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. 2018 Jul 31;9(4):e01096-18. doi: 10.1128/mBio.01096-18

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Copyright © 2018 Charova et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license.

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FIG 2 — HrpG, HrpV, and HrpJ form the gatekeeper complex in P. syringae pv. phaseolicola and E. amylovora. (A and B) Successive elutions derived from affinity chromatography isolation of various E. coli-expressed complexes between the HrpG, HrpV, and HrpJ proteins from P. syringae pv. phaseolicola and E. amylovora analyzed by SDS-PAGE. His₆-tagged proteins are designated by HT. (C to F) SEC of HrpG/HrpV/HrpJ from P. syringae pv. phaseolicola and E. amylovora showing the ternary HrpG/HrpV/HrpJ complex coexisting with the HrpG/HrpV complex. The estimated molecular weights of the HrpG/HrpV/HrpJ and HrpG/HrpV complexes from P. syringae pv. phaseolicola are 72 kDa and 32 kDa, respectively, while in E. amylovora HrpG/HrpV/HrpJ elutes at 74 kDa and HrpG/HrpV elutes abnormally at 18 kDa. (G) nLC-MS/MS identification of full-length and cleaved forms of HrpJ from E. amylovora and P. syringae pv. phaseolicola. Due to solubility problems, HrpJ from P. syringae pv. phaseolicola was analyzed from the soluble HrpG/HrpV/HrpJ complex. The truncated versions of HrpJ are depicted with the symbols * and #, respectively, in panels A, B, and G.