The discovery and characterization of two novel structural motifs on the carboxy-terminal domain of kinetoplastid RNA editing ligases

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FIGURE 5.
FIGURE 5.

In vitro functional assays of KREL1 with and without KREPA2 over time. (A) Three-step ligation activity over time of KREL1 WT with and without the addition of KREPA2 WT and KREPA2 ΔαΗ1 mutant. (B) Two other conditions, KREL1 WT with KREPA2 ΔOB mutant and KREPA2 ZnF mutant (alanine substitutions of cysteine residues), were extracted from the graph of panel A for easier visualization. (C) KREL1 adenylylation activity over time with and without the addition of KREPA2 WT. (D) KREL1 deadenylylation activity over time with and without the addition of KREPA2 WT. (E) KREL1 preadenylated ligation activity over time with and without the addition of KREPA2 WT. Error bars on each graph represent SD obtained from three replicate experiments.

This Article

  1. RNA 29: 188-199