메뉴 건너뛰기




Volumn 6, Issue 1, 2008, Pages 28-40

Getting organized - How bacterial cells move proteins and DNA

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN LIKE PROTEIN; ADENOSINE TRIPHOSPHATASE; BACTERIAL DNA; BACTERIAL PROTEIN; CRESCENTIN; INTERMEDIATE FILAMENT PROTEIN; MEMBRANE PROTEIN; PROTEIN MREC; TUBULIN; UNCLASSIFIED DRUG; WALKER TYPE ADENOSINE TRIPHOSPHATASE;

EID: 37349036312     PISSN: 17401526     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrmicro1795     Document Type: Review
Times cited : (95)

References (128)
  • 1
    • 0037172980 scopus 로고    scopus 로고
    • Evidence that subcellular localization of a bacterial membrane protein is achieved by diffusion and capture
    • Rudner, D. Z., Pan, O. & Losick, R. M. Evidence that subcellular localization of a bacterial membrane protein is achieved by diffusion and capture. Proc. Natl Acad. Sci. USA 99, 8701-8706 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 8701-8706
    • Rudner, D.Z.1    Pan, O.2    Losick, R.M.3
  • 2
    • 8644231698 scopus 로고    scopus 로고
    • Visualization of the movement of single histidine kinase molecules in live Caulobacter cells
    • Deich, J., Judd, E. M., McAdams, H. H. & Moerner, W. E. Visualization of the movement of single histidine kinase molecules in live Caulobacter cells. Proc. Natl Acad. Sci. USA 101, 15921-15926 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 15921-15926
    • Deich, J.1    Judd, E.M.2    McAdams, H.H.3    Moerner, W.E.4
  • 3
    • 21844441637 scopus 로고    scopus 로고
    • Diverse paths to midcell: Assembly of the bacterial cell division machinery
    • Goehring, N. W. & Beckwith, J. Diverse paths to midcell: Assembly of the bacterial cell division machinery. Curr. Biol. 15, 11514-11526 (2005).
    • (2005) Curr. Biol , vol.15 , pp. 11514-11526
    • Goehring, N.W.1    Beckwith, J.2
  • 4
    • 2342640965 scopus 로고    scopus 로고
    • Septal localization of forespore membrane proteins during engulfment in Bacillus subtilis
    • Rubio, A. & Pogliano, K. Septal localization of forespore membrane proteins during engulfment in Bacillus subtilis. EMBO J. 23, 1636-1646 (2004).
    • (2004) EMBO J , vol.23 , pp. 1636-1646
    • Rubio, A.1    Pogliano, K.2
  • 5
    • 10044268409 scopus 로고    scopus 로고
    • Zipper-like interaction between proteins in adjacent daughter cells mediates protein localization
    • Blaylock, B., Jiang, X., Rubio, A., Moran, C. P. Jr. & Pogliano, K. Zipper-like interaction between proteins in adjacent daughter cells mediates protein localization. Genes Dev. 18, 2916-2928 (2004).
    • (2004) Genes Dev , vol.18 , pp. 2916-2928
    • Blaylock, B.1    Jiang, X.2    Rubio, A.3    Moran Jr., C.P.4    Pogliano, K.5
  • 6
    • 14744274820 scopus 로고    scopus 로고
    • Subcellular localization of a sporulation membrane protein is achieved through a network of interactions along and across the septum
    • Doan, T., Marquis, K. A. & Rudner. D. Z. Subcellular localization of a sporulation membrane protein is achieved through a network of interactions along and across the septum. Mol. Microbiol. 55 1767-1781 (2005).
    • (2005) Mol. Microbiol , vol.55 , pp. 1767-1781
    • Doan, T.1    Marquis, K.A.2    Rudner, D.Z.3
  • 8
    • 21844459467 scopus 로고    scopus 로고
    • Localization of translocation complex components in Bacillus subtills: Enrichment of the signal recognition particle receptor at early sporulation septa
    • Rubio, A., Jiang, X. & Pogliano, K. Localization of translocation complex components in Bacillus subtills: Enrichment of the signal recognition particle receptor at early sporulation septa. J. Bacteriol. 187, 5000-5002 (2005).
    • (2005) J. Bacteriol , vol.18 , Issue.7 , pp. 5000-5002
    • Rubio, A.1    Jiang, X.2    Pogliano, K.3
  • 9
    • 0032920830 scopus 로고    scopus 로고
    • The unipolar Shigella surface protein IcsA is targeted directly to the bacterial old pole: IcsP cleavage of IcsA occurs over the entire bacterial surface
    • Steinhauer, J., Agha, R., Pham, T, Varga. A. W. & Goldberg, M. B. The unipolar Shigella surface protein IcsA is targeted directly to the bacterial old pole: IcsP cleavage of IcsA occurs over the entire bacterial surface. Mol. Microbiol. 32, 367-377 (1999).
