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. 2021 May 28;297(1):100844. doi: 10.1016/j.jbc.2021.100844

Figure 2.

Figure 2

The association between the NCP and RAD51AP1 occurs through the RAD51AP1-F3 domain.A, schematic of full-length RAD51AP1 (isoform two; in black) and RAD51AP1 fragments (F1 (blue), F2 (purple), and F3 (red)), as described earlier (7), including the two mapped DNA-binding domains (gray), as previously shown (4, 6). B, EMSA of MBP-/His6-tagged full-length RAD51AP1, -F1 and -F3 (0.2 μM each) with the NCP (0.2 μM) assessed by ethidium bromide. C, western blots obtained after Ni-NTA pull-down of MBP-RAD51AP1-His6 to show that RAD51AP1 directly interacts with histone H3 (lane 5). D, western blots obtained after Ni-NTA pull-down of the three MBP-/His6-tagged RAD51AP1 fragments to show that the interaction between RAD51AP1 and histone H3 occurs through the F3 domain (lane 6).