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Volumn 34, Issue 1-2 SPEC. ISS., 2008, Pages 237-247

In vitro reconstitution of the initial stages of the bacterial cell division machinery

Author keywords

Atomic force microscope; Bacterial cytoskeleton; FtsZ; Planar lipid bilayers; Theoretical modeling

Indexed keywords

ESCHERICHIA COLI PROTEIN; FTSZ PROTEIN; MICA; PROTEIN ZIPA; UNCLASSIFIED DRUG;

EID: 55349102644     PISSN: 00920606     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10867-008-9118-8     Document Type: Article
Times cited : (7)

References (36)
  • 1
    • 33846246039 scopus 로고    scopus 로고
    • Bacterial cell division: The mechanism and its precision
    • doi:10.1016/S0074-7696(06)53002-5
    • E. Harry L. Monahan L. Thompson 2006 Bacterial cell division: the mechanism and its precision Int. Rev. Cytol. 253 27 93 doi:10.1016/S0074- 7696(06)53002-5
    • (2006) Int. Rev. Cytol. , vol.253 , pp. 27-93
    • Harry, E.1    Monahan, L.2    Thompson, L.3
  • 2
    • 33745209434 scopus 로고    scopus 로고
    • The order of the ring: Assembly of Escherichia coli cell division components
    • 1
    • M. Vicente A.I. Rico 2006 The order of the ring: assembly of Escherichia coli cell division components Mol. Microbiol. 61 1 5 8
    • (2006) Mol. Microbiol. , vol.61 , pp. 5-8
    • Vicente, M.1    Rico, A.I.2
  • 3
    • 0342903325 scopus 로고    scopus 로고
    • Physical properties determining self-organization of motors and microtubules
    • 5519. doi:10.1126/science.1059758
    • T. Surrey F. Nédélec S. Leibler E. Karsenti 2001 Physical properties determining self-organization of motors and microtubules Science 292 5519 1167 1171 doi:10.1126/science.1059758
    • (2001) Science , vol.292 , pp. 1167-1171
    • Surrey, T.1    Nédélec, F.2    Leibler, S.3    Karsenti, E.4
  • 4
    • 33750530385 scopus 로고    scopus 로고
    • Modelling microtubule patterns
    • 11. doi:10.1038/ncb1498
    • E. Karsenti F. Nédélec T. Surrey 2006 Modelling microtubule patterns Nat. Cell Biol. 8 11 1204 1211 doi:10.1038/ncb1498
    • (2006) Nat. Cell Biol. , vol.8 , pp. 1204-1211
    • Karsenti, E.1    Nédélec, F.2    Surrey, T.3
  • 6
    • 33847773123 scopus 로고    scopus 로고
    • Direct measurement of force generation by actin filament polymerization using an optical trap
    • 7. doi:10.1073/pnas.0607052104
    • M.J. Footer J.W.J. Kerssemakers J.A. Theriot M. Dogterom 2007 Direct measurement of force generation by actin filament polymerization using an optical trap Proc. Natl. Acad. Sci. U. S. A. 104 7 2181 2186 doi:10.1073/pnas.0607052104
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 2181-2186
    • Footer, M.J.1    Kerssemakers, J.W.J.2    Theriot, J.A.3    Dogterom, M.4
  • 7
    • 33846839169 scopus 로고    scopus 로고
    • Microtubule organization in three-dimensional confined geometries: Evaluating the role of elasticity through a combined in vitro and modeling approach
    • 3. doi:10.1529/biophysj.105.076893
    • M.C. Lagomarsino C. Tanase J.W. Vos A.M.C. Emons B.M. Mulder M. Dogterom 2007 Microtubule organization in three-dimensional confined geometries: evaluating the role of elasticity through a combined in vitro and modeling approach Biophys. J. 92 3 1046 1057 doi:10.1529/biophysj.105.076893