    • (1999) Mol. Microbiol , vol.32 , pp. 367-377
    • Steinhauer, J.1    Agha, R.2    Pham, T.3    Varga, A.W.4    Goldberg, M.B.5
  • 10
    • 0035859884 scopus 로고    scopus 로고
    • Polar targeting of Shigella virulence factor IcsA in Enterobacteriacae and Vibrio
    • Charles, M., Perez, M., Kobil, J. H. & Goldberg, M. B. Polar targeting of Shigella virulence factor IcsA in Enterobacteriacae and Vibrio. Proc. Natl Acad. Sci. USA 98, 9871-9876 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 9871-9876
    • Charles, M.1    Perez, M.2    Kobil, J.H.3    Goldberg, M.B.4
  • 11
    • 0141484348 scopus 로고    scopus 로고
    • IcsA, a polarly localized autotransporter with an atypical signal pepticle. uses the Sec apparatus for secretion, although the Sec apparatus is circumferentially distributed
    • Brandon, L. D. et al. IcsA, a polarly localized autotransporter with an atypical signal pepticle. uses the Sec apparatus for secretion, although the Sec apparatus is circumferentially distributed. Mol. Microbiol. 50, 45-60 (2003).
    • (2003) Mol. Microbiol , vol.50 , pp. 45-60
    • Brandon, L.D.1
  • 12
    • 0035937396 scopus 로고    scopus 로고
    • Control of cell shape in bacteria: Helical. actin-like filaments in Bacillus subtilis
    • Jones, L J.. Carballido-Lopez, R. & Errington, J. Control of cell shape in bacteria: Helical. actin-like filaments in Bacillus subtilis. Cell 104, 913-922 (2001).
    • (2001) Cell , vol.104 , pp. 913-922
    • Jones, L.J.1    Carballido-Lopez, R.2    Errington, J.3
  • 13
    • 4444285310 scopus 로고    scopus 로고
    • Dynamic movement of actin-like proteins within bacterial cells
    • 789-794
    • Defeu Soufo, H. J. & Graumann, P. L. Dynamic movement of actin-like proteins within bacterial cells. EMBO Rep. 5, 789-794 (2004).
    • (2004) EMBO Rep , vol.5
    • Defeu Soufo, H.J.1    Graumann, P.L.2
  • 14
    • 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., Le, T. & Rothfield. L. 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. USA 100, 7865-7870 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 7865-7870
    • Shih, Y.L.1    Le, T.2    Rothfield, L.3
  • 15
    • 1542616355 scopus 로고    scopus 로고
    • MreB, the cell shape-determining bacterial actin homologue, co-ordinates cell wall morphogenesis in Caulobocter crescentus
    • Figge, R. M., Divakaruni, A. V. & Gober. J. W. MreB, the cell shape-determining bacterial actin homologue, co-ordinates cell wall morphogenesis in Caulobocter crescentus. Mol. Microbiol. 51, 1321-1332 (2004).
    • (2004) Mol. Microbiol , vol.51 , pp. 1321-1332
    • Figge, R.M.1    Divakaruni, A.V.2    Gober, J.W.3
  • 16
    • 2942588534 scopus 로고    scopus 로고
    • An actin-like gene can determine cell polarity in bacteria
    • Gitai. Z., Dye, N. & Shapiro, L. An actin-like gene can determine cell polarity in bacteria. Proc. Natl Acad. Sci. USA 101, 8643-8648 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 8643-8648
    • Gitai, Z.1    Dye, N.2    Shapiro, L.3
  • 17
    • 13544274210 scopus 로고    scopus 로고
    • MreB actin-mediated segregation of a specific region of a bacterial chromosome
    • Gitai, Z., Dye, N. A., Reisenauer. A., Wachi, M. & Shapiro, L. MreB actin-mediated segregation of a specific region of a bacterial chromosome. Cell 120, 329-341 (2005).
    • (2005) Cell , vol.120 , pp. 329-341
    • Gitai, Z.1    Dye, N.A.2    Reisenauer, A.3    Wachi, M.4    Shapiro, L.5
  • 18
    • 29944438325 scopus 로고    scopus 로고
    • Actin homolog MreB and RNA polymerase interact and are both required for chromosome segregation in Escherichia coli
    • Kruse, T et al. Actin homolog MreB and RNA polymerase interact and are both required for chromosome segregation in Escherichia coli. Genes Dev. 20, 113-124 (2006).
    • (2006) Genes Dev , vol.20 , pp. 113-124
    • Kruse, T.1
  • 19
    • 34247644614 scopus 로고    scopus 로고
    • Regulation of actin filament assembly by arp2/3 complex and formins
    • Pollard, T. D. Regulation of actin filament assembly by arp2/3 complex and formins. Annu. Rev. Biophys. Biomol. Struct. 36, 451-477 (2007).
