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. 2008 May 3;36(11):3579–3589. doi: 10.1093/nar/gkn236

Figure 1.

Figure 1.

Different constructs of Tudor-SN, and their DNase and RNase activity assays. (A) Six constructs of Tudor-SN were prepared. (B) The purity of Tudor-SN proteins was assayed by 10% SDS–PAGE. (C) Plasmid digestion assays show that TSN, TSN-90 and TSN-70 had detectable DNase activity (14% to 3%), whereas TSN-64, TSN-50 and TSN-25 had residual activity (1%). (D) Tudor-SN truncated mutants were incubated with 20-bp RNAs (5′-end labeled on top strand) containing the wobble base-paired IIUI/UIUU sequence or Watson–Crick base-paired AAUA/UAUU sequence, in a reaction buffer for 8 h at 20°C. TSN and TSN-90 cleaved IIUI-dsRNA with the highest activities (5 and 15%), whereas TSN-70, TSN-64, TSN-50 and TSN-25 had no detectable activities (marked by -). The intensity of the cleavage product gel band of the 10-mer RNA (marked by *) was quantified and the substrate cleavage percentage was estimated, listed at the bottom of the gel. Undetectable cleavage was marked by -.