Rotational Fluctuation of the Sodium-driven Flagellar Motor of Induced by Binding of Inhibitors

Muramoto, Kazumasa; Magariyama, Yukio; Homma, Michio; Kawagishi, Ikuro; Sugiyama, Shigeru; Imae, Yasuo; Kudo, Satoshi

doi:10.1006/jmbi.1996.0350

Cited by 16 publications

(29 citation statements)

References 33 publications

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“…When the rotation rate was reduced by decreasing external concentration of NaCl or adding amiloride or carbonylcyanide mchlorophenylhydrazone (CCCP), the motor rotated smoothly. On the other hand, we found that the polar flagella showed remarkably larger speed fluctuations when the rotation rate was reduced by phenamil (Muramoto et al, 1996). The speed fluctuations induced by phenamil can be explained by the slow dissociation rate of the inhibitor from the force-generating unit.…”

Section: Introductionmentioning

confidence: 75%

“…This difference between the two species might reflect differences in the mutations or in the Na + binding regions. It has been observed that the motor rotation rate fluctuates in the presence of phenamil but not amiloride or CCCP (Muramoto et al, 1996) and it was suggested that this phenomenon is due to the longer duration of phenamil binding to the motor. If there are several force-generating units in one motor and each unit functions independently, then the number of functional units is proportional to the rotation rate and changes in this number cause the fluctuations of rotation rate.…”

Section: Discussionmentioning

confidence: 99%

“…It has been shown that the rotation rate becomes very unstable in the presence of phenamil but not in the presence of amiloride or CCCP, even when the inhibitors are used at concentrations that reduce the rotation rate by the same amount (Muramoto et al, 1996). We investigated the stability of Mpa r flagellar rotation at 50 mM NaCl in the presence of phenamil and amiloride.…”

Section: Fluctuation Of the Rotation Rate In The Phenamil-resistant Mmentioning

confidence: 99%

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Vibrio alginolyticus mutants resistant to phenamil, a specific inhibitor of the sodium-driven flagellar motor

Kojima

Atsumi

Muramoto

et al. 1997

Journal of Molecular Biology

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Section: Introductionmentioning

confidence: 75%

Section: Discussionmentioning

confidence: 99%

Section: Fluctuation Of the Rotation Rate In The Phenamil-resistant Mmentioning

confidence: 99%

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Vibrio alginolyticus mutants resistant to phenamil, a specific inhibitor of the sodium-driven flagellar motor

Kojima

Atsumi

Muramoto

et al. 1997

Journal of Molecular Biology

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“…The independent force-generating unit probably functions as described above in the Na ϩ -driven motor of V. alginolyticus. We plan to analyze the rotation speed at low numbers of the force-generating units by laser dark-field microscopy (38) and to investigate the stability or the stepping of the speed.…”

Section: Vol 179 1997 Genes Of Sodium-driven Flagellar Motor 5107mentioning

confidence: 99%

“…When the rotation rate is reduced by amiloride, the motor still rotates smoothly though the rotation rate tends to fluctuate. On the other hand, polar flagella showed remarkably larger speed fluctuations upon addition of phenamil, an amiloride analog (38). The speed fluctuations induced by phenamil were explained by a low rate of dissociation of the inhibitor from the force-generating unit.…”

mentioning

confidence: 95%

Putative channel components for the fast-rotating sodium-driven flagellar motor of a marine bacterium

et al. 1997

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The polar flagellum of Vibrio alginolyticus rotates remarkably fast (up to 1,700 revolutions per second) by using a motor driven by sodium ions. Two genes, motX and motY, for the sodium-driven flagellar motor have been identified in marine bacteria, Vibrio parahaemolyticus and V. alginolyticus. They have no similarity to the genes for proton-driven motors, motA and motB, whose products constitute a proton channel. MotX was proposed to be a component of a sodium channel. Here we identified additional sodium motor genes, pomA and pomB, in V. alginolyticus. Unexpectedly, PomA and PomB have similarities to MotA and MotB, respectively, especially in the predicted transmembrane regions. These results suggest that PomA and PomB may be sodium-conducting channel components of the sodium-driven motor and that the motor part consists of the products of at least four genes, pomA, pomB, motX, and motY. Furthermore, swimming speed was controlled by the expression level of the pomA gene, suggesting that newly synthesized PomA proteins, which are components of a force-generating unit, were successively integrated into the defective motor complexes. These findings imply that Na ؉ -driven flagellar motors may have similar structure and function as proton-driven motors, but with some interesting differences as well, and it is possible to compare and study the coupling mechanisms of the sodium and proton ion flux for the force generation.

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Evaluating the feasibility of utilizing the small molecule phenamil as a novel biofactor for bone regenerative engineering

Ulery

Kan

et al. 2012

J Tissue Eng Regen Med

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Osteoblast cell adhesion and differentiation on biomaterials are important achievements necessary for implants to be useful in bone regenerative engineering. Recombinant bone morphogenetic proteins (BMPs) have been shown to be important for these processes; however, there are many challenges associated with the widespread use of these proteins. A recent report demonstrated that the small molecule phenamil, a diuretic derivative, was able to induce osteoblast differentiation and mineralization in vitro via the canonical BMP signalling cascade (Park et al., 2009). In this study, the feasibility of using phenamil as a novel biofactor in conjunction with a biodegradable poly(lactide-co-glycolide acid) (PLAGA) polymeric scaffold for engineering bone tissue was evaluated. The in vitro cellular behaviour of osteoblast-like MC3T3-E1 cells cultured on PLAGA scaffolds in the presence of phenamil at 10 μM were characterized with regard to initial cell adhesion, proliferation, alkaline phosphatase (ALP) activity and matrix mineralization. The results demonstrate that phenamil supported cell proliferation, promoted ALP activity and facilitated matrix mineralization of osteoblast-like MC3T3-E1 cells. Moreover, in this study, we found that phenamil promoted integrin-mediated cell adhesion on PLAGA scaffolds. It was also shown that phenamil encapsulated within porous, microsphere PLAGA scaffolds retained its osteogenic activity upon release. Based on these findings, the small molecule phenamil has the potential to serve as a novel biofactor for the repair and regeneration of bone tissues.

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Rotational Fluctuation of the Sodium-driven Flagellar Motor of Induced by Binding of Inhibitors

Cited by 16 publications

References 33 publications

Vibrio alginolyticus mutants resistant to phenamil, a specific inhibitor of the sodium-driven flagellar motor

Vibrio alginolyticus mutants resistant to phenamil, a specific inhibitor of the sodium-driven flagellar motor

Putative channel components for the fast-rotating sodium-driven flagellar motor of a marine bacterium

Evaluating the feasibility of utilizing the small molecule phenamil as a novel biofactor for bone regenerative engineering

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