    • (2007) Biophys. J. , vol.92 , pp. 1046-1057
    • Lagomarsino, M.C.1    Tanase, C.2    Vos, J.W.3    Emons, A.M.C.4    Mulder, B.M.5    Dogterom, M.6
  • 8
    • 34748876488 scopus 로고    scopus 로고
    • Cargo pick-up from engineered loading stations by kinesin driven molecular shuttles
    • doi:10.1039/b707301a
    • C. Brunner C. Wahnes V. Vogel 2007 Cargo pick-up from engineered loading stations by kinesin driven molecular shuttles Lab Chip 7 1263 1271 doi:10.1039/b707301a
    • (2007) Lab Chip , vol.7 , pp. 1263-1271
    • Brunner, C.1    Wahnes, C.2    Vogel, V.3
  • 9
    • 1942469927 scopus 로고    scopus 로고
    • Motor-protein "roundabouts": Microtubules moving on kinesin-coated tracks through engineered networks
    • J. Clemmens H. Hess R. Doot C.M. Matzke G.D. Bachand V. Vogel 2004 Motor-protein "roundabouts": microtubules moving on kinesin-coated tracks through engineered networks Lab Chip 4 83 86
    • (2004) Lab Chip , vol.4 , pp. 83-86
    • Clemmens, J.1    Hess, H.2    Doot, R.3    Matzke, C.M.4    Bachand, G.D.5    Vogel, V.6
  • 10
    • 33749264425 scopus 로고    scopus 로고
    • The bacterial cytoskeleton
    • 3. doi:10.1128/MMBR.00017-06
    • Y.-L. Shih L. Rothfield 2006 The bacterial cytoskeleton Microbiol. Mol. Biol. Rev. 70 3 729 754 doi:10.1128/MMBR.00017-06
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 729-754
    • Shih, Y.-L.1    Rothfield, L.2
  • 11
    • 0025733254 scopus 로고
    • FtsZ is an essential cell division gene in Escherichia coli
    • 11
    • K. Dai J. Lutkenhaus 1991 FtsZ is an essential cell division gene in Escherichia coli J. Bacteriol. 173 11 3500 3506
    • (1991) J. Bacteriol. , vol.173 , pp. 3500-3506
    • Dai, K.1    Lutkenhaus, J.2
  • 12
    • 27644540151 scopus 로고    scopus 로고
    • FtsZ and the division of prokaryotic cells and organelles
    • doi:10.1038/nrm1745
    • W. Margolin 2005 FtsZ and the division of prokaryotic cells and organelles Nat. Rev. Mol. Cell Biol. 6 862 871 doi:10.1038/nrm1745
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 862-871
    • Margolin, W.1
  • 13
    • 33748777110 scopus 로고    scopus 로고
    • Z ring as executor of bacterial cell division
    • doi:10.1159/000094050
    • A. Dajkovic J. Lutkenhaus 2006 Z ring as executor of bacterial cell division J. Mol. Microbiol. Biotechnol. 11 140 151 doi:10.1159/000094050
    • (2006) J. Mol. Microbiol. Biotechnol. , vol.11 , pp. 140-151
    • Dajkovic, A.1    Lutkenhaus, J.2
  • 14
    • 0242693139 scopus 로고    scopus 로고
    • Assembly dynamics of the bacterial cell division protein FtsZ: Poised at the edge of stability
    • doi:10.1146/annurev.micro.57.012903.074300
    • L. Romberg P.A. Levin 2003 Assembly dynamics of the bacterial cell division protein FtsZ: poised at the edge of stability Annu. Rev. Microbiol. 57 125 154 doi:10.1146/annurev.micro.57.012903.074300
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 125-154
    • Romberg, L.1    Levin, P.A.2
  • 15
    • 0037022642 scopus 로고    scopus 로고
    • Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching
    • doi:10.1073/pnas.052595099
    • J. Stricker P. Maddox E.D. Salmon H.P. Erickson 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 doi:10.1073/pnas.052595099
