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. 2023 Jul 13;51(16):8643–8662. doi: 10.1093/nar/gkad589

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© The Author(s) 2023. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 5. — RAD54-T700D binds RAD51 with higher affinity. (A, B) RAD54 phosphomimic mutant proteins exhibit different affinities to RAD51 than RAD54-WT (reactions eluted from beads shown in silver-stained gel in (A) and quantified in (B). (C, D) RAD54-T700D shows enhanced affinity for RAD51 (Eluate (E) and Supernatant (S) fraction shown in silver-stained gel (C), and quantification shown in (D). (E, F) ATPase activity of RAD54-WT, NTD mutants (T2D, T3D) and CTD mutant (T700D) with dsDNA shown as %ATP hydrolysis (y-axis) in TLC and in the absence and presence of RAD51 (E). Quantification of the results (F). One-way ANOVA, Tukey's multiple comparison test (*P< 0.05; **P< 0.01; ****P< 0.0001).