    • (2007) Annu. Rev. Biophys. Biomol. Struct , vol.36 , pp. 451-477
    • Pollard, T.D.1
  • 20
    • 31344480941 scopus 로고    scopus 로고
    • GTPase activity, structure, and mechanical properties of filaments assembled from bacterial cytoskeleton protein MreB
    • Esue, O., Wirtz, D. & Iseng, Y. GTPase activity, structure, and mechanical properties of filaments assembled from bacterial cytoskeleton protein MreB. J. Bacteriol. 188, 968-976 (2006).
    • (2006) J. Bacteriol , vol.188 , pp. 968-976
    • Esue, O.1    Wirtz, D.2    Iseng, Y.3
  • 21
    • 0035817819 scopus 로고    scopus 로고
    • Prokaryotic origin of the actin cytoskeleton
    • van den Ent, F., Amos. L. A. & Löwe, J. Prokaryotic origin of the actin cytoskeleton. Nature 413, 39-44 (2001).
    • (2001) Nature , vol.413 , pp. 39-44
    • van den Ent, F.1    Amos, L.A.2    Löwe, J.3
  • 22
    • 13244278205 scopus 로고    scopus 로고
    • The assembly of MreB. a prokaryotic homolog of actin
    • Esue, O., Cordero, M., Wirtz, D. & Tseng, Y. The assembly of MreB. a prokaryotic homolog of actin. J. Biol. Chem. 280, 2628-2635 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 2628-2635
    • Esue, O.1    Cordero, M.2    Wirtz, D.3    Tseng, Y.4
  • 23
    • 0037237123 scopus 로고    scopus 로고
    • The bacterial cytoskeleton: In vivo dynamics of the actin-like protein Mb1 of Bacillus subtilis
    • Carballido-Lopez, R. & Errington, J. The bacterial cytoskeleton: in vivo dynamics of the actin-like protein Mb1 of Bacillus subtilis. Dev. Cell 4, 19-28 (2003).
    • (2003) Dev. Cell , vol.4 , pp. 19-28
    • Carballido-Lopez, R.1    Errington, J.2
  • 24
    • 11144257131 scopus 로고    scopus 로고
    • Localization of MreB in Rhodobacter sphaeroides under conditions causing changes in cell shape and membrane structure
    • Slovak, P. M., Wadhams, G. H. & Armitage, J. P. Localization of MreB in Rhodobacter sphaeroides under conditions causing changes in cell shape and membrane structure. J. Bacteriol. 187, 54-64 (2005).
    • (2005) J. Bacteriol , vol.187 , pp. 54-64
    • Slovak, P.M.1    Wadhams, G.H.2    Armitage, J.P.3
  • 25
    • 33644776090 scopus 로고    scopus 로고
    • Differential localization of Mre proteins with PBP2 in Rhodobacter sphaeroides
    • Slovak, P. M., Porter, S. L. & Armitage, J. P. Differential localization of Mre proteins with PBP2 in Rhodobacter sphaeroides. J. Bacteriol. 188. 1691-1700 (2006).
    • (2006) J. Bacteriol , vol.188 , pp. 1691-1700
    • Slovak, P.M.1    Porter, S.L.2    Armitage, J.P.3
  • 26
    • 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. & Graumann, P. L. Dynamic localization and interaction with other Bacillus subtilis actin-like proteins are important for the function of MreB. Mol. Microbiol. 62, 1340-1356 (2006).
    • (2006) Mol. Microbiol , vol.62 , pp. 1340-1356
    • Defeu Soufo, H.J.1    Graumann, P.L.2
  • 27
    • 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, 399-409 (2006).
    • (2006) Dev. Cell , vol.11 , pp. 399-409
    • Carballido-Lopez, R.1
  • 28
    • 33746655349 scopus 로고    scopus 로고
    • Single molecules of the bacterial actin MreB undergo directed treadmilling motion in Caulobacter crescentus
    • Kim, S. Y., Gitai, Z., Kinkhabwala, A., Shapiro, L & Moerner, W. E. Single molecules of the bacterial actin MreB undergo directed treadmilling motion in Caulobacter crescentus. Proc Natl Acad Sci USA 103, 10929-10934 (2006).
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 10929-10934
    • Kim, S.Y.1    Gitai, Z.2    Kinkhabwala, A.3    Shapiro, L.4    Moerner, W.E.5
  • 29
    • 12344306119 scopus 로고    scopus 로고
    • The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex
    • Kruse, T., Bork-Jensen, J. & Gerdes, K. The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex. Mol. Microbiol. 55, 78-89 (2005).
    • (2005) Mol. Microbiol , vol.55 , pp. 78-89
    • Kruse, T.1    Bork-Jensen, J.2    Gerdes, K.3
  • 30
    • 33751363915 scopus 로고    scopus 로고
    • Dimeric structure of the cell shape protein MreC and its functional implications
    • van den Ent, F. et al. Dimeric structure of the cell shape protein MreC and its functional implications. Mol Microbiol. 62, 1631-1642 (2006).
