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FEBS Lett. 2006 Jul 10;580(16):3916-20. Epub 2006 Jun 21.

Interaction of FliS flagellar chaperone with flagellin.

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  • 1Department of Nanotechnology, Faculty of Information Technology, Pannon University, Egyetem u. 10, H-8200 Veszprém, Hungary.


Premature polymerization of flagellin (FliC), the main component of flagellar filaments, is prevented by the FliS chaperone in the cytosol. Interaction of FliS with flagellin was characterized by isothermal titration calorimetry producing an association constant of 1.9x10(7) M-1 and a binding stoichiometry of 1:1. Experiments with truncated FliC fragments demonstrated that the C-terminal disordered region of flagellin is essential for FliS binding. As revealed by thermal unfolding experiments, FliS does not function as an antifolding factor keeping flagellin in a secretion-competent conformation. Instead, FliS binding facilitates the formation of alpha-helical secondary structure in the chaperone binding region of flagellin.

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