메뉴 건너뛰기




Volumn 17, Issue 5, 2007, Pages 239-245

The push and pull of the bacterial cytoskeleton

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSKELETON PROTEIN; FTSZ PROTEIN; MREB PROTEIN;

EID: 34247559763     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2007.03.005     Document Type: Review
Times cited : (24)

References (72)
  • 2
    • 8344247018 scopus 로고    scopus 로고
    • Dynamic instability in a DNA-segregating prokaryotic actin homolog
    • Garner E.C., et al. Dynamic instability in a DNA-segregating prokaryotic actin homolog. Science 306 (2004) 1021-1025
    • (2004) Science , vol.306 , pp. 1021-1025
    • Garner, E.C.1
  • 3
    • 33847675333 scopus 로고    scopus 로고
    • Reconstitution of DNA segregation driven by assembly of a prokaryotic actin homolog
    • Garner E.C., et al. Reconstitution of DNA segregation driven by assembly of a prokaryotic actin homolog. Science 315 (2007) 1270-1274
    • (2007) Science , vol.315 , pp. 1270-1274
    • Garner, E.C.1
  • 4
    • 33845789065 scopus 로고    scopus 로고
    • Concerning the dynamic instability of actin homolog ParM
    • Popp D., et al. Concerning the dynamic instability of actin homolog ParM. Biochem. Biophys. Res. Commun. 353 (2007) 109-114
    • (2007) Biochem. Biophys. Res. Commun. , vol.353 , pp. 109-114
    • Popp, D.1
  • 5
    • 0346980557 scopus 로고    scopus 로고
    • Bacterial mitosis: ParM of plasmid R1 moves plasmid DNA by an actin-like insertional polymerization mechanism
    • Moller-Jensen J., et al. Bacterial mitosis: ParM of plasmid R1 moves plasmid DNA by an actin-like insertional polymerization mechanism. Mol. Cell 12 (2003) 1477-1487
    • (2003) Mol. Cell , vol.12 , pp. 1477-1487
    • Moller-Jensen, J.1
  • 6
    • 0023042564 scopus 로고
    • Partitioning of plasmid R1. Structural and functional analysis of the parA locus
    • Gerdes K., and Molin S. Partitioning of plasmid R1. Structural and functional analysis of the parA locus. J. Mol. Biol. 190 (1986) 269-279
    • (1986) J. Mol. Biol. , vol.190 , pp. 269-279
    • Gerdes, K.1    Molin, S.2
  • 7
    • 0031580213 scopus 로고    scopus 로고
    • Partitioning of plasmid R1. The ParM protein exhibits ATPase activity and interacts with the centromere-like ParR-parC complex
    • Jensen R.B., and Gerdes K. Partitioning of plasmid R1. The ParM protein exhibits ATPase activity and interacts with the centromere-like ParR-parC complex. J. Mol. Biol. 269 (1997) 505-513
    • (1997) J. Mol. Biol. , vol.269 , pp. 505-513
    • Jensen, R.B.1    Gerdes, K.2
  • 8
    • 29444437147 scopus 로고    scopus 로고
    • Plasmid segregation mechanisms
    • Ebersbach G., and Gerdes K. Plasmid segregation mechanisms. Annu. Rev. Genet. 39 (2005) 453-479
    • (2005) Annu. Rev. Genet. , vol.39 , pp. 453-479
    • Ebersbach, G.1    Gerdes, K.2
  • 9
    • 0033565651 scopus 로고    scopus 로고
    • Mechanism of DNA segregation in prokaryotes: ParM partitioning protein of plasmid R1 co-localizes with its replicon during the cell cycle
    • Jensen R.B., and Gerdes K. Mechanism of DNA segregation in prokaryotes: ParM partitioning protein of plasmid R1 co-localizes with its replicon during the cell cycle. EMBO J. 18 (1999) 4076-4084
    • (1999) EMBO J. , vol.18 , pp. 4076-4084
    • Jensen, R.B.1    Gerdes, K.2
  • 10
    • 0037124325 scopus 로고    scopus 로고
    • Prokaryotic DNA segregation by an actin-like filament
    • Moller-Jensen J., et al. Prokaryotic DNA segregation by an actin-like filament. EMBO J. 21 (2002) 3119-3127
    • (2002) EMBO J. , vol.21 , pp. 3119-3127
    • Moller-Jensen, J.1
  • 11
    • 12244298896 scopus 로고    scopus 로고
    • F-actin-like filaments formed by plasmid segregation protein ParM
