Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 321, Issue 3, Pages 383-395Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/S0022-2836(02)00616-2
Keywords
archaeabacteria; bacterial flagella; bacterial motility; cryoelectron-microscopy; extrernophiles
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Although the phenomenology and mechanics of swimming are very similar in eubacteria and archaeabacteria (e.g. reversible rotation, helical polymorphism of the filament and formation of bundles), the dynamic flagellar filaments seem completely unrelated in terms of morphogenesis, structure and amino acid composition. Archeabacterial flagellar filaments share important features with type IV pili, which are components of retractable linear motors involved in twitching motility and cell adhesion. The archeabacterial filament is unique. in: (1) having a relatively smooth surface and a small diameter of similar to 100 Angstrom as compared to similar to 240 Angstrom of eubacterial filaments and similar to 50 Angstrom of type IV pili; (2) being glycosylated and sulfated in a pattern similar to the S-layer; (3) being synthesized as preflagellin with a signal-peptide cleavable by membrane peptidases upon transport; and (4) having an N terminus highly hydrophobic and homologous with that of the olygomerization domain of pilin. The synthesis of archeabacterial flagellin monomers as pre-flagellin and their post-translational, extracellular glycosylation suggest a different mode of monomer transport and polymerization at the cell-proximal end of the filament, similar to pili rather than to eubacterial flagellar filaments. The polymerization mode and small diameter may indicate the absence of a central channel in the filament. Using low-electron-dose images of cryo-negative-stained filaments, we determined the unique symmetry of the flagellar filament of the extreme halophile Halobacterium salinarum strain R1M1 and calculated a three-dimensional density map to a resolution of 19 A. The map is based on layer-lines of order n = 0, + 10, - 7, + 3, - 4, + 6, and - 1. The cross-section of the density map has a triskelion shape and is dominated by seven outer densities clustered into three groups, which are connected by lower-density arms to a dense central core surrounded by a lower-density shell. There is no evidence for a central channel. On the basis of the homology with the oligomerization domain of type IV pilin and the density distribution of the filament map, we propose a structure for the central core. (C) 2002 Elsevier Science Ltd. All rights reserved
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