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The archaellum, the rotating motility structure of archaea, is best studied in the crenarchaeon   Sulfolobus acidocaldarius . To better understand how assembly and rotation of this structure is driven, two ATP-binding proteins, FlaI and FlaH of the motor complex of the archaellum of the euryarchaeon   Pyrococcus furiosus , were overexpressed, purified and studied. Contrary to the FlaI ATPase of   S. acidocaldarius , which only forms a hexamer after binding of nucleotides, FlaI of  P. furiosus  formed a hexamer in a nucleotide independent manner. In this hexamer only 2 of the ATP binding sites were available for binding of the fluorescent ATP-analog MANT-ATP, suggesting a twofold symmetry in the hexamer.  P. furiosus  FlaI showed a 250-fold higher ATPase activity than   S. acidocaldarius  FlaI. Interaction studies between the isolated N- and C-terminal domains of FlaI showed interactions between the N- and C-terminal domains and strong interactions between the N-terminal domains not previously observed for ATPases involved in archaellum assembly. These interactions played a role in oligomerization and activity, suggesting a conformational state of the hexamer not observed before. Further interaction studies show that the C-terminal domain of   Pf FlaI interacts with the nucleotide binding protein FlaH. This interaction stimulates the ATPase activity of FlaI optimally at a 1:1 stoichiometry, suggesting that hexameric  Pf FlaI interacts with hexameric  Pf FlaH. These data help to further understand the complex interactions that are required to energize the archaellar motor.

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Characterization of the ATPase FlaI of the motor complex of the<i>Pyrococcus furiosus</i>archaellum and its interactions between the ATP-binding protein FlaH

Characterization of the ATPase FlaI of the motor complex of thePyrococcus furiosusarchaellum and its interactions between the ATP-binding protein FlaH