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. 2013 Aug 6;288(38):27031–27041. doi: 10.1074/jbc.M113.499772

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© 2013 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 4. — TssK1 interacts with T6SS phage-like complex components. TssK1 co-immunoprecipitates with TssA1 (A), TssC1 (B), and Hcp1 (C). Soluble lysates from 10¹¹ E. coli K12 W3110 cells producing HA-tagged TssK1 (TssK1_HA) and FLAG-tagged TssA1 (TssA1_FL, A), TssC1 (TssC1_FL, B), or Hcp1 (Hcp1_FL, C) proteins were subjected to immunoprecipitation with anti-FLAG-coupled beads. The total soluble (Tot) and the immunoprecipitated (IP) material were separated by 12.5% acrylamide SDS-PAGE and immunodetected with anti-HA (TssK1_HA, lower panel) and anti-FLAG (TssA1_FL, TssC1_FL, and Hcp1_FL, upper panel) monoclonal antibodies. Molecular weight markers (in kDa) are indicated on the left. D, surface plasmon resonance analysis of the TssK1-Hcp1 complex. The Hcp1 was immobilized on HC200m chip and SPR sensorgrams (variation of plasmon resonance in arbitrary unit (ΔRU) as a function of reaction time (in seconds)) were recorded upon passage of the indicated concentrations of TssK1 (TssK) (left panel). The graph reporting ΔRU as a function of TssK1 (TssK) concentration (right panel) was used to estimate the dissociation constant of the TssK1-Hcp1 complex (26.5 ± 2.3 μm).