    • (2006) Mol Microbiol , vol.62 , pp. 1631-1642
    • van den Ent, F.1
  • 31
    • 29344476196 scopus 로고    scopus 로고
    • The cell-shape protein MreC interacts with extracytoplasmic proteins including cell wall assembly complexes in Couldbacter crescentus
    • Divakaruni, A. V., Loo, R. R., Xie, Y.. Loo, J. A. & Gober, J. W. The cell-shape protein MreC interacts with extracytoplasmic proteins including cell wall assembly complexes in Couldbacter crescentus. Proc. Natl Acad. Sci. USA 102, 18602-18607 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 18602-18607
    • Divakaruni, A.V.1    Loo, R.R.2    Xie, Y.3    Loo, J.A.4    Gober, J.W.5
  • 32
    • 0038782140 scopus 로고    scopus 로고
    • Essential nature of the mreC determinant of Bacillus subtilis
    • Lee, J. C. & Stewart, G. C. Essential nature of the mreC determinant of Bacillus subtilis. J. Bacteriol. 185, 4490-4498 (2003).
    • (2003) J. Bacteriol , vol.185 , pp. 4490-4498
    • Lee, J.C.1    Stewart, G.C.2
  • 33
    • 23844444807 scopus 로고    scopus 로고
    • Roles for MreC and MreD proteins in helical growth ofthe cylindrical cell wall in Bacillus subtilis
    • Leaver, M. & Errington, J. Roles for MreC and MreD proteins in helical growth ofthe cylindrical cell wall in Bacillus subtilis. Mol. Microbiol. 57, 1196-1209 (2005).
    • (2005) Mol. Microbiol , vol.57 , pp. 1196-1209
    • Leaver, M.1    Errington, J.2
  • 34
    • 0242381270 scopus 로고    scopus 로고
    • Actin-like proteins MreB and Mbl from Bacillus subtilis are required for bipolar positioning of replication origins
    • Soufo, H. J. & Graumann, P. L. Actin-like proteins MreB and Mbl from Bacillus subtilis are required for bipolar positioning of replication origins. Curr. Biol. 13, 1916-1920 (2003).
    • (2003) Curr. Biol , vol.13 , pp. 1916-1920
    • Soufo, H.J.1    Graumann, P.L.2
  • 36
    • 0346020436 scopus 로고    scopus 로고
    • The bacterial cytoskeleton: An intermediate filament-like function in cell shape
    • Ausmees, N., Kuhn, J. R. & Jacobs-Wagner. C. The bacterial cytoskeleton: an intermediate filament-like function in cell shape, Cell 115 705-713 (2003).
    • (2003) Cell , vol.115 , pp. 705-713
    • Ausmees, N.1    Kuhn, J.R.2    Jacobs-Wagner, C.3
  • 37
    • 34249750035 scopus 로고    scopus 로고
    • Towards a molecular description of intermediate filament structure and assembly
    • Parry D. A., Strelkov, S. V., Burkhard, P., Aebi, U. & Herrmann, H. Towards a molecular description of intermediate filament structure and assembly. Exp. Cell Res. 313, 2204-2216 (2007).
    • (2007) Exp. Cell Res , vol.313 , pp. 2204-2216
    • Parry, D.A.1    Strelkov, S.V.2    Burkhard, P.3    Aebi, U.4    Herrmann, H.5
  • 38
    • 34248364322 scopus 로고    scopus 로고
    • The tubulin homologue FtsZ contributes to cell elongation by guiding cell wall precursor synthesis in Caulobacter crescentus
    • Aaron, M. et al. The tubulin homologue FtsZ contributes to cell elongation by guiding cell wall precursor synthesis in Caulobacter crescentus. Mol. Microbiol. 64, 938-952 (2007).
    • (2007) Mol. Microbiol , vol.64 , pp. 938-952
    • Aaron, M.1
  • 39
    • 34548677525 scopus 로고    scopus 로고
    • The cell shape proteins MreB and MreC control cell morphogenesis by positioning cell wall synthetic complexes
    • Divakaruni, A. V., Saida, C., White, C. L & Gober, J. W. The cell shape proteins MreB and MreC control cell morphogenesis by positioning cell wall synthetic complexes. Mol Microbiol. 66, 174-188 (2007).
    • (2007) Mol Microbiol , vol.66 , pp. 174-188
    • Divakaruni, A.V.1    Saida, C.2    White, C.L.3    Gober, J.W.4
  • 40
    • 34547651288 scopus 로고    scopus 로고
    • The essential peptidoglycan glycosyltransferase MurG forms a complex with proteins involved in lateral envelope growth as well as with proteins involved in cell division in Escherichia coli
    • Mohammadi, T. et al. The essential peptidoglycan glycosyltransferase MurG forms a complex with proteins involved in lateral envelope growth as well as with proteins involved in cell division in Escherichia coli. Mol. Microbiol. 65, 1106-1121 (2007).
