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- W1910389675 endingPage "3796" @default.
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- W1910389675 abstract "Holliday structures are formed and resolved by FLP protein during site-specific recombination. These structures have been isolated and are visualized in both native and partially denatured states by electron microscopy. No single-strand breaks are found within the junction, indicating that the structure results from a reciprocal exchange of strands. These structures have properties consistent with being reaction intermediates. Double-strand cleavage products and Y structures are also detected and appear to be by-products of the reaction. The Y structures are three-armed branched molecules with a covalently closed junction located at the FLP recombination target site. Models are discussed, suggesting that both of these novel structures are made by aberrant cleavages during formation and resolution of the Holliday intermediate." @default.
- W1910389675 created "2016-06-24" @default.
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- W1910389675 date "1988-09-01" @default.
- W1910389675 modified "2023-10-16" @default.
- W1910389675 title "Holliday intermediates and reaction by-products in FLP protein-promoted site-specific recombination." @default.
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- W1910389675 doi "https://doi.org/10.1128/mcb.8.9.3784" @default.
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