title: Recent advances in the structure and assembly of the archaeal flagellum.
abstract: Archaeal motility occurs through the rotation of flagella that are distinct from the flagella found on bacteria. The differences between the two structures include the multi-flagellin nature of the archaeal filament, the widespread posttranslational modification of the flagellins and the presence of a short signal peptide on each flagellin that is cleaved by a specific signal peptidase prior to the incorporation of the mature flagellin into the flagellar filament. Research has revealed similarities between the archaeal flagellum and the type IV pilus, including the presence of similar unusual signal peptides on the flagellins and pilins, similarities in the amino acid sequences of the major structural proteins themselves, as well as similarities between potential assembly and processing components. The recent suggestion that type IV pili are part of a family of cell surface complexes, coupled with the similarities between type IV pili and archaeal flagella, raise questions about the evolution of these systems and possible inclusion of archaeal flagella into this surface complex family.
authors.affiliation: Department of Microbiology and Immunology, Queen's University, Kingston, Ont, Canada.
authors.forename: Sonia L
authors.initials: SL
authors.lastname: Bardy
authors.forename: Sandy Y M
authors.initials: SY
authors.lastname: Ng
authors.forename: Ken F
authors.initials: KF
authors.lastname: Jarrell
mesh_terms: D001105:Archaea / Q000235:genetics* / Q000648:ultrastructure*; D019843:Archaeal Proteins / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism; D005407:Flagella / Q000235:genetics* / Q000648:ultrastructure*; D017017:Methanococcus / Q000235:genetics / Q000648:ultrastructure; D008954:Models, Biological; D005810:Multigene Family
chemical_list: D019843:Archaeal Proteins; D010450:Endopeptidases; C432693:preflagellin peptidase