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- W2019606105 abstract "To study the mechanism of precise excision ofgypsy from genomic sites, the integrase domain ofgypsy pol was cloned and expressed inEscherichia coli. The endonuclease activity of recombinant integrase was assayed with synthetic substrates corresponding to 3′-U5 ofgypsy LTR and to the known genomic insertion sites ofgypsy. Integrase nicked the 5′-A ⇓ YR-3′ triplet in the (+) strand of the double-stranded substrates; cleavage of a single-stranded substrate was nonspecific. Cleavage proved to be affected by the local conformation of the substrate: the (+) strand was cleaved more efficiently when the (−) strand had an unpaired base in the triplet and was not cleaved when the (−) strand was interrupted or branched. The triplet corresponded to the consensus region ofgypsy insertion (5′-YRYR ⇓ YR-3′), the site of cleavagein vitro coinciding with the site of insertionin vivo. The unique mechanism ofgypsy excision was assumed to depend to a great extent on the enzymic properties of its integrase." @default.
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- W2019606105 date "2000-03-01" @default.
- W2019606105 modified "2023-10-14" @default.
- W2019606105 title "Specific endonuclease activity of integrase encoded by the mdg4 (gypsy) retrotransposon" @default.
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- W2019606105 doi "https://doi.org/10.1007/bf02759646" @default.
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