Soluble components of the flagellar export apparatus,FliI, FliJ,and FliH,do not deliver flagellin,the major filament protein,from the cytosol to the export gate |
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| Authors: | Rá chel Sajó ,Ká roly Liliom,Adé l Muskotá l,Á gnes Klein,Pé ter Zá vodszky,Ferenc Vonderviszt,Jó zsef Dobó |
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| Affiliation: | 1. Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Magyar Tudósok krt. 2, H-1117 Budapest, Hungary;2. Bio-Nanosystems Laboratory, Faculty of Information Technology, University of Pannonia, Egyetem u. 10, H-8200 Veszprém, Hungary |
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| Abstract: | Flagella, the locomotion organelles of bacteria, extend from the cytoplasm to the cell exterior. External flagellar proteins are synthesized in the cytoplasm and exported by the flagellar type III secretion system. Soluble components of the flagellar export apparatus, FliI, FliH, and FliJ, have been implicated to carry late export substrates in complex with their cognate chaperones from the cytoplasm to the export gate. The importance of the soluble components in the delivery of the three minor late substrates FlgK, FlgL (hook–filament junction) and FliD (filament-cap) has been convincingly demonstrated, but their role in the transport of the major filament component flagellin (FliC) is still unclear. |
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| Keywords: | FliI, a soluble ATPase component of the flagellar export apparatus FliH and FliJ, soluble regulatory components of the export apparatus FliC, flagellin, the major filament protein FliS, chaperone for FliC T3SS, type III secretion system FlhA FlhB, FliO, FliP, FliQ and FliR, membrane components of the flagellar export apparatus FlgK and FlgL, hook&ndash filament junction proteins FlgN, chaperone for FlgK and FlgL FliD, filament-cap protein FliT, chaperone for FliD FliN, a C-ring protein |
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