    • (2007) Mol. Microbiol , vol.65 , pp. 1106-1121
    • Mohammadi, T.1
  • 41
    • 0036034803 scopus 로고    scopus 로고
    • The P1 plasmid is segregated to daughter cells by a 'capture and ejection', mechanism coordinated with Escherichia coli cell division
    • Li, Y. & Austin, S. The P1 plasmid is segregated to daughter cells by a 'capture and ejection', mechanism coordinated with Escherichia coli cell division. Mol. Microbiol. 46, 63-74 (2002).
    • (2002) Mol. Microbiol , vol.46 , pp. 63-74
    • Li, Y.1    Austin, S.2
  • 42
    • 0942301205 scopus 로고    scopus 로고
    • Kinetics of plasmid segregation in Escherichia coli
    • Gordon, S., Rech, J., Lane, D. & Wright, A. Kinetics of plasmid segregation in Escherichia coli. Mol. Microbiol. 51, 461-469 (2004).
    • (2004) Mol. Microbiol , vol.51 , pp. 461-469
    • Gordon, S.1    Rech, J.2    Lane, D.3    Wright, A.4
  • 43
    • 1942468854 scopus 로고    scopus 로고
    • Bacterial mitosis: Partitioning protein ParA oscillates in spiral-shaped structures and positions plasmids at mid-cell
    • Ebersbach, G. & Gerdes, K. Bacterial mitosis: Partitioning protein ParA oscillates in spiral-shaped structures and positions plasmids at mid-cell. Mol. Microbiol. 52, 385-398 (2004).
    • (2004) Mol. Microbiol , vol.52 , pp. 385-398
    • Ebersbach, G.1    Gerdes, K.2
  • 44
    • 0037007199 scopus 로고    scopus 로고
    • Compatible bacterial plasmids are targeted to independent cellular locations in Escherichia coli
    • Ho, T. Q., Zhong, Z., Aung, S. & Pogliano, J. Compatible bacterial plasmids are targeted to independent cellular locations in Escherichia coli. EMBO J. 21, 1864-1872 (2002).
    • (2002) EMBO J , vol.21 , pp. 1864-1872
    • Ho, T.Q.1    Zhong, Z.2    Aung, S.3    Pogliano, J.4
  • 45
    • 0030768426 scopus 로고    scopus 로고
    • Subcellular distribution of actively partitioning F plasmid during the cell division cycle in E. coli
    • Niki, H. & Hiraga. S. Subcellular distribution of actively partitioning F plasmid during the cell division cycle in E. coli. Cell 90 951-957 (1997).
    • (1997) Cell , vol.90 , pp. 951-957
    • Niki, H.1    Hiraga, S.2
  • 46
    • 0030928717 scopus 로고    scopus 로고
    • Chromosome-and low copy plasmid segregation in E. coli: Visual evidence for distinct mechanisms
    • Gordon, G. S. et al. Chromosome-and low copy plasmid segregation in E. coli: Visual evidence for distinct mechanisms. Cell 90, 1113-1121 (1997).
    • (1997) Cell , vol.90 , pp. 1113-1121
    • Gordon, G.S.1
  • 47
    • 0028222812 scopus 로고
    • Partitioning of plasmid R1. Ten direct repeats flanking the par A promoter constitute a centromere-like partition site parC, that expresses incompatibility
    • Dam, M. & Gerdes, K. Partitioning of plasmid R1. Ten direct repeats flanking the par A promoter constitute a centromere-like partition site parC, that expresses incompatibility. J. Mol Biol. 236, 1289-1298 (1994).
    • (1994) J. Mol Biol , vol.236 , pp. 1289-1298
    • Dam, M.1    Gerdes, K.2
  • 48
    • 0346980557 scopus 로고    scopus 로고
    • Bacterial mitosis: ParM of plasmid R1 moves plasmid DNA by an actin-like insertional polymerization mechanism
    • Møller-Jensen, J. et al. Bacterial mitosis: ParM of plasmid R1 moves plasmid DNA by an actin-like insertional polymerization mechanism. Mol Cell 12, 1477-1487 (2003).
    • (2003) Mol Cell , vol.12 , pp. 1477-1487
    • Møller-Jensen, J.1
  • 49
    • 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. & 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, 505-513 (1997).
    • (1997) J. Mol. Biol , vol.269 , pp. 505-513
    • Jensen, R.B.1    Gerdes, K.2
  • 50
    • 12244298896 scopus 로고    scopus 로고
    • F-actin-like filaments formed by plasmid segregation protein ftrM
    • van den Ent, F., Møller-Jensen, J., Amos, L A., Gerdes, K & Löwe. J. F-actin-like filaments formed by plasmid segregation protein ftrM. EABO J. 21, 6935-6943 (2002).
