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. Author manuscript; available in PMC: 2015 Apr 1.
Published in final edited form as: Nat Struct Mol Biol. 2014 Sep 7;21(10):893–900. doi: 10.1038/nsmb.2886

Fig. 4.

Fig. 4

Rad52 regulates RPA turnover. (a) Schematic for determining Rad52 binding lifetime on RPA–ssDNA. (b) Kymographs showing SNAP488–Rad52 dissociation over 10–minutes (upper panel) or 2–hours (lower panel); shuttering time was adjusted so that the total illumination time was identical for both experimental measurements 39. (c) Models for the potential influence of Rad52 on RPA turnover. (d) RPA–mCherry turnover after chasing with wt RPA, ±1 nM SNAP488–Rad52. Aligned images of ssDNA molecules showing persistent co–localization of SNAP488–Rad52 and RPA–mCherry clusters. (e) Examples showing quantitation of RPA–mCherry turnover on single ssDNA molecules. (f) Aligned images of RPA–mCherry and SNAP488–Rad52 on different ssDNA molecules. (g) Line graphs of SNAP488–Rad52 and RPA–mCherry co–localization. (h) Correlation analysis of RPA–mCherry and SNAP488–Rad52 after exchange with wt RPA (n = 255).