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- W2000517812 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. In the absence of calcium ions, RecBCD translocation rate is found to slow down after recognizing chi sequence. However, in the presence of calcium ions, the rate change in individual RecBCD translocation is abolished, returning similar averaged translocation rate before (71 ± 20 bp/s) and post (81 ± 36 bp/s) chi-sequence, under 30μM ATP. Furthermore, large portion of individual RecBCD unwinding time courses (13 out of 32) revealed repetitive forward and backward translocation along individual DNA molecules. Compared with the experiments carried out without calcium ions, the processivity of RecBCD also decreases when the nuclease domain is inhibited. About 50 percent of translocating tethers (17 out of 32) stalled within 1.5 Kb DNA used in the presence of calcium ions. Together, these observations suggest that the nuclease domain, located in the RecB subunit, plays regulatory roles not only in RecBCD translocation properties but also in chi-regulated intersubunit interaction in this complex machine of the RecBCD enzyme." @default.
- W2000517812 created "2016-06-24" @default.
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- W2000517812 date "2010-01-01" @default.
- W2000517812 modified "2023-10-18" @default.
- W2000517812 title "Intersubunit Regulation Between Nuclease and Helicase Domains of Recbcd Enzyme" @default.
- W2000517812 doi "https://doi.org/10.1016/j.bpj.2009.12.405" @default.
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