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. 2014 Oct 30;94(5):1179–1195. doi: 10.1111/mmi.12826

Figure 5.

Figure 5

Verification by immunoblotting of Vipp1 interaction partners in Synechocystis identified by mass spectrometry.A. Immunoblots on fractions isolated from HL-treated wild-type, vipp1–gfp and futA1–gfp cells, showing that DnaK2, DnaK3 and EF-G (but not Slr1768) are retained in the GFP affinity-bound fraction specifically in vipp1–gfp cells. Spaces shown between the lanes on the blots for DnaK3, EF-G and Slr1768 indicate combination of data from different places on the blot, but all data are from the same blots. Sample dilutions (100%, 10%, and 1%) for unfractionated (whole extract) Synechocystis vipp1–gfp are shown for comparison. The first (post) elution is the fraction washed through the column, whereas the final elution is the fraction retained by GFP-affinity binding.B. Immunoblots showing that the Ycf48 and D1 proteins are affinity-bound in HL vipp1–gfp cells, but not wild-type or futA1–gfp. Spaces shown between the lanes on the blots for D1 and Ycf48 indicate combination of data from different places on the blot, but all data are from the same blots.C. DnaK2, DnaK3, Ycf48 and D1 are not affinity-bound in LL vipp1–gfp cells (in contrast to HL vipp1–gfp cells, see A, B).