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. 2017 Apr 3;13(4):e1006304. doi: 10.1371/journal.ppat.1006304

Fig 7. DSF stimulation changes the DHp-CA interface of RpfC.

Fig 7

(A and B) Limited proteolysis of RpfCFL liposomes. SDS-PAGE and molecular weight analyses of samples revealed DSF-dependent changes in trypsinolysis patterns, as indicated by asterisks. (A) Limited proteolysis of RpfCFL liposome. (B) Limited proteolysis of RpfCQ22A liposome. Limited proteolysis of other substitutions was shown in S5 Fig. (C) Replacement of essential residue affects RpfCFL autokinase activity. Autokinase activities of RpfC liposomes containing corresponding amino acid replacement were measured by in vitro phosphorylation assay. DSF was added to reactions at 0.75 μM. Each lane contained 1.4 μg liposome phosphorylated by 100 μM ATP, including 10 μCi [γ-32P]-ATP, for 5 min. Experiments were independently repeated three times, and a representative experiment is shown.