A single active site in the mariner transposase cleaves DNA strands of opposite polarity
(2017)
Journal Article
Claeys Bouuaert, C., & Chalmers, R. (in press). A single active site in the mariner transposase cleaves DNA strands of opposite polarity. Nucleic Acids Research, gkx826, https://doi.org/10.1093/nar/gkx826
The RNase H structural fold defines a large family of nucleic acid metabolizing enzymes that catalyze phosphoryl transfer reactions using two divalent metal ions in the active site. Almost all of these reactions involve only one strand of the nucleic... Read More about A single active site in the mariner transposase cleaves DNA strands of opposite polarity.