PMID:10037776
| Citation |
Grainge, I and Sherratt, DJ (1999) Xer site-specific recombination. DNA strand rejoining by recombinase XerC. J. Biol. Chem. 274:6763-9 |
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| Abstract |
Xer site-specific recombination functions in the stable maintenance of circular replicons in Escherichia coli. Each of two related recombinase proteins, XerC and XerD, cleaves a specific pair of DNA strands, exchanges them, and rejoins them to the partner DNA molecule during a complete recombination reaction. The rejoining activity of recombinase XerC has been analyzed using isolated covalent XerC-DNA complexes resulting from DNA cleavage reactions upon Holliday junction substrates. These covalent protein-DNA complexes are competent in the rejoining reaction, demonstrating that covalently bound XerC can catalyze strand rejoining in the absence of other proteins. This contrasts with a recombinase-mediated cleavage reaction, which requires the presence of both recombinases, the recombinase mediating catalysis at any given time requiring activation by the partner recombinase. In a recombining nucleoprotein complex, both cleavage and rejoining can occur prior to dissociation of the complex. |
| Links | |
| Keywords |
Base Sequence; DNA Nucleotidyltransferases/genetics; DNA, Bacterial/genetics; Escherichia coli/genetics; Escherichia coli Proteins; Integrases; Molecular Sequence Data; Recombinases; Recombination, Genetic |
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