    • (2002) EABO J , vol.21 , pp. 6935-6943
    • van den Ent, F.1    Møller-Jensen, J.2    Amos, L.A.3    Gerdes, K.4    Löwe, J.5
  • 51
    • 0037124325 scopus 로고    scopus 로고
    • Prokaryotic DNA segregation by an actin-like filament
    • Møller-Jensen, J., Jensen, R. B., Löwe, J. & Gerdes, K. Prokaryotic DNA segregation by an actin-like filament. EMBO J. 21, 3119-3127 (2002).
    • (2002) EMBO J , vol.21 , pp. 3119-3127
    • Møller-Jensen, J.1    Jensen, R.B.2    Löwe, J.3    Gerdes, K.4
  • 52
    • 8344247018 scopus 로고    scopus 로고
    • Dynamic instability in a DNA-segregating prokaryotic actin homolog
    • Garner, E. C., Campbell. C. S. & Mullins, R. D. Dynamic instability in a DNA-segregating prokaryotic actin homolog. Science 306, 1021-1025 (2004).
    • (2004) Science , vol.306 , pp. 1021-1025
    • Garner, E.C.1    Campbell, C.S.2    Mullins, R.D.3
  • 53
    • 33847675333 scopus 로고    scopus 로고
    • Reconstitution at DNA segregation driven by assembly of a prokaryotic actin homolog
    • Garner, E. C., Campbell, C. S., Weibel, D. B, & Mullins, R. D. Reconstitution at DNA segregation driven by assembly of a prokaryotic actin homolog. Science 315, 1270-1274 (2007).
    • (2007) Science , vol.315 , pp. 1270-1274
    • Garner, E.C.1    Campbell, C.S.2    Weibel, D.B.3    Mullins, R.D.4
  • 54
    • 0021686169 scopus 로고
    • Dynamic instability of microtubule growth
    • Mitchison, T. & Kirschner, M. Dynamic instability of microtubule growth. Nature 312, 237-242 (1984).
    • (1984) Nature , vol.312 , pp. 237-242
    • Mitchison, T.1    Kirschner, M.2
  • 55
    • 33845772164 scopus 로고    scopus 로고
    • DNA segregation by the bacterial actin AIFA during Bacillus subtilis growth and development
    • Becker, E. et al. DNA segregation by the bacterial actin AIFA during Bacillus subtilis growth and development. EMBO J. 25, 5919-5931 (2006).
    • (2006) EMBO J , vol.25 , pp. 5919-5931
    • Becker, E.1
  • 56
    • 33746358181 scopus 로고    scopus 로고
    • Dynamic filaments of the bacterial cytoskeleton
    • Michie. K. A. & Löwe. J. Dynamic filaments of the bacterial cytoskeleton. Annu. Rev. Biochem. 75, 467-492 (2006).
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 467-492
    • Michie, K.A.1    Löwe, J.2
  • 57
    • 29444437147 scopus 로고    scopus 로고
    • Plasmid segregation mechanisms
    • Ebersbach. G. & Gerdes, K. Plasmid segregation mechanisms. Annu. Rev. Ganet. 39, 453-479 (2005).
    • (2005) Annu. Rev. Ganet , vol.39 , pp. 453-479
    • Ebersbach, G.1    Gerdes, K.2
  • 58
    • 31544463593 scopus 로고    scopus 로고
    • The bacterial segrosome: A dynamic nucleoprotein machine far DNA trafficking and segregation
    • Hayes, F. & Barilla. D. The bacterial segrosome: A dynamic nucleoprotein machine far DNA trafficking and segregation. Nature Rev. Microbiol. 4, 133-143 (2006).
    • (2006) Nature Rev. Microbiol , vol.4 , pp. 133-143
    • Hayes, F.1    Barilla, D.2
  • 59
    • 20544475284 scopus 로고    scopus 로고
    • Towards understanding the molecular basis of bacterial DNA segregation
    • Leonard, T A., Møller-Jensen, J. & Löwe, J. Towards understanding the molecular basis of bacterial DNA segregation. Philos. Trans. R. Soc. Lond. B 360, 523-535 (2005).
    • (2005) Philos. Trans. R. Soc. Lond. B , vol.360 , pp. 523-535
    • Leonard, T.A.1    Møller-Jensen, J.2    Löwe, J.3
  • 60
    • 0035910030 scopus 로고    scopus 로고
    • The double par locus of virulence factor pB 171: DNA segregation is correlated with oscillation of ParA
    • Ebersbach, G. & Gerdes, K. The double par locus of virulence factor pB 171: DNA segregation is correlated with oscillation of ParA. Proc. Natl Acad. Sci. US4 98, 15078-15083 (2001).
