C‐ring requirement in flagellar type III secretion is bypassed by FlhDC upregulation

Abstract

The cytoplasmic C-ring of the flagellum consists of FliG, FliM and FliN and acts as an affinity cup to localize secretion substrates for protein translocation via the flagellar-specific type III secretion system. Random T-POP transposon mutagenesis was employed to screen for insertion mutants that allowed flagellar type III secretion in the absence of the C-ring using the flagellar type III secretion system-specific hook-beta-lactamase reporter (Lee and Hughes, 2006). Any condition resulting in at least a twofold increase in flhDC expression was sufficient to overcome the requirement for the C-ring and the ATPase complex FliHIJ in flagellar type III secretion. Insertions in known and unknown flagellar regulatory loci were isolated as well as chromosomal duplications of the flhDC region. The twofold increased flhDC mRNA level coincided in a twofold increase in the number of hook-basal bodies per cell as analysed by fluorescent microscopy. These results indicate that the C-ring functions as a nonessential affinity cup-like structure during flagellar type III secretion to enhance the specificity and efficiency of the secretion process.