Fig. 4

Schematic comparison of the domain architecture of the macrodomain-containing ARTD family members ARTD7, ARTD8 and ARTD9 Domain architecture of the human diptheria toxin-like macro-domain containing mono-ADP-ribosyltransferases and ARTD family members ARTD7, ARTD8 and ARTD9. The following domains are indicated: The diptheria toxin-like ART(D) domain is the catalytic core required for basal (mono-)ADP-ribosyltransferae (ART) activity. The WWE domain is named after three conserved residues (W-W-E) and is predicted to mediate specific protein-protein interactions in ubiquitin- and ADP-ribose conjugation systems [555, 636, 637]. The macro or A1pp domains are structurally related to the catalytic domain of enzymes that process ADP-ribose-1-phosphate, a reaction product derived from ADP-ribose 1-2′cyclic phosphate generated by TpT [638]. The macrodomain can serve as ADP-ribose or O-acetyl-ADP-ribose binding module [638]. RRM is an RNA and poly-ADP-ribose-binding/recognition motif [639]