    • (2001) Proc. Natl Acad. Sci , vol.US4 , Issue.98 , pp. 15078-15083
    • Ebersbach, G.1    Gerdes, K.2
  • 61
    • 29144454213 scopus 로고    scopus 로고
    • Bacterial DNA segregation by dynamic SopA polymers
    • Lim, G. E., Derman, A. I. & Pogliano. J. Bacterial DNA segregation by dynamic SopA polymers. Proc. Natl Acad. Sci USA 102, 17658-17663 (2005).
    • (2005) Proc. Natl Acad. Sci USA , vol.102 , pp. 17658-17663
    • Lim, G.E.1    Derman, A.I.2    Pogliano, J.3
  • 62
    • 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, 1428-11442 (2006).
    • (2006) Mol. Microbiol , vol.61 , pp. 1428-11442
    • Ebersbach, G.1
  • 63
    • 33744485810 scopus 로고    scopus 로고
    • The positioning of cytoplasmic protein clusters in bacteria
    • Thompson, S. R., Wadhams, G. H. & Armitage, J. P. The positioning of cytoplasmic protein clusters in bacteria. Proc Natl Acad. Sci. US4 103, 8209-8214 (2006).
    • (2006) Proc Natl Acad. Sci , vol.US4 , Issue.103 , pp. 8209-8214
    • Thompson, S.R.1    Wadhams, G.H.2    Armitage, J.P.3
  • 64
    • 33750979309 scopus 로고    scopus 로고
    • Minireplicon from pBtoxis of Bacillus thuringiensis subsp. israelensis
    • Tang, M. Bideshi. D. K., Park. H. W. & Federici, B. A. Minireplicon from pBtoxis of Bacillus thuringiensis subsp. israelensis. Appl. Environmen. Microbiol. 72, 6948-6954 (2006).
    • (2006) Appl. Environmen. Microbiol , vol.72 , pp. 6948-6954
    • Tang, M.1    Bideshi, D.K.2    Park, H.W.3    Federici, B.A.4
  • 65
    • 34249897760 scopus 로고    scopus 로고
    • treadmilling of a prokaryotic tubulin-like protein, 70bZ, required for plasmid stability in Bacillius thuringiensis
    • Larsen, R. A. et al. treadmilling of a prokaryotic tubulin-like protein, 70bZ, required for plasmid stability in Bacillius thuringiensis. Genes Dev. 21, 1340-1352 (2007).
    • (2007) Genes Dev , vol.21 , pp. 1340-1352
    • Larsen, R.A.1
  • 66
    • 18044363711 scopus 로고    scopus 로고
    • The choreographec dynamics of bacterial chromosomes
    • Gitai, Z., Thanbichler, M. & Shapiro, L. The choreographec dynamics of bacterial chromosomes. Trenda Microbiol. 13, 221-228 (2005).
    • (2005) Trenda Microbiol , vol.13 , pp. 221-228
    • Gitai, Z.1    Thanbichler, M.2    Shapiro, L.3
  • 67
    • 27144448812 scopus 로고    scopus 로고
    • The bacterial nucleoid: A highly organized and dynamic structure
    • Thanbichler, W., Wang, S. C. & Shapiro, L. The bacterial nucleoid: A highly organized and dynamic structure. J. Cell. Biochem. 96 506-521.(2005).
    • (2005) J. Cell. Biochem , vol.96 , pp. 506-521
    • Thanbichler, W.1    Wang, S.C.2    Shapiro, L.3
  • 69
    • 3042548402 scopus 로고    scopus 로고
    • Rapid and sequential movement of individual chromosomal loci to specific subcellular locations during bacterial DNA replication
    • Viollier, P. H. et al. Rapid and sequential movement of individual chromosomal loci to specific subcellular locations during bacterial DNA replication. Proc. Natl Acad. Sci. USA, 101, 9257-9262 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 9257-9262
    • Viollier, P.H.1
  • 70
    • 33745603713 scopus 로고    scopus 로고
    • The two Escherichia coli chromosome arms locate to separate cell halves
    • Wang, X, Liu, X., Possoz. C. & Sherratt, D. J. The two Escherichia coli chromosome arms locate to separate cell halves. Genes Dev. 20, 1727-1731 (2006).
    • (2006) Genes Dev , vol.20 , pp. 1727-1731
    • Wang, X.1    Liu, X.2    Possoz, C.3    Sherratt, D.J.4
  • 71
    • 33749177128 scopus 로고    scopus 로고
    • The Escherichia coli chromosome is organized with the left and right chromosome arms in separate cell halves
    • Nielsen, H.J., Ottesen, J. R., Youngren, B. Austin, S. J. & Hansen, F. G. The Escherichia coli chromosome is organized with the left and right chromosome arms in separate cell halves. Mol. Microbiol. 62, 331-338 (2006).
