Please use this identifier to cite or link to this item: https://doi.org/10.1021/bi7018546
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dc.titleBerberine targets assembly of Escherichia coli cell division protein FtsZ
dc.contributor.authorDomadia, P.N.
dc.contributor.authorBhunia, A.
dc.contributor.authorSivaraman, J.
dc.contributor.authorSwarup, S.
dc.contributor.authorDasgupta, D.
dc.date.accessioned2014-10-27T08:22:44Z
dc.date.available2014-10-27T08:22:44Z
dc.date.issued2008-03-11
dc.identifier.citationDomadia, P.N., Bhunia, A., Sivaraman, J., Swarup, S., Dasgupta, D. (2008-03-11). Berberine targets assembly of Escherichia coli cell division protein FtsZ. Biochemistry 47 (10) : 3225-3234. ScholarBank@NUS Repository. https://doi.org/10.1021/bi7018546
dc.identifier.issn00062960
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/100160
dc.description.abstractThe ever increasing problem of antibiotic resistance necessitates a search for new drug molecules that would target novel proteins in the prokaryotic system. FtsZ is one such target protein involved in the bacterial cell division machinery. In this study, we have shown that berberine, a natural plant alkaloid, targets Escherichia coli FtsZ, inhibits the assembly kinetics of the Z-ring, and perturbs cytokinesis. It also destabilizes FtsZ protofilaments and inhibits the FtsZ GTPase activity. Saturation transfer difference NMR spectroscopy of the FtsZ-berberine complex revealed that the dimethoxy groups, isoquinoline nucleus, and benzodioxolo ring of berberine are intimately involved in the interaction with FtsZ. Berberine perturbs the Z-ring morphology by disturbing its typical midcell localization and reduces the frequency of Z-rings per unit cell length to half. Berberine binds FtsZ with high affinity (K D ∼ 0.023 μM) and displaces bis-ANS, suggesting that it may bind FtsZ in a hydrophobic pocket. Isothermal titration calorimetry suggests that the FtsZ-berberine interaction occurs spontaneously and is enthalpy/entropy-driven. In silico molecular modeling suggests that the rearrangement of the side chains of the hydrophobic residues in the GTP binding pocket may facilitate the binding of the berberine to FtsZ and lead to inhibition of the association between FtsZ monomers. Together, these results clearly indicate the inhibitory role of berberine on the assembly function of FtsZ, establishing it as a novel FtsZ inhibitor that halts the first stage in bacterial cell division. © 2008 American Chemical Society.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1021/bi7018546
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1021/bi7018546
dc.description.sourcetitleBiochemistry
dc.description.volume47
dc.description.issue10
dc.description.page3225-3234
dc.description.codenBICHA
dc.identifier.isiut000253726900016
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