    • van den Ent F., et al. F-actin-like filaments formed by plasmid segregation protein ParM. EMBO J. 21 (2002) 6935-6943
    • (2002) EMBO J. , vol.21 , pp. 6935-6943
    • van den Ent, F.1
  • 12
    • 0033754902 scopus 로고    scopus 로고
    • The polymerization motor
    • Theriot J.A. The polymerization motor. Traffic 1 (2000) 19-28
    • (2000) Traffic , vol.1 , pp. 19-28
    • Theriot, J.A.1
  • 13
    • 33845772164 scopus 로고    scopus 로고
    • DNA segregation by the bacterial actin AlfA during Bacillus subtilis growth and development
    • Becker E., et al. DNA segregation by the bacterial actin AlfA during Bacillus subtilis growth and development. EMBO J. 25 (2006) 5919-5931
    • (2006) EMBO J. , vol.25 , pp. 5919-5931
    • Becker, E.1
  • 14
    • 33644850985 scopus 로고    scopus 로고
    • The Dam1 kinetochore ring complex moves processively on depolymerizing microtubule ends
    • Westermann S., et al. The Dam1 kinetochore ring complex moves processively on depolymerizing microtubule ends. Nature 440 (2006) 565-569
    • (2006) Nature , vol.440 , pp. 565-569
    • Westermann, S.1
  • 15
    • 33845460999 scopus 로고    scopus 로고
    • A dynamic, mitotic-like mechanism for bacterial chromosome segregation
    • Fogel M.A., and Waldor M.K. A dynamic, mitotic-like mechanism for bacterial chromosome segregation. Genes Dev. 20 (2006) 3269-3282
    • (2006) Genes Dev. , vol.20 , pp. 3269-3282
    • Fogel, M.A.1    Waldor, M.K.2
  • 16
    • 33745288732 scopus 로고    scopus 로고
    • Fine-scale time-lapse analysis of the biphasic, dynamic behaviour of the two Vibrio cholerae chromosomes
    • Fiebig A., et al. Fine-scale time-lapse analysis of the biphasic, dynamic behaviour of the two Vibrio cholerae chromosomes. Mol. Microbiol. 60 (2006) 1164-1178
    • (2006) Mol. Microbiol. , vol.60 , pp. 1164-1178
    • Fiebig, A.1
  • 17
    • 12344338949 scopus 로고    scopus 로고
    • Distinct segregation dynamics of the two Vibrio cholerae chromosomes
    • Fogel M.A., and Waldor M.K. Distinct segregation dynamics of the two Vibrio cholerae chromosomes. Mol. Microbiol. 55 (2005) 125-136
    • (2005) Mol. Microbiol. , vol.55 , pp. 125-136
    • Fogel, M.A.1    Waldor, M.K.2
  • 18
    • 33748670272 scopus 로고    scopus 로고
    • Multiple large filament bundles observed in Caulobacter crescentus by electron cryotomography
    • Briegel A., et al. Multiple large filament bundles observed in Caulobacter crescentus by electron cryotomography. Mol. Microbiol. 62 (2006) 5-14
    • (2006) Mol. Microbiol. , vol.62 , pp. 5-14
    • Briegel, A.1
  • 19
    • 0032875384 scopus 로고    scopus 로고
    • The Caulobacter crescentus smc gene is required for cell cycle progression and chromosome segregation
    • Jensen R.B., and Shapiro L. The Caulobacter crescentus smc gene is required for cell cycle progression and chromosome segregation. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 10661-10666
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 10661-10666
    • Jensen, R.B.1    Shapiro, L.2
  • 20
    • 0030901361 scopus 로고    scopus 로고
    • Cell cycle-dependent polar localization of chromosome partitioning proteins in Caulobacter crescentus
    • Mohl D.A., and Gober J.W. Cell cycle-dependent polar localization of chromosome partitioning proteins in Caulobacter crescentus. Cell 88 (1997) 675-684
    • (1997) Cell , vol.88 , pp. 675-684
    • Mohl, D.A.1    Gober, J.W.2
  • 21
    • 33744485810 scopus 로고    scopus 로고
    • The positioning of cytoplasmic protein clusters in bacteria
    • Thompson S.R., et al. The positioning of cytoplasmic protein clusters in bacteria. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 8209-8214
