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

(Downloading may take up to 30 seconds. If the slide opens in your browser, select File -> Save As to save it.)

Click on image to view larger version.

FIGURE 4.
FIGURE 4.

Locating motif VI on KREL1 carboxy-terminal domain. (A) Three-step ligation assay with KREL1 FL and CTD truncations. (B) Adenylylation assay with KREL1 FL and CTD truncations. (C) Adenylylation assay of KREL1 WT and group mutants (alanine substitutions for residues 441–444, KWKE) with and without the addition of KREPA2. (D) Adenylylation of point mutants and group mutants of KREL1, compared to adenylylation activity of KREL1 WT. Group mutants (GM) include KWKE substituted for AWAA and AAAA. (E) Adenylylation assay of KREL1 WT and group mutants with the addition of KREPA2 WT. Error bars on each graph represent SD obtained from three replicate experiments. (****) P < 0.0001, (***) P < 0.001, (**) P < 0.01, (*) P < 0.05.

This Article

  1. Published in Advance November 18, 2022, doi: 10.1261/rna.079431.122 RNA 29: 188-199

Current Issue

  1. August 2026, 32 (8)
  1. Current Issue
  1. Alert me to new issues of RNA