Multiple domains of the integral KREPA3 protein are critical for the structure and precise functions of RNA editing catalytic complexes in Trypanosoma brucei

Summary of A3 protein characteristics, interactions, and effects of mutations. (A) Location of OB-fold domains and residues with planar side chains of the A3 OB-fold (blue) in complex with A6 (tan). (B) Location of cross-linked Lys residues (orange) in the predicted AlphaFold model of A3 (McDermott et al. 2016) showing the OB-fold (blue), ZFs (yellow) and ZF, and OB-fold adjacent regions (teal). (C) Summary diagram showing cross-links of A3 Lys residues with other CC proteins, domain locations, and effects of the mutations on cell line growth, CCs, and editing. Heat map indicates increasing strength of observed defects in CC abundance, association, and editing of A6, RPS12, and MURF2, as increasing intensity of blue shades (see legend).