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Volumn 46, Issue 14, 2007, Pages 4211-4220

Totarol inhibits bacterial cytokinesis by perturbing the assembly dynamics of FtsZ

Author keywords

[No Author keywords available]

Indexed keywords

BACILLUS SUBTILIS CELLS; BACTERIAL CYTOKINESIS; MYCOBACTERIUM TUBERCULOSIS; TOTAROL;

EID: 34147136107     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi602573e     Document Type: Article
Times cited : (122)

References (43)
  • 1
    • 1642430703 scopus 로고    scopus 로고
    • Microtubule-targeted anticancer agents and apoptosis
    • Bhalla, K. N. (2003) Microtubule-targeted anticancer agents and apoptosis, Oncogene 22, 9075-9086.
    • (2003) Oncogene , vol.22 , pp. 9075-9086
    • Bhalla, K.N.1
  • 2
    • 33645802798 scopus 로고    scopus 로고
    • Antimitotic agents of natural origin
    • Nagle, A., Hur, W., and Gray, N. S. (2006) Antimitotic agents of natural origin, Curr. Drug Targets 7, 305-326.
    • (2006) Curr. Drug Targets , vol.7 , pp. 305-326
    • Nagle, A.1    Hur, W.2    Gray, N.S.3
  • 3
    • 22244469477 scopus 로고    scopus 로고
    • Kinetic suppression of microtubule dynamic instability by griseofulvin: Implications for its possible use in the treatment of cancer
    • Panda, D., Rathinasamy, K., Santra, M. K., and Wilson, L. (2005) Kinetic suppression of microtubule dynamic instability by griseofulvin: implications for its possible use in the treatment of cancer, Proc. Natl. Acad. Sci. U.S.A. 102, 9878-9883.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 9878-9883
    • Panda, D.1    Rathinasamy, K.2    Santra, M.K.3    Wilson, L.4
  • 4
    • 11244309692 scopus 로고    scopus 로고
    • New microtubule/tubulin-targeted anticancer drugs and novel chemotherapeutic strategies
    • Wilson, L., and Jordan, M. A. (2004) New microtubule/tubulin-targeted anticancer drugs and novel chemotherapeutic strategies, J. Chemother. 16, 83-85.
    • (2004) J. Chemother , vol.16 , pp. 83-85
    • Wilson, L.1    Jordan, M.A.2
  • 5
    • 0036019535 scopus 로고    scopus 로고
    • The tubulin ancestor, FtsZ, draughtsman, designer and driving force for bacterial cytokinesis
    • Addinall, S. G., and Holland, B. (2002) The tubulin ancestor, FtsZ, draughtsman, designer and driving force for bacterial cytokinesis, J. Mol. Biol. 318, 219-236.
    • (2002) J. Mol. Biol , vol.318 , pp. 219-236
    • Addinall, S.G.1    Holland, B.2
  • 7
    • 33746358181 scopus 로고    scopus 로고
    • Dynamic filaments of the bacterial cytoskeleton
    • Michie, K. A., and Lowe, J. (2006) Dynamic filaments of the bacterial cytoskeleton, Annu. Rev. Biochem. 75, 467-492.
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 467-492
    • Michie, K.A.1    Lowe, J.2
  • 8
    • 27644540151 scopus 로고    scopus 로고
    • FtsZ and the division of prokaryotic cells and organelles
    • Margolin, W. (2005) FtsZ and the division of prokaryotic cells and organelles, Nat. Rev. Mol. Cell Biol. 6, 862-871.
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 862-871
    • Margolin, W.1
  • 9
    • 0037022642 scopus 로고    scopus 로고
    • Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching
    • Stricker, J., Maddox, P., Salmon, E. D., and Erickson, H. P. (2002) Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching, Proc. Natl. Acad. Sci. U.S.A. 99, 3171-3175.
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 3171-3175
    • Stricker, J.1    Maddox, P.2    Salmon, E.D.3    Erickson, H.P.4
  • 11
    • 0023129313 scopus 로고
    • Analysis of cell division gene ftsZ (sulB) from Gram-negative and Gram-positive bacteria
    • Corton, J. C., Ward, J. E., Jr., and Lutkenhaus, J. (1987) Analysis of cell division gene ftsZ (sulB) from Gram-negative and Gram-positive bacteria, J. Bacteriol. 169, 1 -7.
    • (1987) J. Bacteriol , vol.169 , pp. 1-7
    • Corton, J.C.1    Ward Jr., J.E.2    Lutkenhaus, J.3
