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Rearrangement of RNA secondary structure is crucial for numerous biological processes . RNA helicases participate in these rearrangements through the unwinding of duplex RNA. We report here ...
been shown to catalyse branch migration , works less processively in isolated unwinding reactions and it has been shown that a mutant RuvB with a damaged DNA helicase activity can still catalyse branch ...
by the E.coli UvrD helicase (8) and branch migration catalyzed by RuvAB (19,20). UvrD is a 3′ to 5′ DNA helicase that belongs to the superfamily 1 and shares extensive sequence similarity (21) and high structural ...
, and coordinates the HJ processing (39). Structural analysis suggested that ATP binding and hydrolysis cause conformational change of SisPINA which promotes HJ branch migration . However, more biochemical, structural ...
Initially discovered in Escherichia coli, RuvAB proteins are ubiquitous in bacteria and play a dual role as molecular motor proteins responsible for branch migration of the Holliday ...
). The ability of DnaB to dislodge proteins from DNA was proposed to facilitate branch migration in DNA recombination or DNA repair. In Saccharomyces cerevisiae, termination of replication forks is controlled ...
activities on partial duplex DNA . However, they promote different outcomes with synthetic DNA structures that mimic Holliday junctions or a replication fork. AtRECQ2 catalyzes Holliday junction branch ...
-stranded (ss) DNA . Consistent with a crystal structure of bacterial RecQ bound to ssDNA by base stacking, abasic sites blocked RecQ unwinding . Removal of the HRDC domain eliminates the slow mode while ...
DNA . Here, we study the unwinding mechanism of E1 at the single-molecule level using magnetic tweezers. The result reveals that E1 as a single hexamer is a poorly processive helicase with a low ...
of genome such as branch migration , regression of stalled fork, and the resolution of telomeric secondary structures (1). WRN interacts with many proteins in DNA metabolism (1,11–13). These include ...
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