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Journal of Bacteriology, October 2009, p. 6186-6191, Vol. 191, No. 19
0021-9193/09/$08.00+0 doi:10.1128/JB.00601-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Department of Life Sciences, Prefectural University of Hiroshima, 562 Nanatsuka, Shobara, Hiroshima 727-0023, Japan,1 Department of Chemistry and Biochemistry, Kennesaw State University, 1000 Chastain Rd., MB 1203, Kennesaw, Georgia 301442
Received 8 May 2009/ Accepted 19 July 2009
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.
Published ahead of print on 31 July 2009.
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