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Interaction of the disordered terminal regions of flagellin upon flagellar filament formation
Author(s) -
Gugolya Zoltán,
Muskotál Adél,
Sebestyén Anett,
Diószeghy Zoltán,
Vonderviszt Ferenc
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03859-0
Subject(s) - flagellin , protein filament , flagellum , terminal (telecommunication) , biophysics , crystallography , polymerization , chemistry , biology , biochemistry , polymer , receptor , telecommunications , organic chemistry , computer science , gene
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 α‐helical N‐ and C‐terminal regions of axially adjacent subunits form an interlocking pattern of helical bundles upon polymerization.