Journal
CHEMICAL REVIEWS
Volume 116, Issue 20, Pages 12785-12820Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.chemrev.6b00077
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Funding
- EU FP7 Grant SyBoSS [242129]
- DFG [SFB655, BU1400/3-1, BU1400/5-1, TPB05]
- TUD Excellence initiative by the German Federal and State Governments (Institutional Strategy, measure support the best) FunPerMed
- Bayer hemophilia awards program
- BMBF [GO-Bio FKZ 0315090]
- Else Kroner-Fresenius-Stiftung [2010_A82]
- Viral Latency program at the Heinrich Pette Institute-Leibniz Institute for Experimental Virology, Hamburg
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Tyrosine-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. As tools they find increasing use for the generation and systematic modification of genomes in a plethora of organisms. If applied in host organisms, they enable precise DNA cleavage and ligation without the gain or loss of nucleotides. Criteria directing the choice of the most appropriate T-SSR system for genetic engineering include that, whenever possible, the recombinase should act independent of cofactors and that the target sequences should be long enough to be unique in a given genome. This review is focused on recent advancements in our mechanistic understanding of simple T-SSRs and their application in developmental and synthetic biology, as well as in biomedical research.
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