FIGURE 5 | Model of the assembly of cell appendices in the cell envelope of Sulfolobus solfataricus.

From the following article:

Protein secretion in the Archaea: multiple paths towards a unique cell surface

Sonja-Verena Albers, Zalán Szabó & Arnold J. M. Driessen

Nature Reviews Microbiology 4, 537-547 (July 2006)

doi:10.1038/nrmicro1440

Protein secretion in the Archaea: multiple paths towards a unique cell surface

The translocated precursor of substrate-binding proteins and flagellins are membrane-associated through their N-terminal hydrophobic anchor sequence that is stabilized by a positively charged N-terminal tail, which is exposed to the cytosolic face of the membrane. The positively charged N-terminal tail is removed by PibD, which allows the dislocation of the flagellin or substrate-binding protein from the cytoplasmic membrane and subsequent assembly into a macromolecular structure. The hydrophobic N terminus functions as a scaffold for the assembly of the flagellin subunits into a flagellum that grows from its base. Assembly is mediated by the FlaHIJ proteins and requires the binding and hydrolysis of ATP. Processed substrate-binding proteins are assembled according to a similar mechanism into a macromolecular extracellular structure called the bindosome. The bindosome either corresponds to a pilus-like or an S-layer associated structure, but its exact structure is unknown.

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