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 8209-8214
    • Thompson, S.R.1
  • 22
    • 31344431592 scopus 로고    scopus 로고
    • Subcellular positioning of F plasmid mediated by dynamic localization of SopA and SopB
    • Adachi S., et al. Subcellular positioning of F plasmid mediated by dynamic localization of SopA and SopB. J. Mol. Biol. 356 (2006) 850-863
    • (2006) J. Mol. Biol. , vol.356 , pp. 850-863
    • Adachi, S.1
  • 23
    • 33748512415 scopus 로고    scopus 로고
    • Regular cellular distribution of plasmids by oscillating and filament-forming ParA ATPase of plasmid pB171
    • Ebersbach G., et al. Regular cellular distribution of plasmids by oscillating and filament-forming ParA ATPase of plasmid pB171. Mol. Microbiol. 61 (2006) 1428-1442
    • (2006) Mol. Microbiol. , vol.61 , pp. 1428-1442
    • Ebersbach, G.1
  • 24
    • 29144454213 scopus 로고    scopus 로고
    • Bacterial DNA segregation by dynamic SopA polymers
    • Lim G.E., et al. Bacterial DNA segregation by dynamic SopA polymers. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 17658-17663
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 17658-17663
    • Lim, G.E.1
  • 25
    • 33745000523 scopus 로고    scopus 로고
    • Visualization of cellulose synthase demonstrates functional association with microtubules
    • Paredez A.R., et al. Visualization of cellulose synthase demonstrates functional association with microtubules. Science 312 (2006) 1491-1495
    • (2006) Science , vol.312 , pp. 1491-1495
    • Paredez, A.R.1
  • 26
    • 0031924531 scopus 로고    scopus 로고
    • FtsZ dynamics during the division cycle of live Escherichia coli cells
    • Sun Q., and Margolin W. FtsZ dynamics during the division cycle of live Escherichia coli cells. J. Bacteriol. 180 (1998) 2050-2056
    • (1998) J. Bacteriol. , vol.180 , pp. 2050-2056
    • Sun, Q.1    Margolin, W.2
  • 27
    • 33846246039 scopus 로고    scopus 로고
    • Bacterial cell division: the mechanism and its precison
    • Harry E., et al. Bacterial cell division: the mechanism and its precison. Int. Rev. Cytol. 253 (2006) 27-94
    • (2006) Int. Rev. Cytol. , vol.253 , pp. 27-94
    • Harry, E.1
  • 28
    • 24944469539 scopus 로고    scopus 로고
    • Cell division in Bacillus subtilis: FtsZ and FtsA association is Z-ring independent, and FtsA is required for efficient midcell Z-ring assembly
    • Jensen S.O., et al. Cell division in Bacillus subtilis: FtsZ and FtsA association is Z-ring independent, and FtsA is required for efficient midcell Z-ring assembly. J. Bacteriol. 187 (2005) 6536-6544
    • (2005) J. Bacteriol. , vol.187 , pp. 6536-6544
    • Jensen, S.O.1
  • 29
    • 0037084109 scopus 로고    scopus 로고
    • Unique and overlapping roles for ZipA and FtsA in septal ring assembly in Escherichia coli
    • Pichoff S., and Lutkenhaus J. Unique and overlapping roles for ZipA and FtsA in septal ring assembly in Escherichia coli. EMBO J. 21 (2002) 685-693
    • (2002) EMBO J. , vol.21 , pp. 685-693
    • Pichoff, S.1    Lutkenhaus, J.2
  • 30
    • 15744385269 scopus 로고    scopus 로고
    • Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA
    • Pichoff S., and Lutkenhaus J. Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA. Mol. Microbiol. 55 (2005) 1722-1734
    • (2005) Mol. Microbiol. , vol.55 , pp. 1722-1734
    • Pichoff, S.1    Lutkenhaus, J.2
  • 31
    • 7744230898 scopus 로고    scopus 로고
    • Z-ring-independent interaction between a subdomain of FtsA and late septation proteins as revealed by a polar recruitment assay
    • Corbin B.D., et al. Z-ring-independent interaction between a subdomain of FtsA and late septation proteins as revealed by a polar recruitment assay. J. Bacteriol. 186 (2004) 7736-7744
