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Article
Flagellar Formation in C-Ring-Defective Mutants by Overproduction of FliI, the ATPase Specific for Flagellar Type III Secretion
Journal of Bacteriology
  • Manabu Konishi, Prefectural University of Hiroshima
  • Masaomi Kanbe, Prefectural University of Hiroshima
  • Jonathan L. McMurry, Kennesaw State University
  • Shin-Ichi Aizawa, Prefectural University of Hiroshima
Department
Chemistry & Biochemistry
Document Type
Article
Publication Date
10-1-2009
Disciplines
Abstract
The flagellar cytoplasmic ring (C ring), which consists of three proteins, FliG, FliM, and FliN, is located on the cytoplasmic side of the flagellum. The C ring is a multifunctional structure necessary for flagellar protein secretion, torque generation, and switching of the rotational direction of the motor. The deletion of any one of the fliG, fliM, and fliN genes results in a Fla - phenotype. Here, we show that the overproduction of the flagellum-specific ATPase FliI overcomes the inability of basal bodies with partial C-ring structures to produce complete flagella. Flagella made upon FliI overproduction were paralyzed, indicating that an intact C ring is essential for motor function. In FliN- or FliM-deficient mutants, flagellum production was about 10% of the wild-type level, while it was only a few percent in FliG-deficient mutants, suggesting that the size of partial C rings affects the extent of flagellation. For flagella made in C-ring mutants, the hook length varied considerably, with many being markedly shorter or longer than that of the wild type. The broad distribution of hook lengths suggests that defective C rings cannot control the hook length as tightly as the wild type even though FliK and FlhB are both intact.
Digital Object Identifier (DOI)
10.1128/JB.00601-09
Citation Information
Konishi M, Kanbe M, McMurry JL, Aizawa S. 2009. Flagellar formation in C-ring-defective mutants by overproduction of FliI, the ATPase specific for flagellar type III secretion. J Bacteriol 191(19):6186-91.