Fig. 6: Cooperative interaction of the BED domain with Hermes left-end (LE) STR1-STR2 motif. | Nature Communications

Fig. 6: Cooperative interaction of the BED domain with Hermes left-end (LE) STR1-STR2 motif.

From: Zinc-finger BED domains drive the formation of the active Hermes transpososome by asymmetric DNA binding

Fig. 6

a The sequence of the top strand of the DNAs ran17, LE11-27mut, and LE11-27 double-stranded DNAs. The subterminal repeats STR1 and STR2 are underlined, and their orientation is indicated with arrows. The mutated bases in LE11-27mut are in bold. Ran17 is the unspecific interaction control. b The electrophoretic mobility shift assay (EMSA) gels (15% polyacrylamide, 0.5X TBE). The DNAs (1 µM) were titrated with increasing amounts of BED protein from 0 (-) to 10 µM. c Binding curves of ran17 (red), LE11-27mut (black), and LE11-27 (blue) with the BED domain derived from EMSAs performed in triplicate (Supplementary Fig. 12). Values are mean ± standard deviations. The dissociation constants (Kd) from the fitting are reported for each DNA sequence.

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