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Limited proteolysis of WRN exonuclease defines domain boundaries. A, Coomassie-stained 12% SDS-PAGE gel of limited proteolysis of WRN(1–333) purified from E. coli with either chymotrypsin (C) or trypsin (T) and incubated for the noted times. B, three purified recombinant WRN nuclease constructs were produced and are shown (gel inset); construct size and position relative to full-length WRN and the RecQ and Helicase and RNase-D C-terminal (HRDC) domains are schematically illustrated.