  • 12
    • 0032128172 scopus 로고    scopus 로고
    • Tubulin and FtsZ structures: Functional and therapeutic implications
    • Desai, A., and Mitchison, T. J. (1998) Tubulin and FtsZ structures: functional and therapeutic implications, BioEssays 20, 523-527.
    • (1998) BioEssays , vol.20 , pp. 523-527
    • Desai, A.1    Mitchison, T.J.2
  • 13
    • 0036791627 scopus 로고    scopus 로고
    • New (and not so new) antibacterial targets - from where and when will the novel drugs come?
    • Projan, S. J. (2002) New (and not so new) antibacterial targets - from where and when will the novel drugs come?, Curr. Opin. Pharmacol. 2, 513-522.
    • (2002) Curr. Opin. Pharmacol , vol.2 , pp. 513-522
    • Projan, S.J.1
  • 14
    • 29244432515 scopus 로고    scopus 로고
    • Sanguinarine blocks cytokinesis in bacteria by inhibiting FtsZ assembly and bundling
    • Beuria, T. K., Santra, M. K., and Panda, D. (2005) Sanguinarine blocks cytokinesis in bacteria by inhibiting FtsZ assembly and bundling, Biochemistry 44, 16584-16593.
    • (2005) Biochemistry , vol.44 , pp. 16584-16593
    • Beuria, T.K.1    Santra, M.K.2    Panda, D.3
  • 15
    • 4143110291 scopus 로고    scopus 로고
    • Targeting cell division: Small-molecule inhibitors of FtsZ GTPase perturb cytokinetic ring assembly and induce bacterial lethality
    • Margalit, D. N., Romberg, L., Mets, R. B., Hebert, A. M., Mitchison, T. J., Kirschner, M. W., and RayChaudhuri, D. (2004) Targeting cell division: small-molecule inhibitors of FtsZ GTPase perturb cytokinetic ring assembly and induce bacterial lethality, Proc. Natl. Acad. Sci. U.S.A. 101, 11821-11826.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 11821-11826
    • Margalit, D.N.1    Romberg, L.2    Mets, R.B.3    Hebert, A.M.4    Mitchison, T.J.5    Kirschner, M.W.6    RayChaudhuri, D.7
  • 17
  • 18
    • 84970571443 scopus 로고
    • Totarol: A non-conventional diterpenoid
    • Bendall, J. G., and Cambie, R. C. (1995) Totarol: a non-conventional diterpenoid, Aust. J. Chem. 48, 883-917.
    • (1995) Aust. J. Chem , vol.48 , pp. 883-917
    • Bendall, J.G.1    Cambie, R.C.2
  • 19
    • 0026663089 scopus 로고
    • Antibacterial activity of totarol and its potentiation
    • Kubo, I., Muroi, H., and Himejima, M. (1992) Antibacterial activity of totarol and its potentiation, J. Nat. Prod. 55, 1436-1440.
    • (1992) J. Nat. Prod , vol.55 , pp. 1436-1440
    • Kubo, I.1    Muroi, H.2    Himejima, M.3
  • 20
    • 0034961176 scopus 로고    scopus 로고
    • (+)-Totarol from Chamaecyparis nootkatensis and activity against Mycobacterium tuberculosis
    • Constantine, G. H., Karchesy, J. J., Franzblau, S. G., and LaFleur, L. E. (2001) (+)-Totarol from Chamaecyparis nootkatensis and activity against Mycobacterium tuberculosis, Fitoterapia 72, 572-574.
    • (2001) Fitoterapia , vol.72 , pp. 572-574
    • Constantine, G.H.1    Karchesy, J.J.2    Franzblau, S.G.3    LaFleur, L.E.4
  • 21
    • 0028222723 scopus 로고
    • Naturally occurring anti-acne agents
    • Kubo, I., Muroi, H., and Kubo, A. (1994) Naturally occurring anti-acne agents, J. Nat. Prod. 57, 9-17.
    • (1994) J. Nat. Prod , vol.57 , pp. 9-17
    • Kubo, I.1    Muroi, H.2    Kubo, A.3
  • 22
    • 0029946709 scopus 로고    scopus 로고
    • Mode of antibacterial action of totarol, a diterpene from Podocarpus nagi
    • Haraguchi, H., Oike, S., Muroi, H., and Kubo, I. (1996) Mode of antibacterial action of totarol, a diterpene from Podocarpus nagi, Planta Med. 62, 122-125.
    • (1996) Planta Med , vol.62 , pp. 122-125
    • Haraguchi, H.1    Oike, S.2    Muroi, H.3    Kubo, I.4
  • 23
    • 0031660150 scopus 로고    scopus 로고
    • Inhibition of oral bacteria by phenolic compounds. Part 1. QSAR analysis using molecular connectivity
    • Shapiro, S., and Guggenheim, B. (1998) Inhibition of oral bacteria by phenolic compounds. Part 1. QSAR analysis using molecular connectivity, Quant. Struct.-Act. Relat. 17, 327-337.
