Figure 4: BLM-dependent unwinding activity on a G4 substrate.
From: Mechanistic insight into the interaction of BLM helicase with intra-strand G-quadruplex structures
(a) Quantification of BLM unwinding efficiency at 50 nM BLM and 2 mM ATP for the G4, G4 (5 nt) and G4 (10 nt) substrates (Error bar=s.e.m.; n=5). (b,c) FRET histograms of the G4 (5 nt) and G4 (10 nt) substrates (b,c, respectively) in the presence of 50 nM BLM and at different ATP concentrations. (d,e) Representative single-molecule trajectories of the G4 (5 nt) and G4 (10 nt) substrates (d,e, respectively) in the presence of 50 nM BLM and 10 μM ATP. FRET trajectories were fitted with HMM (Cyan). (f,g) Generated TDP matrix of the G4 (5 nt) and G4 (10 nt) substrates (f,g, respectively) in the presence of 50 nM BLM and 10 μM ATP. (h,i) The calculated mean unfolding and refolding rates for the G4 (5 nt) and G4 (10 nt) substrates (h,i, respectively) in the presence of 50 nM BLM and at different ATP concentrations. (Error bars=s.e.m.; n>15 for all measurements).
