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Volumn 60, Issue 9, 2011, Pages 1317-1325

Phenylpropanoids inhibit protofilament formation of Escherichia coli cell division protein FtsZ

Author keywords

[No Author keywords available]

Indexed keywords

2,4,5 TRIMETHOXYCINNAMIC ACID; 3,4 DIMETHOXYCINNAMIC ACID; ANTIINFECTIVE AGENT; CAFFEIC ACID; CARBON; CHLOROGENIC ACID; CINNAMIC ACID; COUMARIC ACID; EUGENOL; FERULIC ACID; FTSZ PROTEIN; GUANOSINE TRIPHOSPHATASE; POLYPHENOL DERIVATIVE; UNCLASSIFIED DRUG;

EID: 80051776582     PISSN: 00222615     EISSN: None     Source Type: Journal    
DOI: 10.1099/jmm.0.030536-0     Document Type: Article
Times cited : (45)

References (46)
  • 1
    • 0029989855 scopus 로고    scopus 로고
    • FtsH (HflB) is an ATP-dependent protease selectively acting on SecY and some other membrane proteins
    • Akiyama, Y., Kihara, A., Tokuda, H. & Ito, K. (1996). FtsH (HflB) is an ATP-dependent protease selectively acting on SecY and some other membrane proteins. J Biol Chem 271, 31196-31201.
    • (1996) J Biol Chem , vol.271 , pp. 31196-31201
    • Akiyama, Y.1    Kihara, A.2    Tokuda, H.3    Ito, K.4
  • 2
    • 0037783310 scopus 로고    scopus 로고
    • The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twinarginine transport pathway
    • Bernhardt, T. G. & de Boer, P. A. (2003). The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twinarginine transport pathway. Mol Microbiol 48, 1171-1182.
    • (2003) Mol Microbiol , vol.48 , pp. 1171-1182
    • Bernhardt, T.G.1    de Boer, P.A.2
  • 3
    • 29244432515 scopus 로고    scopus 로고
    • Sanguinarine blocks cytokinesis in bacteria by inhibiting FtsZ assembly and bundling
    • Beuria, T. K., Santra, M. K. & 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
  • 4
    • 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
  • 5
    • 34548024874 scopus 로고    scopus 로고
    • Eugenol and thymol, alone or in combination, induce morphological alterations in the envelope of Candida albicans
    • Braga, P. C., Sasso, M. D., Culici, M. & Alfieri, M. (2007). Eugenol and thymol, alone or in combination, induce morphological alterations in the envelope of Candida albicans. Fitoterapia 78, 396-400.
    • (2007) Fitoterapia , vol.78 , pp. 396-400
    • Braga, P.C.1    Sasso, M.D.2    Culici, M.3    Alfieri, M.4
  • 7
    • 0025212540 scopus 로고
    • A second consensus sequence of ATP-requiring proteins resides in the 21-kDa C-terminal segment of myosin subfragment 1
    • Burke, M., Rajasekharan, K. N., Maruta, S. & Ikebe, M. (1990). A second consensus sequence of ATP-requiring proteins resides in the 21-kDa C-terminal segment of myosin subfragment 1. FEBS Lett 262, 185-188.
    • (1990) FEBS Lett , vol.262 , pp. 185-188
    • Burke, M.1    Rajasekharan, K.N.2    Maruta, S.3    Ikebe, M.4
  • 9
    • 0038610624 scopus 로고    scopus 로고
    • Crystal structure of the SOS cell division inhibitor SulA and in complex with FtsZ
    • Cordell, S. C., Robinson, E. J. H. & Lowe, J. (2003). Crystal structure of the SOS cell division inhibitor SulA and in complex with FtsZ. Proc Natl Acad Sci U S A 100, 7889-7894.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 7889-7894
    • Cordell, S.C.1    Robinson, E.J.H.2    Lowe, J.3
  • 10
    • 0023751431 scopus 로고
    • Comparative molecular field analysis (CoMFA). 1. Effect of shape on binding of steroids to carrier proteins
    • Cramer, R. D., Patterson, D. E. & Bunce, J. D. (1988). Comparative molecular field analysis (CoMFA). 1. Effect of shape on binding of steroids to carrier proteins. J Am Chem Soc 110, 5959-5967.
    • (1988) J Am Chem Soc , vol.110 , pp. 5959-5967
    • Cramer, R.D.1    Patterson, D.E.2    Bunce, J.D.3
  • 12
  • 13
    • 40549143035 scopus 로고    scopus 로고
