Archaea use a unique structure for swimming motility which is not hoomologous to bacterial flagella, but instead resembles type IV pili. But in contrast to type IV pili, motion is not achieved by elongation and disassembly of the filament, but by rotation.
The smallest known archaellum operon is present in Sulfolobus acidocaldarius. Therefore we used the S. acidoalcarius archaellum as a model system to understand which role the different proteins play during assembly and rotation of the archaellum. To that end we use biochemical, genetic and structural approaches.
So far we have reported the structures of FlaI, FlaH and FlaF (follow the links to the publications). These structural analyses were done in a successful collaboration with the lab of John Tainer .
The image shows the graphical abstract of our recent paper about FlaH in Molecular Microbiology (Chaudhury et al, 2016). Although FlaH is not an active ATPase, nucleotide binding is essential for its interaction with FlaH and therefore archaellum assembly.
This work was funded from 2013- 2018 by an starting ERC grant. At the moment the work is continuing within the FEt Open grant MARA.