    • (1998) Quant. Struct.-Act. Relat , vol.17 , pp. 327-337
    • Shapiro, S.1    Guggenheim, B.2
  • 24
    • 0035795111 scopus 로고    scopus 로고
    • Effects of (+)-totarol, a diterpenoid antibacterial agent, on phospholipids model membranes
    • Micol, V., Mateo, C. R., Shapiro, S., Aranda, F. J., and Villalain, J. (2001) Effects of (+)-totarol, a diterpenoid antibacterial agent, on phospholipids model membranes, Biochim. Biophys. Acta 1511, 281-290.
    • (2001) Biochim. Biophys. Acta , vol.1511 , pp. 281-290
    • Micol, V.1    Mateo, C.R.2    Shapiro, S.3    Aranda, F.J.4    Villalain, J.5
  • 25
    • 0033920245 scopus 로고    scopus 로고
    • The synthesis and anti bacterial activity of totarol derivatives. Part 3: Modification of ring-B
    • Evans, G. B., Furneaux, R. H., Gainsford, G. J., and Murphy, M. P. (2000) The synthesis and anti bacterial activity of totarol derivatives. Part 3: Modification of ring-B, Bioorg. Med. Chem. 8, 1663-1675.
    • (2000) Bioorg. Med. Chem , vol.8 , pp. 1663-1675
    • Evans, G.B.1    Furneaux, R.H.2    Gainsford, G.J.3    Murphy, M.P.4
  • 27
    • 2942709709 scopus 로고    scopus 로고
    • Ruthenium red-induced bundling of bacterial cell division protein, FtsZ
    • Santra, M. K., Beuria, T. K., Banerjee, A., and Panda, D. (2004) Ruthenium red-induced bundling of bacterial cell division protein, FtsZ, J. Biol. Chem. 279, 25959-25965.
    • (2004) J. Biol. Chem , vol.279 , pp. 25959-25965
    • Santra, M.K.1    Beuria, T.K.2    Banerjee, A.3    Panda, D.4
  • 29
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 30
    • 0025967969 scopus 로고
    • A malachite green colorimetric assay for protein phosphatase activity
    • Geladopoulos, T. P., Sotiroudis, T. G., and Evangelopoulos, A. E. (1991) A malachite green colorimetric assay for protein phosphatase activity, Anal. Biochem. 192, 112-116.
    • (1991) Anal. Biochem , vol.192 , pp. 112-116
    • Geladopoulos, T.P.1    Sotiroudis, T.G.2    Evangelopoulos, A.E.3
  • 31
    • 20444474170 scopus 로고    scopus 로고
    • A natural osmolyte trimethylamine N-oxide promotes assembly and bundling of the bacterial cell division protein, FtsZ and counteracts the denaturing effects of urea
    • Mukherjee, A., Santra, M. K., Beuria, T. K., and Panda, D. (2005) A natural osmolyte trimethylamine N-oxide promotes assembly and bundling of the bacterial cell division protein, FtsZ and counteracts the denaturing effects of urea, FEBS J. 272, 2760-2772.
    • (2005) FEBS J , vol.272 , pp. 2760-2772
    • Mukherjee, A.1    Santra, M.K.2    Beuria, T.K.3    Panda, D.4
  • 32
    • 0016701089 scopus 로고
    • Interaction of vinblastine with calf brain microtubule protein
    • Lee, J. C., Harrison, D., and Timasheff, S. N. (1975) Interaction of vinblastine with calf brain microtubule protein, J. Biol. Chem. 250, 9276-9282.
    • (1975) J. Biol. Chem , vol.250 , pp. 9276-9282
    • Lee, J.C.1    Harrison, D.2    Timasheff, S.N.3
  • 33
    • 2542603198 scopus 로고    scopus 로고
    • Antimitotic antifungal compound benomyl inhibits brain microtubule polymerization and dynamics and cancer cell proliferation at mitosis, by binding to a novel site in tubulin
    • Gupta, K., Bishop, J., Peck, A., Brown, J., Wilson, L., and Panda, D. (2004) Antimitotic antifungal compound benomyl inhibits brain microtubule polymerization and dynamics and cancer cell proliferation at mitosis, by binding to a novel site in tubulin, Biochemistry 43, 6645-6655.
    • (2004) Biochemistry , vol.43 , pp. 6645-6655
    • Gupta, K.1    Bishop, J.2    Peck, A.3    Brown, J.4    Wilson, L.5    Panda, D.6
  • 34
    • 0037195283 scopus 로고    scopus 로고
    • Perturbation of microtubule polymerization by quercetin through tubulin binding: A novel mechanism of its antiproliferative activity
