Genetic analysis of revertants isolated from the rod-fragile <i>fliF</i> mutant of <i>Salmonella</i>

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    • Hayashi Fumio
    • Division of Molecular Science, Faculty of Science and Technology, Gunma University
    • Namba Keiichi
    • Protonic NanoMachine Project, ERATO, JST|Graduate School of Frontier Biosciences, Osaka University
    • Oosawa Kenji
    • Protonic NanoMachine Project, ERATO, JST|Division of Molecular Science, Faculty of Science and Technology, Gunma University|Department of Biosciences, Teikyo University


FliF is the protein comprising the MS-ring of the bacterial flagellar basal body, which is the base for the assembly of flagellar axial structures. From a <i>fliF</i> mutant that easily releases the rod-hook-filament in viscous environments, more than 400 revertants that recovered their swarming ability in viscous conditions, were isolated. The second-site mutations were determined for approximately 70% of them. There were three regions where the mutations were localized: two in Region I, 112 in Region II, and 71 in Region III including the true reversion. In Region I, second-site mutations were found in FlgC and FlgF of the proximal rod, suggesting that they affect the interaction between the MS-ring and the rod. In Region II, there were 69 and 42 mutations in MotA and MotB, respectively, suggesting that the second-site mutations in MotA and MotB may decrease the rotational speed of the flagellar motor to reduce the probability of releasing the rod under this condition. One exception is a mutation in FlhC that caused a down regulation of the flagellar proteins production but it may directly affect transcription or translation of <i>motA</i> and <i>motB</i>. In Region III, there were 44, 24, and 3 mutations in FliG, FliM, and FliF, respectively. There were no second-site mutations identified in FliN although it is involved in torque generation as a component of the C-ring. Many of the mutations were involved in the motor rotation, and it is suggested that such reduced speeds result in stabilizing the filament attachment to the motor.


  • Biophysics and Physicobiology

    Biophysics and Physicobiology 13(0), 13-25, 2016

    The Biophysical Society of Japan


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