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. Author manuscript; available in PMC: 2012 Dec 10.
Published in final edited form as: DNA Repair (Amst). 2011 Oct 2;10(12):1223–1231. doi: 10.1016/j.dnarep.2011.09.010

Figure 1. The C-terminal domain of DdrB is dispensable for radioresistance and binding to single-stranded DNA.

Figure 1

(A) Radioresistance of mutants expressing truncated or C-terminal fused DdrB proteins. Survival curves of wild-type (filled squares), GY12835: ΔddrB (filled circles), GY13928: ddrBΔ5 (open triangles), GY13930: ddrBΔ41 (open circles) are shown. (B) Binding affinities of DdrB and DdrBΔ41 proteins to ssDNA were measured by electrophoretic mobility shift assay. Increasing protein concentrations (from 10 nM to 10 μM) were incubated with 50 μM fluorescent oligonucleotides and loaded onto a native 4% PAGE. Protein to total nucleotides ratios are indicated on the top of each lane.