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. Author manuscript; available in PMC: 2008 Sep 3.
Published in final edited form as: Mol Microbiol. 2001 Feb;39(3):781–791. doi: 10.1046/j.1365-2958.2001.02268.x

Fig. 5.

Fig. 5

Complementation of flgN and fliT mutants by chaperone C-terminal regions.

A. Representations of (top) FliT and FlgN indicating putative N-terminal dimerization (shaded) and C-terminal substrate-binding (hatched) domains; (middle) the FlgN and FliT N-terminally histidine-tagged (H6) polypeptides; and (bottom) GST translational fusions. The C-terminal amphipathic helix is predicted to span amino acids 74–114 in FlgN and residues 60–98 in FliT. The predicted FlgN leucine zipper is located between residues 1 and 30.

B. Flagellar proteins collected from the supernatants of late exponential phase flgN (left) or fliT (right) mutant cultures alone (–) or expressing either His-tagged FlgN or FliT (labelled N and T) or the respective GST fusion or the C-terminal polypeptide. The same proteins exported by WT S. typhimurium are shown in each case in the leftmost columns. Proteins separated by SDS–(12%)PAGE were immunoblotted with anti-FlgK, anti-FlgL, anti-FliD or anti-FlgM antisera or by Coomassie blue staining (FliC).