The FliS chaperone selectively binds the disordered flagellin C-terminal D0 domain central to polymerisation.
Assembly of each Salmonella typhimurium flagellum filament requires export and polymerisation of ca. 30000 flagellin (FliC) subunits. This is facilitated by the cytosolic chaperone FliS, which binds to the 494 residue FliC and inhibits its polymerisation. Yeast two-hybrid assays, co-purification and affinity blotting showed that FliS binds specifically to the C-terminal 40 amino acid component of the disordered D0 domain central to polymerisation. Without FliS binding, the C-terminus is degraded. Our data provide further support for the view that FliS is a domain-specific bodyguard preventing premature monomer interaction.
Ozin
Amanda J
AJ
Cambridge University Department of Pathology, Tennis Court Road, CB2 1QP, Cambridge, UK.
Claret
Laurent
L
Auvray
Frederic
F
Hughes
Colin
C
D001426:Bacterial Proteins / Q000378:metabolism*; D001704:Biopolymers / Q000737:chemistry / Q000378:metabolism; D005408:Flagellin / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000378:metabolism*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D012486:Salmonella typhimurium / Q000166:cytology / Q000235:genetics / Q000378:metabolism*; D012680:Sensitivity and Specificity
D001426:Bacterial Proteins; D001704:Biopolymers; D018832:Molecular Chaperones; D005408:Flagellin; C076734:FliS protein, Bacteria