Fig. 4: SSB-χ interactions are required for YoaA-χ to bind DNA-SSB.

A EMSA of Cy5-labeled dT₆₅ oligo (50 nM, S21) titrated with YoaA-χ (50, 100, 200, and 400 nM) with (right panel) and without (left panel) SSB (75 nM) pre-bound to the DNA. Quantification of percent of DNA bound by YoaA-χ in the absence (black) and presence (green) of SSB versus YoaA-χ concentration. B EMSA of Cy5-labeled dT₆₅ oligo (50 nM, S21) titrated with DinG (50, 100, 200, and 400 nM) with (right panel) and without (left panel) SSB (75 nM) pre-bound to the DNA. Quantification of percent of DNA bound by DinG in in the absence (black) and presence (green) of SSB versus DinG concentration. C EMSA of Cy5-labeled dT₆₅ oligo (50 nM, S21) titrated with YoaA-χ (50, 100, 200, and 400 nM) with (right panel) and without (left panel) SSB ΔC1 (75 nM) pre-bound to the DNA. Quantification of percent of DNA bound by YoaA-χ in the absence (black) and presence (pink) of SSB ΔC1 versus YoaA-χ concentration. D EMSA of Cy5-labeled dT₆₅ oligo (50 nM, S21) titrated with YoaA-χ R128A (50, 100, 200, and 400 nM) with (right panel) and without (left panel) SSB (75 nM) pre-bound to the DNA. Quantification of percent of DNA bound by YoaA-χ R128A in the absence (black) and presence (green) of SSB versus YoaA-χ R128A concentration. E EMSA of Cy5-labeled dT₆₅ oligo (50 nM, S21) titrated with DinG (50, 100, 200, and 400 nM) with (right panel) and without (left panel) SSB ΔC1 (75 nM) pre-bound to the DNA. Quantification of percent of DNA bound by DinG in the absence (black) and presence (green) of SSB ΔC1 versus DinG concentration. The (-) lanes contain zero helicase in the reaction. The gels shown are representative of three experiments. Dots represent individual experiments, dashed lines represent averages of these three experiments, and error bars indicate standard deviation. Source data are provided as a source data file.