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. 1988 Nov;85(21):7902–7906. doi: 10.1073/pnas.85.21.7902

Holliday junctions in FLP recombination: resolution by step-arrest mutants of FLP protein.

M Jayaram 1, K L Crain 1, R L Parsons 1, R M Harshey 1
PMCID: PMC282308  PMID: 3054874

Abstract

The FLP "recombinase" of the 2-micron circle yeast plasmid can resolve synthetic FLP site-Holliday junctions. Mutants of the FLP protein that are blocked in recombination but are normal in substrate cleavage can also mediate resolution. The products of resolution by these mutants are almost exclusively nicked molecules with a protein-bound 3' end. There is no significant asymmetry in strand cleavage (top versus bottom) by the mutants in linear or in circular FLP substrates; nor is there a bias in resolution (toward parentals or toward recombinants) of Holliday junctions (corresponding to top- or to bottom-strand exchange) by wild-type FLP. During normal FLP recombination, a small amount of the expected Holliday intermediate can be detected.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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