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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

ECs2665  -  flagellar biosynthesis protein FliT

Escherichia coli O157:H7 str. Sakai

 
 
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Disease relevance of ECs2665

  • Nevertheless, stable unique complexes were assembled efficiently in vitro by co-incubation of FlgN and FliT with target HAPs purified from recombinant Escherichia coli [1].
 

High impact information on ECs2665

  • The flagellar proteins FlgN and FliT have been proposed to act as substrate-specific export chaperones, facilitating incorporation of the enterobacterial hook-associated axial proteins (HAPs) FlgK/FlgL and FliD into the growing flagellum [1].
  • Gel filtration chromatography of wild-type S. typhimurium cell extracts identified stable pools of FlgN and FliT homodimers in the cytosol, but no chaperone-substrate complexes were evident [1].
 

Anatomical context of ECs2665

  • Substrate-specific binding of hook-associated proteins by FlgN and FliT, putative chaperones for flagellum assembly [2].

References

  1. Substrate complexes and domain organization of the Salmonella flagellar export chaperones FlgN and FliT. Bennett, J.C., Thomas, J., Fraser, G.M., Hughes, C. Mol. Microbiol. (2001) [Pubmed]
  2. Substrate-specific binding of hook-associated proteins by FlgN and FliT, putative chaperones for flagellum assembly. Fraser, G.M., Bennett, J.C., Hughes, C. Mol. Microbiol. (1999) [Pubmed]
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