PMID:1829835
| Citation |
Connolly, B, Parsons, CA, Benson, FE, Dunderdale, HJ, Sharples, GJ, Lloyd, RG and West, SC (1991) Resolution of Holliday junctions in vitro requires the Escherichia coli ruvC gene product. Proc. Natl. Acad. Sci. U.S.A. 88:6063-7 |
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| Abstract |
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. |
| Links | |
| Keywords |
Bacterial Proteins/genetics; Bacteriophage phi X 174/genetics; Base Sequence; DNA Replication; DNA, Bacterial/genetics; DNA, Viral/genetics; Endodeoxyribonucleases; Escherichia coli/genetics; Escherichia coli Proteins; Gene Expression; Genes, Bacterial; Molecular Sequence Data; Oligonucleotide Probes; Plasmids |
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