Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Gugolya Z,Muskotál A,Sebestyén A,Diószeghy Z,Vonderviszt Fdoi
10.1016/s0014-5793(02)03859-0keywords:
subject
Has Abstractpub_date
2003-01-30 00:00:00pages
66-70issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579302038590journal_volume
535pub_type
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