Curcumin inhibits FtsZ assembly: an attractive mechanism for its antibacterial activity
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Title |
Curcumin inhibits FtsZ assembly: an attractive mechanism for its antibacterial activity
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Creator |
RAI, D
SINGH, JK ROY, N PANDA, D |
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Subject |
division protein ftsz
cell-division bacterial cytokinesis targeting ftsz small-molecule gtp degradation stability discovery products antibacterial activity curcumin filamentation ftsz polymerization gtpase activity z-ring |
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Description |
The assembly and stability of FtsZ protofilaments have been shown to play critical roles in bacterial cytokinesis. Recent evidence suggests that FtsZ may be considered as an important antibacterial drug target. Curcumin, a dietary polyphenolic compound, has been shown to have a potent antibacterial activity against a number of pathogenic bacteria including Staphylococcus aureus, Staphylococcus epidermidis and Enterococcus. We found that curcumin induced filamentation in the Bacillus subtilis 168, suggesting that it inhibits bacterial cytokinesis. Further, curcumin strongly inhibited the formation of the cytokinetic Z-ring in B. subtilis 168 without detectably affecting the segregation and organization of the nucleoids. Since the assembly dynamics of FtsZ protofilaments plays a major role in the formation and functioning of the Z-ring, we analysed the effects of curcumin on the assembly of FtsZ protofilaments. Curcumin inhibited the assembly of FtsZ protofilaments and also increased the GTPase activity of FtsZ. Electron microscopic analysis showed that curcumin reduced the bundling of FtsZ protofilaments in vitro. Further, curcumin was found to bind to FtsZ in vitro with a dissociation constant of 7.3 +/- 1.8 mu M and the agent also perturbed the secondary structure of FtsZ. The results indicate that the perturbation of the GTPase activity of FtsZ assembly is lethal to bacteria and suggest that curcumin inhibits bacterial cell proliferation by inhibiting the assembly dynamics of FtsZ in the Z-ring.
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Publisher |
PORTLAND PRESS LTD
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Date |
2011-08-27T06:55:31Z
2011-12-26T12:57:47Z 2011-12-27T05:45:14Z 2011-08-27T06:55:31Z 2011-12-26T12:57:47Z 2011-12-27T05:45:14Z 2008 |
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Type |
Article
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Identifier |
BIOCHEMICAL JOURNAL, 410(), 147-155
0264-6021 http://dx.doi.org/10.1042/BJ20070891 http://dspace.library.iitb.ac.in/xmlui/handle/10054/11578 http://hdl.handle.net/10054/11578 |
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Language |
en
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