    • (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
  • 16
    • 0031444158 scopus 로고    scopus 로고
    • Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. coli
    • doi:10.1016/S0092-8674(00)81838-3
    • C.A. Hale P.A.J. de Boer 1997 Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. coli Cell 88 175 185 doi:10.1016/S0092-8674(00)81838-3
    • (1997) Cell , vol.88 , pp. 175-185
    • Hale, C.A.1    De Boer, P.A.J.2
  • 17
    • 0040735625 scopus 로고    scopus 로고
    • Magnesium-induced linear self-association of the FtsZ bacterial cell division protein monomer-the primary steps for the FtsZ assembly
    • doi:10.1074/jbc.275.16.11740
    • G. Rivas A. López J. Mingorance M.J. Ferrandiz S. Zorrilla A. Minton M. Vicente J.M. Andreu 2000 Magnesium-induced linear self-association of the FtsZ bacterial cell division protein monomer-the primary steps for the FtsZ assembly J. Biol. Chem. 275 11740 11749 doi:10.1074/jbc.275.16.11740
    • (2000) J. Biol. Chem. , vol.275 , pp. 11740-11749
    • Rivas, G.1    López, A.2    Mingorance, J.3    Ferrandiz, M.J.4    Zorrilla, S.5    Minton, A.6    Vicente, M.7    Andreu, J.M.8
  • 18
    • 0033522467 scopus 로고    scopus 로고
    • ZipA is a MAP-Tau homolog and is essential for structural integrity of the cytokinetic FtsZ ring during bacterial cell division
    • doi:10.1093/emboj/18.9.2372
    • D. RayChaudhuri 1999 ZipA is a MAP-Tau homolog and is essential for structural integrity of the cytokinetic FtsZ ring during bacterial cell division EMBO J. 18 2372 2383 doi:10.1093/emboj/18.9.2372
    • (1999) EMBO J. , vol.18 , pp. 2372-2383
    • Raychaudhuri, D.1
  • 20
    • 0035979743 scopus 로고    scopus 로고
    • Two-dimensional crystallization of membrane proteins: The lipid layer strategy
    • doi:10.1016/S0014-5793(01)02748-X
    • D.C.M. Levy J.L. Rigaud 2001 Two-dimensional crystallization of membrane proteins: the lipid layer strategy FEBS Lett. 504 187 193 doi:10.1016/S0014- 5793(01)02748-X
    • (2001) FEBS Lett. , vol.504 , pp. 187-193
    • Levy, D.C.M.1    Rigaud, J.L.2
  • 21
    • 20144383298 scopus 로고    scopus 로고
    • Visualization of single Escherichia coli FtsZ filament dynamics with atomic force microscopy
    • doi:10.1074/jbc.M503059200
    • J. Mingorance M. Tadros M. Vicente J.M. González G. Rivas M. Vélez 2005 Visualization of single Escherichia coli FtsZ filament dynamics with atomic force microscopy J. Biol. Chem. 280 20909 20914 doi:10.1074/jbc.M503059200
    • (2005) J. Biol. Chem. , vol.280 , pp. 20909-20914
    • Mingorance, J.1    Tadros, M.2    Vicente, M.3    González, J.M.4    Rivas, G.5    Vélez, M.6
  • 22
    • 13844312609 scopus 로고    scopus 로고
    • The cooperative behavior of E. coli cell division protein FtsZ assembly involves the preferential cyclization of long single-stranded fibrils
    • doi:10.1073/pnas.0409517102
    • J.M. González M. Vélez M. Jiménez C. Alfonso P. Schuck J. Mingorance M. Vicente A.P. Minton G. Rivas 2005 The cooperative behavior of E. coli cell division protein FtsZ assembly involves the preferential cyclization of long single-stranded fibrils Proc. Natl. Acad. Sci. U. S. A. 102 1895 1900 doi:10.1073/pnas.0409517102
