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- W2034743014 abstract "One class of superfamily-2 (SF2) helicases, the RecQ family, plays crucial roles in DNA repair and homologous recombination in order to maintain the genome integrity. Archaeal RecQ-like DNA helicases, such as Hjm/Hel308, have been biochemically characterized in hyperthermophilic and thermophilic archaea. The studies suggest that Hjm/Hel308 helicases target stalled replication forks and have specificity for unwinding lagging strands. In this study, we cloned and purified Hjm/Hel308 homologue (MacHjm) from a mesophilic archaeon, Methanosarcina acetivorans. Single molecule fluorescence resonance energy transfer (smFRET) assay was used to study the single-stranded DNA (ssDNA) binding ability and behavior, the double-stranded DNA (dsDNA) unwinding kinetics, and Holliday junction migration activity induced by MacHjm. By this method, we determined that four MacHjm molecules were able to bind to 17-nucleotide ssDNA with each MacHjm occupying three to four nucleotides of the DNA. In addition, we were able to observe the binding and unwinding activity of MacHjm on DNA in real time. The MacHjm was observed to bind to ssDNA and translocate on ssDNA in 3′ to 5′ in ATP dependent manner. Within three seconds MacHjm was able to complete the unwinding of 18 base-pair dsDNA. The results from our smFRET studies on MacHjm provide important insights into DNA unwinding, stalled replication fork processing, and Holliday junction migration mechanisms for SF2 helicase." @default.
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- W2034743014 date "2009-02-01" @default.
- W2034743014 modified "2023-09-26" @default.
- W2034743014 title "Single-Molecule Fluorescence Resonance Energy Transfer Studies of Hjm/Hel308 DNA Helicase in Mesophilic Archaeon, Methanosarcina acetivorans" @default.
- W2034743014 doi "https://doi.org/10.1016/j.bpj.2008.12.2114" @default.
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