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. 2007 Dec 17;36(3):963–969. doi: 10.1093/nar/gkm1118

Figure 1.

Figure 1.

Characterization of RNase T-tat. (a) The expression, purification and ribonuclease activity of RNase T-tat. Lanes 1–3 are Coomassie staining of a 15% SDS-polyacrylamide gel analyzing the expression of RNase T-tat gene with (lane 1) and without (lane 2) IPTG induction and the purified recombinant protein RNase T-tat (lane 3). Lanes 4 and 5 are the RNA-impregnated gel electrophoresis analysis of the ribonuclease activity of recombinant RNase T-tat against naked RNA (lane 4) and poly G (lane 5). The gels were visualized using toluidine blue O staining of RNA. Negative results were obtained for poly A- and poly U-impregnated gels. (b) The simulated structure of RNase T-tat (yellow ribbon with the TAT peptide in red) superimposed on the structure of RNase T1 (green ribbon whose L3 loop is blue in color). (c) Molecular docking of RNase T-tat with TAR RNA. Both protein (gray) and RNA (orange) present in backbone mode except for the contact region, which is highlighted with a wire-structure in red color for the amino acid residues and yellow color for the UCU bulge. (d) Atomic detail of interaction between the Arg70 of the RNase T-tat and U33 of TAR RNA. The distances indicated (underlined) affect docking and the measurements were made after docking.