    • (2004) J. Bacteriol. , vol.186 , pp. 7736-7744
    • Corbin, B.D.1
  • 32
    • 4444300864 scopus 로고    scopus 로고
    • Role of two essential domains of Escherichia coli FtsA in localization and progression of the division ring
    • Rico A.I., et al. Role of two essential domains of Escherichia coli FtsA in localization and progression of the division ring. Mol. Microbiol. 53 (2004) 1359-1371
    • (2004) Mol. Microbiol. , vol.53 , pp. 1359-1371
    • Rico, A.I.1
  • 33
    • 33645055098 scopus 로고    scopus 로고
    • SepF, a novel FtsZ-interacting protein required for a late step in cell division
    • Hamoen L.W., et al. SepF, a novel FtsZ-interacting protein required for a late step in cell division. Mol. Microbiol. 59 (2006) 989-999
    • (2006) Mol. Microbiol. , vol.59 , pp. 989-999
    • Hamoen, L.W.1
  • 34
    • 33744479995 scopus 로고    scopus 로고
    • A new FtsZ-interacting protein, YlmF, complements the activity of FtsA during progression of cell division in Bacillus subtilis
    • Ishikawa S., et al. A new FtsZ-interacting protein, YlmF, complements the activity of FtsA during progression of cell division in Bacillus subtilis. Mol. Microbiol. 60 (2006) 1364-1380
    • (2006) Mol. Microbiol. , vol.60 , pp. 1364-1380
    • Ishikawa, S.1
  • 35
    • 4344652693 scopus 로고    scopus 로고
    • Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins
    • Anderson D.E., et al. Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins. J. Bacteriol. 186 (2004) 5775-5781
    • (2004) J. Bacteriol. , vol.186 , pp. 5775-5781
    • Anderson, D.E.1
  • 36
    • 3142602980 scopus 로고    scopus 로고
    • FtsZ exhibits rapid movement and oscillation waves in helix-like patterns in Escherichia coli
    • Thanedar S., and Margolin W. FtsZ exhibits rapid movement and oscillation waves in helix-like patterns in Escherichia coli. Curr. Biol. 14 (2004) 1167-1173
    • (2004) Curr. Biol. , vol.14 , pp. 1167-1173
    • Thanedar, S.1    Margolin, W.2
  • 37
    • 30544445654 scopus 로고    scopus 로고
    • Spatial control of bacterial division-site placement
    • Rothfield L., et al. Spatial control of bacterial division-site placement. Nat. Rev. Microbiol. 3 (2005) 959-968
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 959-968
    • Rothfield, L.1
  • 38
    • 33745699284 scopus 로고    scopus 로고
    • MipZ, a spatial regulator coordinating chromosome segregation with cell division in Caulobacter
    • Thanbichler M., and Shapiro L. MipZ, a spatial regulator coordinating chromosome segregation with cell division in Caulobacter. Cell 126 (2006) 147-162
    • (2006) Cell , vol.126 , pp. 147-162
    • Thanbichler, M.1    Shapiro, L.2
  • 39
    • 0037133943 scopus 로고    scopus 로고
    • Asymmetric cell division in B. subtilis involves a spiral-like intermediate of the cytokinetic protein FtsZ
    • Ben-Yehuda S., and Losick R. Asymmetric cell division in B. subtilis involves a spiral-like intermediate of the cytokinetic protein FtsZ. Cell 109 (2002) 257-266
    • (2002) Cell , vol.109 , pp. 257-266
    • Ben-Yehuda, S.1    Losick, R.2
  • 40
    • 0032539813 scopus 로고    scopus 로고
    • Inhibition of FtsZ polymerization by SulA, an inhibitor of septation in Escherichia coli
    • Mukherjee A., et al. Inhibition of FtsZ polymerization by SulA, an inhibitor of septation in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 2885-2890
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 2885-2890
    • Mukherjee, A.1
  • 41
    • 0037494988 scopus 로고    scopus 로고
    • Control of cell morphogenesis in bacteria: two distinct ways to make a rod-shaped cell