    • Berberine targets assembly of Escherichia coli cell division protein FtsZ
    • Domadia, P. N., Bhunia, A., Sivaraman, J., Swarup, S. & Dasgupta, D. (2008). Berberine targets assembly of Escherichia coli cell division protein FtsZ. Biochemistry 47, 3225-3234.
    • (2008) Biochemistry , vol.47 , pp. 3225-3234
    • Domadia, P.N.1    Bhunia, A.2    Sivaraman, J.3    Swarup, S.4    Dasgupta, D.5
  • 14
    • 0026783544 scopus 로고
    • Site-directed mutagenesis of the GTP-binding domain of b-tubulin
    • Farr, G. W. & Sternlicht, H. (1992). Site-directed mutagenesis of the GTP-binding domain of b-tubulin. J Mol Biol 227, 307-321.
    • (1992) J Mol Biol , vol.227 , pp. 307-321
    • Farr, G.W.1    Sternlicht, H.2
  • 15
    • 77956668282 scopus 로고    scopus 로고
    • Overview perspective of bacterial resistance
    • Furtado, G. H. & Nicolau, D. P. (2010). Overview perspective of bacterial resistance. Expert Opin Ther Pat 20, 1273-1276.
    • (2010) Expert Opin Ther Pat , vol.20 , pp. 1273-1276
    • Furtado, G.H.1    Nicolau, D.P.2
  • 16
    • 33645418479 scopus 로고    scopus 로고
    • Disruption of Escherichia coli, Listeria monocytogenes and Lactobacillus sakei cellular membranes by plant oil aromatics
    • Gill, A. O. & Holley, R. A. (2006). Disruption of Escherichia coli, Listeria monocytogenes and Lactobacillus sakei cellular membranes by plant oil aromatics. Int J Food Microbiol 108, 1-9.
    • (2006) Int J Food Microbiol , vol.108 , pp. 1-9
    • Gill, A.O.1    Holley, R.A.2
  • 17
    • 0011143599 scopus 로고    scopus 로고
    • Merck molecular force field. III. Molecular geometries and vibrational frequencies
    • Halgren, T. A. (1996). Merck molecular force field. III. Molecular geometries and vibrational frequencies. J Comput Chem 17, 553-586.
    • (1996) J Comput Chem , vol.17 , pp. 553-586
    • Halgren, T.A.1
  • 19
    • 70349780588 scopus 로고    scopus 로고
    • Synergistic interaction of eugenol with antibiotics against Gram negative bacteria
    • Hemaiswarya, S. & Doble, M. (2009). Synergistic interaction of eugenol with antibiotics against Gram negative bacteria. Phytomedicine 16, 997-1005.
    • (2009) Phytomedicine , vol.16 , pp. 997-1005
    • Hemaiswarya, S.1    Doble, M.2
  • 20
    • 78649405752 scopus 로고    scopus 로고
    • Synergistic interaction of phenylpropanoids with antibiotics against bacteria
    • Hemaiswarya, S. & Doble, M. (2010). Synergistic interaction of phenylpropanoids with antibiotics against bacteria. J Med Microbiol 59, 1469-1476.
    • (2010) J Med Microbiol , vol.59 , pp. 1469-1476
    • Hemaiswarya, S.1    Doble, M.2
  • 21
    • 34147136107 scopus 로고    scopus 로고
    • Totarol inhibits bacterial cytokinesis by perturbing the assembly dynamics of FtsZ
    • Jaiswal, R., Beuria, T. K., Mohan, R., Mahajan, S. K. & Panda, D. (2007). Totarol inhibits bacterial cytokinesis by perturbing the assembly dynamics of FtsZ. Biochemistry 46, 4211-4220.
    • (2007) Biochemistry , vol.46 , pp. 4211-4220
    • Jaiswal, R.1    Beuria, T.K.2    Mohan, R.3    Mahajan, S.K.4    Panda, D.5
  • 22
    • 34249023323 scopus 로고    scopus 로고
    • Phenylpropanoids as naturally occurring antioxidants: From plant defense to human health
    • Korkina, L. G. (2007). Phenylpropanoids as naturally occurring antioxidants: from plant defense to human health. Cell Mol Biol (Noisy-le-grand) 53, 15-25.
    • (2007) Cell Mol Biol (Noisy-le-grand) , vol.53 , pp. 15-25
    • Korkina, L.G.1
  • 23
    • 2642593025 scopus 로고    scopus 로고
    • Crystal structure of the bacterial celldivision protein FtsZ
    • Löwe, J. & Amos, L. A. (1998). Crystal structure of the bacterial celldivision protein FtsZ. Nature 391, 203-206.
    • (1998) Nature , vol.391 , pp. 203-206
    • Löwe, J.1    Amos, L.A.2
  • 24
    • 0037495314 scopus 로고    scopus 로고
