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. 2010 May 14;38(18):6219–6233. doi: 10.1093/nar/gkq372

Figure 2.

Figure 2.

G4-RNA unwinding and binding by N-terminal truncated RHAU proteins. (A) G4-RNA unwinding assay: radio-labelled tetramolecular rAGA at a concentration of 4 nM was incubated in the presence of ATP without protein (−) or with increasing amounts (1, 3, 10 and 30 nM) of WT RHAU or ΔGly–RSM mutant. The reaction products were resolved by native PAGE after disrupting RNA–protein interactions with SDS. An autoradiogram of the gel is shown. The positions of the tetraplex substrate RNA (G4-RNA) and the unwound single-stranded product (ssRNA) are denoted on the left. An aliquot of the tetraplex substrate that was heat-denatured (95°C, 5 min) and then quenched (ΔT) serves as a marker for the position of ssRNA. (B) G4-RNA binding assay: radio-labelled tetramolecular rAGA at a concentration of 100 pM was incubated without protein (−) or with increasing amounts (1, 3, 10 and 30 nM) of WT RHAU or ΔGly–RSM mutant in the absence of ATP. The reaction mixtures were analysed by native PAGE. An autoradiogram of the gel is shown. The positions of the free tetramolecular RNA substrate and the protein–RNA complex are indicated on the left.