Interaction of the disordered terminal regions of flagellin upon flagellar filament formation.
Helical filaments of bacterial flagella are built up by a self-assembly process from thousands of flagellin subunits. To clarify how the disordered terminal regions of flagellin interact upon filament formation, polymerization ability of various terminally truncated fragments was investigated. Fragments deprived of 19 N-terminal residues were able to bind to the end of filaments, however, only a single layer was formed. Removal of C-terminal segments or truncation at both ends resulted in the complete loss of binding ability. Our observations are consistent with the coiled-coil model of filament formation, which suggests that the alpha-helical N- and C-terminal regions of axially adjacent subunits form an interlocking pattern of helical bundles upon polymerization.
Gugolya
Zoltán
Z
Department of Physics, University of Veszprém, Egyetem u. 10, H-8200 Veszprém, Hungary.
Muskotál
Adél
A
Sebestyén
Anett
A
Diószeghy
Zoltán
Z
Vonderviszt
Ferenc
F
D001426:Bacterial Proteins / Q000737:chemistry*; D005407:Flagella / Q000737:chemistry*; D005408:Flagellin / Q000737:chemistry*; D031541:Fluorescence Resonance Energy Transfer; D005456:Fluorescent Dyes / Q000737:chemistry; D021122:Protein Subunits / Q000737:chemistry; D012475:Salmonella; D013050:Spectrometry, Fluorescence
D001426:Bacterial Proteins; D005456:Fluorescent Dyes; D021122:Protein Subunits; D005408:Flagellin