    • Daniel R.A., and Errington J. Control of cell morphogenesis in bacteria: two distinct ways to make a rod-shaped cell. Cell 113 (2003) 767-776
    • (2003) Cell , vol.113 , pp. 767-776
    • Daniel, R.A.1    Errington, J.2
  • 42
    • 0035937396 scopus 로고    scopus 로고
    • Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis
    • Jones L.J., et al. Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis. Cell 104 (2001) 913-922
    • (2001) Cell , vol.104 , pp. 913-922
    • Jones, L.J.1
  • 43
    • 1542616355 scopus 로고    scopus 로고
    • MreB, the cell shape-determining bacterial actin homologue, coordinates cell wall morphogenesis in Caulobacter crescentus
    • Figge R.M., et al. MreB, the cell shape-determining bacterial actin homologue, coordinates cell wall morphogenesis in Caulobacter crescentus. Mol. Microbiol. 51 (2004) 1321-1332
    • (2004) Mol. Microbiol. , vol.51 , pp. 1321-1332
    • Figge, R.M.1
  • 44
    • 33747837700 scopus 로고    scopus 로고
    • Actin homolog MreBH governs cell morphogenesis by localization of the cell wall hydrolase LytE
    • Carballido-Lopez R., et al. Actin homolog MreBH governs cell morphogenesis by localization of the cell wall hydrolase LytE. Dev. Cell 11 (2006) 399-409
    • (2006) Dev. Cell , vol.11 , pp. 399-409
    • Carballido-Lopez, R.1
  • 45
    • 29344476196 scopus 로고    scopus 로고
    • The cell-shape protein MreC interacts with extracytoplasmic proteins including cell wall assembly complexes in Caulobacter crescentus
    • Divakaruni A.V., et al. The cell-shape protein MreC interacts with extracytoplasmic proteins including cell wall assembly complexes in Caulobacter crescentus. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 18602-18607
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 18602-18607
    • Divakaruni, A.V.1
  • 46
    • 29444457542 scopus 로고    scopus 로고
    • Two independent spiral structures control cell shape in Caulobacter
    • Dye N.A., et al. Two independent spiral structures control cell shape in Caulobacter. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 18608-18613
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 18608-18613
    • Dye, N.A.1
  • 47
    • 23844444807 scopus 로고    scopus 로고
    • Roles for MreC and MreD proteins in helical growth of the cylindrical cell wall in Bacillus subtilis
    • Leaver M., and Errington J. Roles for MreC and MreD proteins in helical growth of the cylindrical cell wall in Bacillus subtilis. Mol. Microbiol. 57 (2005) 1196-1209
    • (2005) Mol. Microbiol. , vol.57 , pp. 1196-1209
    • Leaver, M.1    Errington, J.2
  • 48
    • 12344306119 scopus 로고    scopus 로고
    • The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex
    • Kruse T., et al. The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex. Mol. Microbiol. 55 (2005) 78-89
    • (2005) Mol. Microbiol. , vol.55 , pp. 78-89
    • Kruse, T.1
  • 49
    • 0037237123 scopus 로고    scopus 로고
    • The bacterial cytoskeleton: in vivo dynamics of the actin-like protein Mbl of Bacillus subtilis
    • Carballido-Lopez R., and Errington J. The bacterial cytoskeleton: in vivo dynamics of the actin-like protein Mbl of Bacillus subtilis. Dev. Cell 4 (2003) 19-28
    • (2003) Dev. Cell , vol.4 , pp. 19-28
    • Carballido-Lopez, R.1    Errington, J.2
  • 50
    • 33750713640 scopus 로고    scopus 로고
    • Dynamic localization and interaction with other Bacillus subtilis actin-like proteins are important for the function of MreB
    • Defeu Soufo H.J., and Graumann P.L. Dynamic localization and interaction with other Bacillus subtilis actin-like proteins are important for the function of MreB. Mol. Microbiol. 62 (2006) 1340-1356
    • (2006) Mol. Microbiol. , vol.62 , pp. 1340-1356
