Figure 4
From: Interactions between flagellar and type III secretion proteins in Chlamydia pneumoniae
Interaction of His-CPn0859 and GST-Cpn0859, and dimerization of His-Cpn0859. A: Full length GST-Cpn0859 was bound to glutathione beads and was used to pull down full length His-Cpn0859 from an E. coli lysate, as seen in Figure 3. GST-Cpn0859 co-purified with His-Cpn0859. GST alone did no co-purify with His-Cpn0859, and GST-Cpn0859 is shown as a loading control. B: Full length His-Cpn0859 was fixed with formaldehyde for 10 minutes prior to being electrophoresed on an 11% PAGE gel and probed for by anti-His Western blot. Cpn0859 monomers can be seen migrating at approximately 22 kDa while the formation of a dimer can be seen migrating at approximately 44 kDa. C: Full length GST-FliI, GST-FliI1-400, or GST-FliI150-470 were bound to glutathione beads and were used to pull down His-Cpn0859 from an E. coli lysate. They were washed in the same manner as above, and only full length GST-FliI and GST-FliI1-400 were able to co-purify with His-Cpn0859. D: Full length GST-Cpn0859 was bound to glutathione beads and was used to pull down either His-FlhA308-583, His-FliF35-341 or His-FliF1-271 from an E. coli lysate. GST-Cpn0859 co-purified with His- FlhA308-583, but not His-FliF35-341 or His-FliF1-271 while GST alone did no co-purify with either.