Molecules and Cells

Indexed in /covered by CAS, KoreaScience & DOI/Crossref:eISSN 0219-1032   pISSN 1016-8478

Fig. 1.

Download original image
Fig. 1. (A) Recombinant GST-RNF168 was loaded onto SDS-PAGE and then transferred to the NC membrane, followed by PAR overlay assay. PAR-binding activity of RNF168 was analyzed by immunoblotting with anti-PAR antibody. GST or H4 was used negative or positive control, respectively. Black and red star indicate GST and H4 protein, respectively. (B) Construction of RNF168 deletion mutants. (C, D) PAR overlay assay was performed with WT, N terminal (N)-, and C terminal (C)-mutants of RNF168 in setting of non-denaturing (C) or denaturing condition (D). (E) Potential PAR-binding sites of RNF168 were analyzed in comparison with the classical PAR-binding motif as indicated. Gray arrowheads indicate postulated PAR-binding residues of RNF168 (F) To validate PAR binding activity of RNF168, its point mutants were generated by a site-direct mutagenesis as indicated. Gray arrow indicates the mutated sites of RNF168 (G) PAR overlay assay was performed along with WT and point mutants of RNF168 as indicated. F.S represents fragment spectrum of GST-RNF168
Mol. Cells 2018;41:799~807 https://doi.org/10.14348/molcells.2018.0078
© Mol. Cells