    • Defeu Soufo, H.J.1    Graumann, P.L.2
  • 51
    • 4444285310 scopus 로고    scopus 로고
    • Dynamic movement of actin-like proteins within bacterial cells
    • Defeu Soufo H.J., and Graumann P.L. Dynamic movement of actin-like proteins within bacterial cells. EMBO Rep. 5 (2004) 789-794
    • (2004) EMBO Rep. , vol.5 , pp. 789-794
    • Defeu Soufo, H.J.1    Graumann, P.L.2
  • 52
    • 33746655349 scopus 로고    scopus 로고
    • Single molecules of the bacterial actin MreB undergo directed treadmilling motion in Caulobacter crescentus
    • Kim S.Y., et al. Single molecules of the bacterial actin MreB undergo directed treadmilling motion in Caulobacter crescentus. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 10929-10934
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 10929-10934
    • Kim, S.Y.1
  • 53
    • 13544274210 scopus 로고    scopus 로고
    • MreB actin-mediated segregation of a specific region of a bacterial chromosome
    • Gitai Z., et al. MreB actin-mediated segregation of a specific region of a bacterial chromosome. Cell 120 (2005) 329-341
    • (2005) Cell , vol.120 , pp. 329-341
    • Gitai, Z.1
  • 54
    • 2942588534 scopus 로고    scopus 로고
    • An actin-like gene can determine cell polarity in bacteria
    • Gitai Z., et al. An actin-like gene can determine cell polarity in bacteria. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 8643-8648
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 8643-8648
    • Gitai, Z.1
  • 55
    • 0037699937 scopus 로고    scopus 로고
    • Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles
    • Shih Y.L., et al. Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 7865-7870
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 7865-7870
    • Shih, Y.L.1
  • 56
    • 30844471175 scopus 로고    scopus 로고
    • Magnetosomes are cell membrane invaginations organized by the actin-like protein MamK
    • Komeili A., et al. Magnetosomes are cell membrane invaginations organized by the actin-like protein MamK. Science 311 (2006) 242-245
    • (2006) Science , vol.311 , pp. 242-245
    • Komeili, A.1
  • 58
    • 33751257193 scopus 로고    scopus 로고
    • Biogenesis of actin-like bacterial cytoskeletal filaments destined for positioning prokaryotic magnetic organelles
    • Pradel N., et al. Biogenesis of actin-like bacterial cytoskeletal filaments destined for positioning prokaryotic magnetic organelles. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 17485-17489
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 17485-17489
    • Pradel, N.1
  • 60
    • 33845874640 scopus 로고    scopus 로고
    • Polar positional information in Escherichia coli spherical cells
    • Pradel N., et al. Polar positional information in Escherichia coli spherical cells. Biochem. Biophys. Res. Commun. 353 (2007) 493-500
    • (2007) Biochem. Biophys. Res. Commun. , vol.353 , pp. 493-500
    • Pradel, N.1
  • 61
    • 11844281590 scopus 로고    scopus 로고
    • Caulobacter crescentus requires RodA and MreB for stalk synthesis and prevention of ectopic pole formation
    • Wagner J.K., et al. Caulobacter crescentus requires RodA and MreB for stalk synthesis and prevention of ectopic pole formation. J. Bacteriol. 187 (2005) 544-553
    • (2005) J. Bacteriol. , vol.187 , pp. 544-553
    • Wagner, J.K.1
  • 62
    • 0346020436 scopus 로고    scopus 로고
    • The bacterial cytoskeleton: an intermediate filament-like function in cell shape
    • Ausmees N., et al. The bacterial cytoskeleton: an intermediate filament-like function in cell shape. Cell 115 (2003) 705-713
    • (2003) Cell , vol.115 , pp. 705-713
    • Ausmees, N.1
  • 63
    • 0037168644 scopus 로고    scopus 로고