    • Tubulin-like protofilaments in Ca2+ -induced FtsZ sheets
    • Löwe, J. & Amos, L. A. (1999). Tubulin-like protofilaments in Ca2+ -induced FtsZ sheets. EMBO J 18, 2364-2371.
    • (1999) EMBO J , vol.18 , pp. 2364-2371
    • Löwe, J.1    Amos, L.A.2
  • 25
    • 19044391883 scopus 로고    scopus 로고
    • Site-specific mutations of FtsZ-ffects on GTPase and in vitro assembly
    • Lu, C., Stricker, J. & Erickson, H. P. (2001). Site-specific mutations of FtsZ-ffects on GTPase and in vitro assembly. BMC Microbiol 1, 7.
    • (2001) BMC Microbiol , vol.1 , pp. 7
    • Lu, C.1    Stricker, J.2    Erickson, H.P.3
  • 26
    • 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
  • 27
    • 77955589135 scopus 로고    scopus 로고
    • Emerging antibiotic resistance in ocular infections and the role of fluoroquinolones
    • McDonald, M. & Blondeau, J. M. (2010). Emerging antibiotic resistance in ocular infections and the role of fluoroquinolones. J Cataract Refract Surg 36, 1588-1598.
    • (2010) J Cataract Refract Surg , vol.36 , pp. 1588-1598
    • McDonald, M.1    Blondeau, J.M.2
  • 28
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and empirical binding free energy function
    • Morris, G. M., Goodsell, D. S., Halliday, R. S., Huey, R., Hart, W. E., Belew, R. K. & Olson, A. J. (1998). Automated docking using a Lamarckian genetic algorithm and empirical binding free energy function. J Comput Chem 19, 1639-1662.
    • (1998) J Comput Chem , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 29
    • 0032916717 scopus 로고    scopus 로고
    • Analysis of FtsZ assembly by light scattering and determination of the role of divalent metal cations
    • Mukherjee, A. & Lutkenhaus, J. (1999). Analysis of FtsZ assembly by light scattering and determination of the role of divalent metal cations. J Bacteriol 181, 823-832.
    • (1999) J Bacteriol , vol.181 , pp. 823-832
    • Mukherjee, A.1    Lutkenhaus, J.2
  • 30
    • 0035209228 scopus 로고    scopus 로고
    • Assembly of an FtsZ mutant deficient in GTPase activity has implications for FtsZ assembly and the role of the Z ring in cell division
    • Mukherjee, A., Saez, C. & Lutkenhaus, J. (2001). Assembly of an FtsZ mutant deficient in GTPase activity has implications for FtsZ assembly and the role of the Z ring in cell division. J Bacteriol 183, 7190-7197.
    • (2001) J Bacteriol , vol.183 , pp. 7190-7197
    • Mukherjee, A.1    Saez, C.2    Lutkenhaus, J.3
  • 31
    • 28844446976 scopus 로고    scopus 로고
    • Antibacterial activity directed isolation of compounds from Onosma hispidum
    • Naz, S., Ahmad, S., Ajaz Rasool, S., Asad Sayeed, S. & Siddiqi, R. (2006). Antibacterial activity directed isolation of compounds from Onosma hispidum. Microbiol Res 161, 43-48.
    • (2006) Microbiol Res , vol.161 , pp. 43-48
    • Naz, S.1    Ahmad, S.2    Ajaz Rasool, S.3    Asad Sayeed, S.4    Siddiqi, R.5
  • 32
    • 0031780061 scopus 로고    scopus 로고
    • Tubulin and FtsZ form a distinct family of GTPases
    • Nogales, E., Downing, K. H., Amos, L. A. & LÖwe, J. (1998). Tubulin and FtsZ form a distinct family of GTPases. Nat Struct Biol 5, 451-458.
    • (1998) Nat Struct Biol , vol.5 , pp. 451-458
    • Nogales, E.1    Downing, K.H.2    Amos, L.A.3
  • 33
    • 44349189806 scopus 로고    scopus 로고
    • K2D2: Estimation of protein secondary structure from circular dichroism spectra
    • Perez-Iratxeta, C. & Andrade-Navarro, M. A. (2008). K2D2: estimation of protein secondary structure from circular dichroism spectra. BMC Struct Biol 8, 25.
    • (2008) BMC Struct Biol , vol.8 , pp. 25
    • Perez-Iratxeta, C.1    Andrade-Navarro, M.A.2
  • 35
    • 39749130244 scopus 로고    scopus 로고
    • Curcumin inhibits FtsZ assembly: An attractive mechanism for its antibacterial activity
