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. 2011 Jun 9;286(30):26568–26575. doi: 10.1074/jbc.M111.235721

FIGURE 3.

FIGURE 3.

A3G-T218E has diminished deaminase activity but retains DNA binding ability. A, representative images from titrated A3G oligo deaminase assays. The upper band is the intact oligo, and the lower band is the product of deamination, uracil excision, and strand cleavage. B, representative images from A3G ssDNA binding assays. Free oligo and protein-bound complexes are labeled. C, quantification of A3G deaminase activity in A and replicas not shown. Data are plotted as the mean ± S.D. of three independent experiments. D, quantification of A3G EMSA data in B. Data are plotted as the mean ± S.D. of three independent experiments. E, Coomassie-stained gel illustrating the purity of A3G enzymes used in these experiments. F, representative images from AID ssDNA binding assays. G, quantification of AID EMSA data in F. Data are plotted as the mean ± S.D. of three independent experiments. H, Coomassie-stained gel illustrating the purity of AID enzymes used in the ssDNA binding assays. The identity of the AID bands was confirmed by immunoblotting (not shown).