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λ Rap Protein is a Structure-Specific Endonuclease Involved in Phage Recombination

Gary J. Sharples, Lisa M. Corbett and Ian R. Graham
Proceedings of the National Academy of Sciences of the United States of America
Vol. 95, No. 23 (Nov. 10, 1998), pp. 13507-13512
Stable URL: http://www.jstor.org/stable/46716
Page Count: 6
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λ  Rap Protein is a Structure-Specific Endonuclease Involved in Phage Recombination
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Abstract

Bacteriophage λ encodes a number of genes involved in the recombinational repair of DNA double-strand breaks. The product of one of these genes, rap, has been purified. Truncated Rap proteins that copurify with the full-length form are derived, at least in part, from a ρ -dependent transcription terminator located within its coding sequence. Full-length and certain truncated Rap polypeptides bind preferentially to branched DNA substrates, including synthetic Holliday junctions and D-loops. In the presence of manganese ions, Rap acts as an endonuclease that cleaves at the branch point of Holliday and D-loop substrates. It shows no obvious sequence preference or symmetry of cleavage on a Holliday junction. The biochemical analysis of Rap gives an insight into how recombinants could be generated by the nicking of a D-loop without the formation of a classical Holliday junction.

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