All Outputs (2)

Analysis of conserved basic residues associated with DNA binding (Arg69) and catalysis (Lys76) by the RusA Holliday junction resolvase. (2000)
Journal Article
Bolt, E., Sharples, G., & Lloyd, R. (2000). Analysis of conserved basic residues associated with DNA binding (Arg69) and catalysis (Lys76) by the RusA Holliday junction resolvase. Journal of Molecular Biology, 304, 165-176

Holliday junctions are key intermediates in both homologous recombination and DNA repair, and are also formed from replication forks stalled at lesions in the template strands. Their resolution is critical for chromosome segregation and cell viabilit... Read More about Analysis of conserved basic residues associated with DNA binding (Arg69) and catalysis (Lys76) by the RusA Holliday junction resolvase..

The acidic pin of RuvA modulates Holliday junction binding and processing by the RuvABC resolvasome. (2000)
Journal Article
Ingleston, S., Sharples, G., & Lloyd, R. (2000). The acidic pin of RuvA modulates Holliday junction binding and processing by the RuvABC resolvasome. The EMBO Journal, 19, 6266-6274

Holliday junctions are four-way branched DNA structures formed during recombination, replication and repair. They are processed in Escherichia coli by the RuvA, RuvB and RuvC proteins. RuvA targets the junction and facilitates loading of RuvB helicas... Read More about The acidic pin of RuvA modulates Holliday junction binding and processing by the RuvABC resolvasome..