    • Rai, D., Singh, J. K., Roy, N. & Panda, D. (2008). Curcumin inhibits FtsZ assembly: an attractive mechanism for its antibacterial activity. Biochem J 410, 147-155.
    • (2008) Biochem J , vol.410 , pp. 147-155
    • Rai, D.1    Singh, J.K.2    Roy, N.3    Panda, D.4
  • 36
    • 58849149503 scopus 로고    scopus 로고
    • Screening of natural phenolic compounds for potential to inhibit bacterial cell division protein FtsZ
    • Rastogi, N., Domadia, P., Shetty, S. & Dasgupta, D. (2008). Screening of natural phenolic compounds for potential to inhibit bacterial cell division protein FtsZ. Indian J Exp Biol 46, 783-787.
    • (2008) Indian J Exp Biol , vol.46 , pp. 783-787
    • Rastogi, N.1    Domadia, P.2    Shetty, S.3    Dasgupta, D.4
  • 37
    • 0242693139 scopus 로고    scopus 로고
    • Assembly dynamics of the bacterial cell division protein FtsZ: Poised at the edge of stability
    • Romberg, L. & Levin, P. A. (2003). Assembly dynamics of the bacterial cell division protein FtsZ: poised at the edge of stability. Annu Rev Microbiol 57, 125-154.
    • (2003) Annu Rev Microbiol , vol.57 , pp. 125-154
    • Romberg, L.1    Levin, P.A.2
  • 38
    • 0035853825 scopus 로고    scopus 로고
    • Polymerization of FtsZ, a bacterial homolog of tubulin: Is assembly cooperative?
    • Romberg, L., Simon, M. & Erickson, H. P. (2001). Polymerization of FtsZ, a bacterial homolog of tubulin: is assembly cooperative? J Biol Chem 276, 11743-11753.
    • (2001) J Biol Chem , vol.276 , pp. 11743-11753
    • Romberg, L.1    Simon, M.2    Erickson, H.P.3
  • 39
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Šali, A. & Blundell, T. L. (1993). Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 234, 779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Šali, A.1    Blundell, T.L.2
  • 40
    • 28644447479 scopus 로고    scopus 로고
    • Deuterium oxide promotes assembly and bundling of FtsZ protofilaments
    • Santra, M. K., Dasgupta, D. & Panda, D. (2005). Deuterium oxide promotes assembly and bundling of FtsZ protofilaments. Proteins 61, 1101-1110.
    • (2005) Proteins , vol.61 , pp. 1101-1110
    • Santra, M.K.1    Dasgupta, D.2    Panda, D.3
  • 41
    • 0037080162 scopus 로고    scopus 로고
    • GTP hydrolysis of cell division protein FtsZ: Evidence that the active site is formed by the association of monomers
    • Scheffers, D.-J., de Wit, J. G., den Blaauwen, T. & Driessen, A. J. M. (2002). GTP hydrolysis of cell division protein FtsZ: evidence that the active site is formed by the association of monomers. Biochemistry 41, 521-529.
    • (2002) Biochemistry , vol.41 , pp. 521-529
    • Scheffers, D.-J.1    de Wit, J.G.2    den Blaauwen, T.3    Driessen, A.J.M.4
  • 43
    • 76049124695 scopus 로고    scopus 로고
    • Antifungal action of chlorogenic acid against pathogenic fungi, mediated by membrane disruption
    • Sung, W. S. & Lee, D. G. (2010). Antifungal action of chlorogenic acid against pathogenic fungi, mediated by membrane disruption. Pure Appl Chem 82, 219-226.
    • (2010) Pure Appl Chem , vol.82 , pp. 219-226
    • Sung, W.S.1    Lee, D.G.2
  • 44
    • 29444442409 scopus 로고    scopus 로고
    • Synthesis of antimicrobial natural products targeting FtsZ: (±)-dichamanetin and (±)-2999-hydroxy-599-benzylisouvarinol- B
    • Urgaonkar, S., La Pierre, H. S., Meir, I., Lund, H., RayChaudhuri, D. & Shaw, J. T. (2005). Synthesis of antimicrobial natural products targeting FtsZ: (±)-dichamanetin and (±)-2999-hydroxy-599-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
  • 45
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J. E., Saraste, M., Runswick, M. J. & Gay, N. J. (1982). Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J 1, 945-951.
    • (1982) EMBO J , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 46


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