Fig. 4: Distinct and competitive binding modes of RSM to DNA and RPA. | Nature Communications

Fig. 4: Distinct and competitive binding modes of RSM to DNA and RPA.

From: Recognition and coacervation of G-quadruplexes by a multifunctional disordered region in RECQ4 helicase

Fig. 4

a Random Coil Index order parameters (RCI-S2) and secondary structure from Chemical Shift Index (CSI) (C: random coil, H: helix) calculated from secondary chemical shifts and 15N R2 relaxation rates measured for free RSM (black; 50 μM RSM) and RSM in complex with DNA (cyan; 4× molar excess dsDNA) or RPA (pink; 16× molar excess RPA32C). Relaxation experiments were performed once. Error bars represent the standard error of the fitted parameters. b Competitive binding of DNA (4× molar excess) and RPA (16× molar excess) to 50 μM RSM, observed by 2D NMR titrations and shown for two residues of RSM. Gray arrows indicate peak trajectories upon binding of each partner, and black arrows indicate peak trajectories upon competition with the other partner (left). Fitted spectra following 2D line shape analysis of the competition binding (right). c Summary of kinetic, thermodynamic, and structural parameters of RSM interactions. Source data are provided as a Source Data file.

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