Sulfonated inhibitors of the RNA editing ligases validate the essential role of the MRP1/2 proteins in kinetoplastid RNA editing

C35 and MrB disengage MRP1/2 association with RECC and suppress in vitro RNA editing activity. KREL1 Calmodulin eluates were prepared after treatment with C35, MrB, and RNase A while binding to the Calmodulin affinity resin. (A) Western blot analysis against KREPA1, KREPA2, KREL1, and KREPA3 antibodies in the top panel and against MRP2 antibody in the bottom panel. Each lane contains ∼900 ng of the respective eluate. (B) “Full-round” and (C) “precleaved” RNA editing activities of these eluates in absence and presence of rMRP1/2 (500 nM).