Fig. 5: RNF114 ZnF2 + ZnF3 + UIM domains are responsible for ADPr-Ub binding and elongation.
From: Identification of RNF114 as ADPr-Ub reader through non-hydrolysable ubiquitinated ADP-ribose
a RNF114 domain organisation and truncations and mutations used in this study. b Binding affinities of RNF114 truncations and mutants to biotin-ADPr-Ub probe 1 determined using Bio-Layer Interferometry. c Ub elongation reactions of biotin-ADPr-Ub probe 1 or biotin-Ub in vitro using RNF114 truncations and mutants. d 32P-NAD+-Ub in vitro elongation reactions with RNF114 truncations and mutants. e Ub elongation reactions of biotin-ADPr-Ub probe 1 or biotin-Ub using RNF114 linker mutations as indicated. f Quantification of biotin-ADPr-Ub(n) normalized to RNF114 WT. Data are presented as mean values ± SEM. For all experiments, two independent biological replicates were performed with similar results. Source data are provided as a Source Data file.
