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. Author manuscript; available in PMC: 2011 Jan 1.
Published in final edited form as: Biochim Biophys Acta. 2010 Jan–Feb;1799(1-2):119. doi: 10.1016/j.bbagrm.2009.11.008

Figure 5.

Figure 5

Characterization of HMGB1 Isolated from HeLa Cells (from Figure 4 of ref. 23). (A) Schematic representation of the dRP lyase substrate generated by treatment of the radiolabeled oligonucleotide substrates with UDG and APE1. (B) The dRP lyase activities of Pol β and HMGB1. (C) The purified HMGB1 (lane 2 and 3, 0.45 and 0.9 μg, respectively) was renatured (lane 4, ~0.2 μg) and analyzed by NuPAGE Bis-Tris gel electrophoresis. (D) NaBH4 crosslinking of renatured HMGB1 at the concentrations of 500 nM (lane 2), 140 nM (lane 3) and 280 nM (lane 4). (E) The dRP lyase activity of renatured HMGB1 at concentration of 420 nM. (F) Quantification of the dRP lyase activities of purified (open circles) and renatured HMGB1 (filled circles). (G) The effects of HMGB1 on single-nucleotide BER.