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. 2016 Jun 14;12(6):e1005660. doi: 10.1371/journal.ppat.1005660

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© 2016 Berneking et al

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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Fig 1 — A) Coprecipitation of bacterially translocated YopM-SBP-CBP with DDX3, RSK1 and PKN in J774A.1 cells. J774A.1 cells were infected with WA314ΔYopM(pYopM-SBP-CBP), WA314ΔYopM(pYopM) or WA314ΔYopE(pYopE-SBP-CBP). Proteins eluting consecutively from streptavidin-sepharose (biotin elution) and calmodulin-sepharose (boiling in sample buffer) were analyzed by Western blot using indicated antibodies. B) GST-YopM pull-down of endogenous DDX3. GST-myc-YopM or GST expressed in HEK293T cells were precipitated with glutathione sepharose beads and analyzed by Western blot using indicated antibodies. C) Myc-YopM co-immunoprecipitates with endogenous DDX3. Endogenous DDX3 was immunoprecipitated in HEK293T cells expressing myc-YopM. Precipitates and whole cell lysates (WCL) were analyzed by Western blot using indicated antibodies. D) Bacterially translocated YopM co-immunoprecipitates with endogenous DDX3. Endogenous DDX3 was immunoprecipitated in HEK293T cells infected with WA314ΔYopM(pYopM) or WA314ΔYopM for 90 min. Precipitates and whole cell lysates (WCL) were analyzed by Western blot using indicated antibodies. E) DDX3 and PKN mutually exclude each other in RSK1/YopM containing complexes. HEK293T cells expressing either DDX3-FLAG (left panel) or PKN-FLAG (right panel) and where indicated myc-YopM were lysed and subjected to anti-FLAG immunoprecipitation. Precipitates and whole cell lysates (WCL) were analyzed by Western blot using indicated antibodies. In DDX3-FLAG immunoprecipitates, myc-YopM, RSK1 but no PKN and in PKN-FLAG immunoprecipitates myc-YopM, RSK1 but no DDX3 were detected.