Resolution of Holliday junctions in vitro requires the Escherichia coli ruvC gene product.
收藏PubMed Central1991-07-15 更新2026-05-16 收录
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https://pmc.ncbi.nlm.nih.gov/articles/PMC52022/
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资源简介：
In previous studies, Holliday junctions generated during RecA-mediated strand-exchange reactions were resolved by fractionated Escherichia coli extracts. We now report the specific binding and cleavage of synthetic Holliday junctions (50 base pairs long) by a fraction purified by chromatography on DEAE-cellulose, phosphocellulose, and single-stranded DNA-cellulose. The cleavage reaction provided a sensitive assay with which to screen extracts prepared from recombination/repair-deficient mutants. Cells with mutations in ruvC lack the nuclease activity that cleaves synthetic Holliday junctions in vitro. This deficiency was restored by a multicopy plasmid carrying a ruvC+ gene that overexpressed junction-resolving activity. The UV sensitivity and deficiency in recombinational repair of DNA exhibited by ruv mutants lead us to suggest that RuvC resolves Holliday junctions in vivo. IMAGES:
提供机构：
National Academy of Sciences
创建时间：
1991-07-15