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 1895-1900
    • González, J.M.1    Vélez, M.2    Jiménez, M.3    Alfonso, C.4    Schuck, P.5    Mingorance, J.6    Vicente, M.7    Minton, A.P.8    Rivas, G.9
  • 23
    • 20144374380 scopus 로고
    • Stabilization of microtubules by inorganic phosphate and its structural analogues, the fluoride complexes of aluminium and beryllium
    • doi:10.1021/bi00434a073
    • M. Carlier D. Didry R. Melki M. Chabre D. Pantaloni 1989 Stabilization of microtubules by inorganic phosphate and its structural analogues, the fluoride complexes of aluminium and beryllium Biochemistry 28 3628 doi:10.1021/ bi00434a073
    • (1989) Biochemistry , vol.28 , pp. 3628
    • Carlier, M.1    Didry, D.2    Melki, R.3    Chabre, M.4    Pantaloni, D.5
  • 24
    • 0023426241 scopus 로고
    • Fluoride complexes of aluminium or beryllium act on G-proteins as reversibly bound analogues of the gamma phosphate of GTP
    • J.D.P. Bigay C. Pfister M. Chabre 1987 Fluoride complexes of aluminium or beryllium act on G-proteins as reversibly bound analogues of the gamma phosphate of GTP EMBO J. 6 2907 2913
    • (1987) EMBO J. , vol.6 , pp. 2907-2913
    • Bigay, J.D.P.1    Pfister, C.2    Chabre, M.3
  • 25
    • 0028142491 scopus 로고
    • A point mutation converts Escherichia coli FtsZ septation GTPase to an ATPase
    • D. RayChaudhuri J.T. Park 1994 A point mutation converts Escherichia coli FtsZ septation GTPase to an ATPase J. Biol. Chem. 269 22941 22944
    • (1994) J. Biol. Chem. , vol.269 , pp. 22941-22944
    • Raychaudhuri, D.1    Park, J.T.2
  • 26
    • 40749098614 scopus 로고    scopus 로고
    • Langevin computer simulations of FtsZ filaments and the force generating mechanism during cell division
    • I. Hörger E. Velasco J. Mingorance G. Rivas M. Vélez P. Tarazona 2008 Langevin computer simulations of FtsZ filaments and the force generating mechanism during cell division Phys. Rev., E 77 011902
    • (2008) Phys. Rev., e , vol.77 , pp. 011902
    • Hörger, I.1    Velasco, E.2    Mingorance, J.3    Rivas, G.4    Vélez, M.5    Tarazona, P.6
  • 27
    • 15744385269 scopus 로고    scopus 로고
    • Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA
    • 6. doi:10.1111/j.1365-2958.2005.04522.x
    • S. Pichoff J. Lutkenhaus 2005 Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA Mol. Microbiol. 55 6 1722 1734 doi:10.1111/j.1365-2958.2005.04522.x
    • (2005) Mol. Microbiol. , vol.55 , pp. 1722-1734
    • Pichoff, S.1    Lutkenhaus, J.2
  • 28
    • 0036063886 scopus 로고    scopus 로고
    • Structural evidence that the P/Q domain of ZipA is an unstructured, flexible tether between the membrane and the C-terminal FtsZ-binding domain
    • 15. doi:10.1128/JB.184.15.4313-4315.2002
    • T. Ohashi C.A. Hale P.A.J. de Boer H.P. Erickson 2002 Structural evidence that the P/Q domain of ZipA is an unstructured, flexible tether between the membrane and the C-terminal FtsZ-binding domain J. Bacteriol. 184 15 4313 4315 doi:10.1128/JB.184.15.4313-4315.2002
    • (2002) J. Bacteriol. , vol.184 , pp. 4313-4315
    • Ohashi, T.1    Hale, C.A.2    De Boer, P.A.J.3    Erickson, H.P.4
  • 29
    • 0033810918 scopus 로고    scopus 로고
