lambda Rap protein is a structure-specific endonuclease involved in phage recombination.

Abstract:

:Bacteriophage lambda 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 rho-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.

authors

Sharples GJ,Corbett LM,Graham IR

doi

10.1073/pnas.95.23.13507

subject

Has Abstract

pub_date

1998-11-10 00:00:00

pages

13507-12

issue

23

eissn

0027-8424

issn

1091-6490

journal_volume

95

pub_type

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