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Sodium‐dependent dynamic assembly of membrane complexes in sodium‐driven flagellar motors
Author(s) -
Fukuoka Hajime,
Wada Tomoyuki,
Kojima Seiji,
Ishijima Akihiko,
Homma Michio
Publication year - 2009
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2008.06569.x
Subject(s) - stator , biophysics , flagellum , vibrio alginolyticus , rotor (electric) , motility , membrane , biology , physics , biochemistry , vibrio , microbiology and biotechnology , bacteria , genetics , quantum mechanics , gene
Summary The bacterial flagellar motor is driven by the electrochemical potential of specific ions, H + or Na + . The motor consists of a rotor and stator, and their interaction generates rotation. The stator, which is composed of PomA and PomB in the Na + motor of Vibrio alginolyticus , is thought to be a torque generator converting the energy of ion flux into mechanical power. We found that specific mutations in PomB, including D24N, F33C and S248F, which caused motility defects, affected the assembly of stator complexes into the polar flagellar motor using green fluorescent protein‐fused stator proteins. D24 of PomB is the predicted Na + ‐binding site. Furthermore, we demonstrated that the coupling ion, Na + , is required for stator assembly and that phenamil (an inhibitor of the Na + ‐driven motor) inhibited the assembly. Carbonyl cyanide m ‐chlorophenylhydrazone, which is a proton ionophore that collapses the sodium motive force in this organism at neutral pH, also inhibited the assembly. Thus we conclude that the process of Na + influx through the channel, including Na + binding, is essential for the assembly of the stator complex to the flagellar motor as well as for torque generation.