Abstract
The Escherichia coliRecBCD helicase/nuclease initiates homologous recombinational repair of damaged blunt-end duplex DNA molecules. RecBCD, a multifunctional enzyme complex, contains two DNA motors as well as a nuclease domain to process duplex DNA and generate single-stranded DNA molecules. We used single-molecule tethered particle motion (TPM) experiments to investigate the regulation mechanism between the nuclease domain and two helicase domains of RecBCD enzyme using calcium ions, which specifically inhibit nuclease activity.
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