    • Gupta, K., and Panda, D. (2002) Perturbation of microtubule polymerization by quercetin through tubulin binding: a novel mechanism of its antiproliferative activity, Biochemistry 41, 13029-13038.
    • (2002) Biochemistry , vol.41 , pp. 13029-13038
    • Gupta, K.1    Panda, D.2
  • 35
    • 33646348698 scopus 로고    scopus 로고
    • Antimitotic sulfonamides inhibit microtubule assembly dynamics and cancer cell proliferation
    • Mohan, R., Banerjee, M., Ray, A., Manna, T., Wilson, L., Owa, T., Bhattacharyya, B., and Panda, D. (2006) Antimitotic sulfonamides inhibit microtubule assembly dynamics and cancer cell proliferation, Biochemistry 45, 5440-5449.
    • (2006) Biochemistry , vol.45 , pp. 5440-5449
    • Mohan, R.1    Banerjee, M.2    Ray, A.3    Manna, T.4    Wilson, L.5    Owa, T.6    Bhattacharyya, B.7    Panda, D.8
  • 37
    • 0028274791 scopus 로고
    • Guanine nucleotide-dependent assembly of FtsZ into filaments
    • Mukherjee, A., and Lutkenhaus, J. (1994) Guanine nucleotide-dependent assembly of FtsZ into filaments, J. Bacteriol. 176, 2754-2758.
    • (1994) J. Bacteriol , vol.176 , pp. 2754-2758
    • Mukherjee, A.1    Lutkenhaus, J.2
  • 38
    • 0034932711 scopus 로고    scopus 로고
    • Escherichia coli FtsZ polymers contain mostly GTP and have a high nucleotide turnover
    • Mingorance, J., Rueda, S., Gomez-Puertasm, P., Valencia, A., and Vicente, M. (2001) Escherichia coli FtsZ polymers contain mostly GTP and have a high nucleotide turnover, Mol. Microbiol. 41, 83-91.
    • (2001) Mol. Microbiol , vol.41 , pp. 83-91
    • Mingorance, J.1    Rueda, S.2    Gomez-Puertasm, P.3    Valencia, A.4    Vicente, M.5
  • 39
    • 0032562286 scopus 로고    scopus 로고
    • Inhibition of assembly of bacterial cell division protein FtsZ by the hydrophobic dye 5,5′-bis-(8-anilino-1- naphthalenesulfonate)
    • Yu, X. C., and Margolin, W. (1998) Inhibition of assembly of bacterial cell division protein FtsZ by the hydrophobic dye 5,5′-bis-(8-anilino-1- naphthalenesulfonate), J. Biol. Chem. 273, 10216-10222.
    • (1998) J. Biol. Chem , vol.273 , pp. 10216-10222
    • Yu, X.C.1    Margolin, W.2
  • 40
    • 0347992030 scopus 로고    scopus 로고
    • In vitro pharmacodynamic activities of ABT-492, a novel quinolone, compared to those of levofloxacin against Streptococcus pneumoniae, Haemophilus influenzae, and Moraxella catarrhalis
    • Gunderson, S. M., Hayes, R. A., Quinn, J. P., and Danziger, L. H. (2004) In vitro pharmacodynamic activities of ABT-492, a novel quinolone, compared to those of levofloxacin against Streptococcus pneumoniae, Haemophilus influenzae, and Moraxella catarrhalis, Antimicrob. Agents Chemother. 48, 203-208.
    • (2004) Antimicrob. Agents Chemother , vol.48 , pp. 203-208
    • Gunderson, S.M.1    Hayes, R.A.2    Quinn, J.P.3    Danziger, L.H.4
  • 41
    • 0031686776 scopus 로고    scopus 로고
    • Activities of LL-37 a cathelin-associated antimicrobial peptide of human neutrophils
    • Turner, J., Cho, Y., Dinh, N. N., Waring, A. J., and Lehrer, R. I. (1998) Activities of LL-37 a cathelin-associated antimicrobial peptide of human neutrophils. Antimicrob. Agents Chemother. 42, 2206-2214.
    • (1998) Antimicrob. Agents Chemother , vol.42 , pp. 2206-2214
    • Turner, J.1    Cho, Y.2    Dinh, N.N.3    Waring, A.J.4    Lehrer, R.I.5
  • 42
    • 29444442409 scopus 로고    scopus 로고
    • Synthesis of antimicrobial natural products targeting FtsZ: (±)-dichamanetin and (±)-2‴-hydroxy-5″- benzylisouvarinol-B
    • Urgaonkar, S., La Pierre, H. S., Meir, I., Lund, H., RayChaudhuri, D., and Shaw, J. T. (2005) Synthesis of antimicrobial natural products targeting FtsZ: (±)-dichamanetin and (±)-2‴-hydroxy-5″- benzylisouvarinol-B, Org. Lett. 7, 5609-5612.
    • (2005) Org. Lett , vol.7 , pp. 5609-5612
    • Urgaonkar, S.1    La Pierre, H.S.2    Meir, I.3    Lund, H.4    RayChaudhuri, D.5    Shaw, J.T.6


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