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Article

Directional resolution of synthetic holliday structures by the Cre recombinase.

The Journal of biological chemistry - 17 Aug 2001

Lee L, Sadowski P D

Abstract excerpt

The Cre recombinase of bacteriophage P1 cleaves its target site, loxP, in a defined order. Recombination is initiated on one pair of strands to form a Holliday intermediate, which is then resolved by cleavage and exchange of the other pair of strands to yield recombinant products. To investigate the influence of the loxP sequence on the directionality of resolution, we constructed synthetic Holliday (chi)...

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Identifiers

PMID: 11406627
DOI: 10.1074/jbc.M103739200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Directional resolution of synthetic holliday structures by the Cre recombinase.PMID 11406627Read ↗

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Engineering spacer specificity of the Cre/loxP system.Semantic proximity Read ↗

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Control of Cre recombination by regulatory elements from Xer recombination systems.Semantic proximity Read ↗

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Coordinated control of XerC and XerD catalytic activities during Holliday junction resolution.Semantic proximity Read ↗

Non-equivalent interactions between amino-terminal domains of neighboring lambda integrase protomers direct Holliday junction resolution.Semantic proximity Read ↗

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