivivus</i> and <i>Prt1</i> from the zygomycete fungus <i>Phycomyces blakesleeanus</i>.
R T M, Poulter, T J D, Goodwin
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Peptide inhibitors of DNA cleavage by tyrosine recombinases and topoisomerases
Journal of Molecular Biology, 2000The study of biochemical pathways requires the isolation and characterization of each and every intermediate in the pathway. For the site-specific recombination reactions catalyzed by the bacteriophage lambda tyrosine recombinase integrase (Int), this has been difficult because of the high level of efficiency of the reaction, the highly reversible ...
M, Klemm +4 more
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Unveiling Hidden Catalytic Contributions of the Conserved His/Trp-III in Tyrosine Recombinases: Assembly of a Novel Active Site in Flp Recombinase Harboring Alanine at this Position [PDF]
The catalytic pentad of tyrosine recombinases, that assists the tyrosine nucleophile, includes a conserved histidine/tryptophan (His/Trp-III). Flp and Cre harbor tryptophan at this position; most of their kin recombinases display histidine. Contrary to the conservation rule, Flp(W330F) is a much stronger recombinase than Flp(W330H).
Makkuni Jayaram, Yuri Voziyanov
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Transgenic expression of Cre recombinase from the tyrosine hydroxylase locus
genesis, 2004AbstractCatecholaminergic neurons are affected in several neurological and psychiatric diseases. Tyrosine hydroxylase (TH) is the first, rate‐limiting enzyme in catecholamine synthesis. We report a knockin mouse expressing Cre‐recombinase from the 3′‐untranslated region of the endogenous Th gene by means of an internal ribosomal entry sequence (IRES ...
Jonas, Lindeberg +6 more
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VIPER was initially characterized as a 2326bp LTR-like retroelement associated to SIRE, a short interspersed repetitive element specific of Trypanosoma cruzi. It carried a single ORF that coded for a putative reverse transcriptase-RNAse H protein, suggesting that it could be a truncated copy of a longer retroelement. Herein we report the identification
Hernan A, Lorenzi +2 more
openaire +2 more sources