    • ZipA-Induced bundling of FtsZ polymers mediated by an interaction between C-terminal domains
    • 18. doi:10.1128/JB.182.18.5153-5166.2000
    • C.A. Hale A.C. Rhee P.A.J. de Boer 2000 ZipA-Induced bundling of FtsZ polymers mediated by an interaction between C-terminal domains J. Bacteriol. 182 18 5153 5166 doi:10.1128/JB.182.18.5153-5166.2000
    • (2000) J. Bacteriol. , vol.182 , pp. 5153-5166
    • Hale, C.A.1    Rhee, A.C.2    De Boer, P.A.J.3
  • 30
    • 0030068218 scopus 로고    scopus 로고
    • Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers
    • doi:10.1073/pnas.93.1.519
    • H. Erickson D. Taylor K.A. Taylor D. Bramhill 1996 Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers Proc. Natl. Acad. Sci. U. S. A. 93 519 523 doi:10.1073/pnas.93.1.519
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 519-523
    • Erickson, H.1    Taylor, D.2    Taylor, K.A.3    Bramhill, D.4
  • 32
    • 44849125736 scopus 로고    scopus 로고
    • FtsZ bacterial cytoskeletal polymers on curved surfaces: The importance of lateral interactions
    • doi:10.1529/biophysj.107.128363
    • I. Hörger E. Velasco G. Rivas M. Vélez P. Tarazona 2008 FtsZ bacterial cytoskeletal polymers on curved surfaces: the importance of lateral interactions Biophys. J. 94 L81 L83 doi:10.1529/biophysj.107.128363
    • (2008) Biophys. J. , vol.94
    • Hörger, I.1    Velasco, E.2    Rivas, G.3    Vélez, M.4    Tarazona, P.5
  • 33
    • 19044391883 scopus 로고    scopus 로고
    • Site-specific mutations of FtsZ-effects on GTPase and in vitro assembly
    • 7
    • C. Lu J. Stricker H.P. Erickson 2001 Site-specific mutations of FtsZ-effects on GTPase and in vitro assembly BMC Microbiol. 1 7 1471 1482
    • (2001) BMC Microbiol. , vol.1 , pp. 1471-1482
    • Lu, C.1    Stricker, J.2    Erickson, H.P.3
  • 34
    • 20544468417 scopus 로고    scopus 로고
    • The rapid onset of elasticity during the assembly of the bacterial cell-division protein FtsZ
    • doi:10.1016/j.bbrc.2005.05.152
    • O. Esue Y. Tseng D. Wirtz 2005 The rapid onset of elasticity during the assembly of the bacterial cell-division protein FtsZ Biochem. Biophys. Res. Commun. 333 508 516 doi:10.1016/j.bbrc.2005.05.152
    • (2005) Biochem. Biophys. Res. Commun. , vol.333 , pp. 508-516
    • Esue, O.1    Tseng, Y.2    Wirtz, D.3
  • 35
    • 34548745271 scopus 로고    scopus 로고
    • A mechanical explanation for cytoskeletal rings and helices in bacteria
    • doi:10.1529/biophysj.106.102343
    • S.S. Andrews A.P. Arkin 2007 A mechanical explanation for cytoskeletal rings and helices in bacteria Biophys. J. 93 1872 1884 doi:10.1529/biophysj.106. 102343
    • (2007) Biophys. J. , vol.93 , pp. 1872-1884
    • Andrews, S.S.1    Arkin, A.P.2
  • 36
    • 0035146299 scopus 로고    scopus 로고
    • The FtsZ protofilament and attachment of ZipA-structural constraints on the FtsZ power stroke
    • doi:10.1016/S0955-0674(00)00174-5
    • H.P. Erickson 2001 The FtsZ protofilament and attachment of ZipA-structural constraints on the FtsZ power stroke Curr. Opin. Cell Biol. 13 55 60 doi:10.1016/S0955-0674(00)00174-5
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 55-60
    • Erickson, H.P.1


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