    • Dynamic assembly of MinD into filament bundles modulated by ATP, phospholipids, and MinE
    • Suefuji K., et al. Dynamic assembly of MinD into filament bundles modulated by ATP, phospholipids, and MinE. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 16776-16781
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 16776-16781
    • Suefuji, K.1
  • 64
    • 0034234636 scopus 로고    scopus 로고
    • Plasmid and chromosome segregation in prokaryotes
    • Moller-Jensen J., et al. Plasmid and chromosome segregation in prokaryotes. Trends Microbiol. 8 (2000) 313-320
    • (2000) Trends Microbiol. , vol.8 , pp. 313-320
    • Moller-Jensen, J.1
  • 65
    • 0033861269 scopus 로고    scopus 로고
    • Plasmid and chromosome partitioning: surprises from phylogeny
    • Gerdes K., et al. Plasmid and chromosome partitioning: surprises from phylogeny. Mol. Microbiol. 37 (2000) 455-466
    • (2000) Mol. Microbiol. , vol.37 , pp. 455-466
    • Gerdes, K.1
  • 66
    • 0027480463 scopus 로고
    • A superfamily of ATPases with diverse functions containing either classical or deviant ATP-binding motif
    • Koonin E.V. A superfamily of ATPases with diverse functions containing either classical or deviant ATP-binding motif. J. Mol. Biol. 229 (1993) 1165-1174
    • (1993) J. Mol. Biol. , vol.229 , pp. 1165-1174
    • Koonin, E.V.1
  • 67
    • 17844403033 scopus 로고    scopus 로고
    • Bacterial DNA segregation dynamics mediated by the polymerizing protein ParF
    • Barilla D., et al. Bacterial DNA segregation dynamics mediated by the polymerizing protein ParF. EMBO J. 24 (2005) 1453-1464
    • (2005) EMBO J. , vol.24 , pp. 1453-1464
    • Barilla, D.1
  • 68
    • 33846081941 scopus 로고    scopus 로고
    • Polymerization of SopA partition ATPase: regulation by DNA binding and SopB
    • Bouet J.Y., et al. Polymerization of SopA partition ATPase: regulation by DNA binding and SopB. Mol. Microbiol. 63 (2007) 468-481
    • (2007) Mol. Microbiol. , vol.63 , pp. 468-481
    • Bouet, J.Y.1
  • 69
    • 13444281991 scopus 로고    scopus 로고
    • Bacterial chromosome segregation: structure and DNA binding of the Soj dimer - a conserved biological switch
    • Leonard T.A., et al. Bacterial chromosome segregation: structure and DNA binding of the Soj dimer - a conserved biological switch. EMBO J. 24 (2005) 270-282
    • (2005) EMBO J. , vol.24 , pp. 270-282
    • Leonard, T.A.1
  • 70
    • 1942468854 scopus 로고    scopus 로고
    • Bacterial mitosis: partitioning protein ParA oscillates in spiral-shaped structures and positions plasmids at mid-cell
    • Ebersbach G., and Gerdes K. Bacterial mitosis: partitioning protein ParA oscillates in spiral-shaped structures and positions plasmids at mid-cell. Mol. Microbiol. 52 (2004) 385-398
    • (2004) Mol. Microbiol. , vol.52 , pp. 385-398
    • Ebersbach, G.1    Gerdes, K.2
  • 71
    • 0033231585 scopus 로고    scopus 로고
    • Dynamic movement of the ParA-like Soj protein of B. subtilis and its dual role in nucleoid organization and developmental regulation
    • Marston A.L., and Errington J. Dynamic movement of the ParA-like Soj protein of B. subtilis and its dual role in nucleoid organization and developmental regulation. Mol. Cell 4 (1999) 673-682
    • (1999) Mol. Cell , vol.4 , pp. 673-682
    • Marston, A.L.1    Errington, J.2
  • 72
    • 0033609139 scopus 로고    scopus 로고
    • Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli
    • Raskin D.M., and de Boer P.A. Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 4971-4976
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 4971-4976
    • Raskin, D.M.1    de Boer, P.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.