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- W2011392023 startingPage "817" @default.
- W2011392023 abstract "Despite the importance of hairpin opening in antigen receptor gene assembly, the molecular machinery that mediates this reaction has not been defined. Here, we show that RAG1 plus RAG2 can open DNA hairpins. Hairpin opening by RAGs is not sequence specific, but in Mg2+, hairpin opening occurs only in the context of a regulated cleavage complex. The chemical mechanism of hairpin opening by RAGs resembles RSS cleavage and 3' end processing by HIV integrase and Mu transposase in that these reactions can proceed through alcoholysis. Mutations in either RAG1 or RAG2 that interfere with RSS cleavage also interfere with hairpin opening, suggesting that RAGs have a single active site that catalyzes several distinct DNA cleavage reactions." @default.
- W2011392023 created "2016-06-24" @default.
- W2011392023 creator A5003699560 @default.
- W2011392023 creator A5005516359 @default.
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- W2011392023 creator A5025061989 @default.
- W2011392023 creator A5031647069 @default.
- W2011392023 creator A5068360457 @default.
- W2011392023 date "1998-12-01" @default.
- W2011392023 modified "2023-10-11" @default.
- W2011392023 title "Hairpin Coding End Opening Is Mediated by RAG1 and RAG2 Proteins" @default.
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