Joseph Bartho

Extended Data Fig. 1 Structural comparison and cryo-EM densities of Mot1 substrate recognition, pre- and posthydrolysis states and Swi2/Snf2 brace comparison. a) Quantification of the native electrophoretic mobility shift assay in Fig. 1b/ Fig. 6d. The bars show the mean from n=4 technical replicates. The error bar represents +/- standard deviation from the mean. b) Structure TBP:DNA (left) and after binding of Mot1 (right), which unbends the DNA by 45°.

DNA double-strand breaks (DSBs) threaten genome stability and are linked to tumorigenesis in humans. Repair of DSBs requires the removal of attached proteins and hairpins through a poorly understood but physiologically critical endonuclease activity by the Mre11-Rad50 complex. Here, we report cryoelectron microscopy (cryo-EM) structures of the bacterial Mre11-Rad50 homolog SbcCD bound to a protein-blocked DNA end and a DNA hairpin.

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