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. Author manuscript; available in PMC: 2022 Mar 4.
Published in final edited form as: Mol Cell. 2021 Jan 15;81(5):1074–1083.e5. doi: 10.1016/j.molcel.2020.12.036

Figure 5. RADX must interact with RAD51 to inhibit strand exchange and D-loop formation.

Figure 5.

(A) The ssDNA-dependent ATPase activity of RAD51 was measured in the presence of wild-type, QVPK, and OB2m RADX proteins (n=3 +/− SD). (B) Strand exchange assay in which RADX wild-type and QVPK mutant were added at the same time as RPA (n=3 +/−SD). (C) D-loop formation assay with representative gel and quantitation (n=3 +/−SD). (D) Nucleofilament formation by RAD51 without RADX (n=178) in the presence of RADX (n=163), RADX OB2m (n=194), or RADX QVPK (n=208). (Error bars are SEM). The panels are representative micrographs.