Journal
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
Volume 83, Issue 7, Pages 1362-1371Publisher
OXFORD UNIV PRESS
DOI: 10.1080/09168451.2019.1597618
Keywords
Motility; flagellum; propionate-oxidizing bacteria; MotB-like protein; proton-driven type
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Funding
- Japan Society for the Promotion of Science [KAKENHI 16K07666]
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The basic functions of a propionate-oxidizing bacterium Pelotomaculum thermopropionicum flagellum, such as motility and chemotaxis, have not been studied. To investigate its motility, we compared with that of Syntrophobacter fumaroxidans, an aflagellar propionate-oxidizing bacterium, in soft agar medium. P. thermopropionicum cells spread, while S. fumaroxidans cells moved downward slightly, indicating flagellum-dependent motility in P. thermopropionicum SI. The motility of P. thermopropionicum was inhibited by the addition of carbonyl cyanide m-chlorophenyl hydrazone, a proton uncoupler, which is consistent with the fact that stator protein, MotB of P. thermopropionicum, shared sequence homology with proton-type stators. In addition, 5-N-ethyl-N-isopropyl amiloride, an Na+ channel blocker, showed no inhibitory effect on the motility. Furthermore, motAB of P. thermopropionicum complemented the defective swimming ability of Escherichia coli increment Delta motAB. These results suggest that the motility of P. thermopropionicum SI depends on the proton-type flagellar motor.
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