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

Sharples, G.J.; Corbett, L.M.; Graham, I.R.

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.

Citation

Sharples, G., Corbett, L., & Graham, I. (1998). Lambda Rap protein is a structure-specific endonuclease involved in phage recombination

• Journal Article Type: Article
• Publication Date: 1998
• Journal: Proc Natl Acad Sci USA
• Volume: 95
• Pages: 13507-13512
• Public URL: https://durham-repository.worktribe.com/output/1583503
• Publisher URL: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9811830