    • (2006) Mol. Microbiol , vol.62 , pp. 331-338
    • Nielsen, H.J.1    Ottesen, J.R.2    Youngren, B.3    Austin, S.J.4    Hansen, F.G.5
  • 72
    • 0032875384 scopus 로고    scopus 로고
    • The Caulobacter crescentus smc gene is required for cell cycle progression and chromosome segregation
    • Jensen, R. B. & Shapiro, L. The Caulobacter crescentus smc gene is required for cell cycle progression and chromosome segregation. Proc Natl Acad. Sci. USA 96, 10661-10666 (1999).
    • (1999) Proc Natl Acad. Sci. USA , vol.96 , pp. 10661-10666
    • Jensen, R.B.1    Shapiro, L.2
  • 73
    • 0036433665 scopus 로고    scopus 로고
    • The segregation of the Escherichia coli origin and terminus of replication
    • Li, Y., Sergueev, K. & Austin, S. The segregation of the Escherichia coli origin and terminus of replication. Mol. Microbiol. 46 985-996 (2002).
    • (2002) Mol. Microbiol , vol.46 , pp. 985-996
    • Li, Y.1    Sergueev, K.2    Austin, S.3
  • 74
    • 0035138267 scopus 로고    scopus 로고
    • The replicated ftsQAZ and minB chromosomal regions of Escherichia coli segregate on average in line with nucleoid movement
    • Roos, M. et al. The replicated ftsQAZ and minB chromosomal regions of Escherichia coli segregate on average in line with nucleoid movement. Mol. Microbiol. 39, 633-640 (2001).
    • (2001) Mol. Microbiol , vol.39 , pp. 633-640
    • Roos, M.1
  • 75
    • 0034650256 scopus 로고    scopus 로고
    • Dynamic organization of chromosomal DNA in Escherichia coli
    • Niki, H., Yamaichi, Y. & Hiraga, S. Dynamic organization of chromosomal DNA in Escherichia coli. Genes Dev. 14, 212-223 (2000).
    • (2000) Genes Dev , vol.14 , pp. 212-223
    • Niki, H.1    Yamaichi, Y.2    Hiraga, S.3
  • 76
  • 77
    • 33750531252 scopus 로고    scopus 로고
    • Chromosome organization and segregation in bacteria
    • Thanbichler, M. & Shapiro, L. Chromosome organization and segregation in bacteria. J. Struct. Biol. 156, 292-303 (2006).
    • (2006) J. Struct. Biol , vol.156 , pp. 292-303
    • Thanbichler, M.1    Shapiro, L.2
  • 79
    • 0031834480 scopus 로고    scopus 로고
    • Use of time-lapse microscopy to visualize rapid movement of the replication origin region of the chromosome during the cell cycle in Bacillus subtilis
    • Webb, C. D. et al. Use of time-lapse microscopy to visualize rapid movement of the replication origin region of the chromosome during the cell cycle in Bacillus subtilis. Mol. Microbiol. 28, 883-892 (1998).
    • (1998) Mol. Microbiol , vol.28 , pp. 883-892
    • Webb, C.D.1
  • 80
    • 33745288732 scopus 로고    scopus 로고
    • Fine-scale time-lapse analysis of the biphasic, dynamic behaviour of the two Vibrio cholerae chromosomes
    • Fiebig, A., Keren, K. & Theriot, J. A. Fine-scale time-lapse analysis of the biphasic, dynamic behaviour of the two Vibrio cholerae chromosomes. Mol. Microbiol. 60, 1164-1178 (2006).
    • (2006) Mol. Microbiol , vol.60 , pp. 1164-1178
    • Fiebig, A.1    Keren, K.2    Theriot, J.A.3
  • 81
    • 0141864658 scopus 로고    scopus 로고
    • Dysfunctional MreB inhibits chromosome segregation in Escherichia coli
    • Kruse, T., Møller-Jensen, J., Løbner-Olesen, A. & Gerdes, K. Dysfunctional MreB inhibits chromosome segregation in Escherichia coli. EMBO J. 22, 5283-5292 (2003).
    • (2003) EMBO J , vol.22 , pp. 5283-5292
    • Kruse, T.1    Møller-Jensen, J.2    Løbner-Olesen, A.3    Gerdes, K.4
  • 83
    • 0032489548 scopus 로고    scopus 로고
    • Identification and characterization of a bacterial chromosome partitioning site
    • Lin, D. C. & Grossman, A. D. Identification and characterization of a bacterial chromosome partitioning site. Cell 92, 675-685 (1998).
    • (1998) Cell , vol.92 , pp. 675-685
    • Lin, D.C.1    Grossman, A.D.2
  • 84
    • 34247497733 scopus 로고    scopus 로고
    • Whole-genome analysis of the chromosome partitioning and sporulation protein SpoOJ (ParB) reveals spreading and origin-distal sites on the Bacillus subtilis chromosome
    • Breier, A. M. & Grossman, A. D. Whole-genome analysis of the chromosome partitioning and sporulation protein SpoOJ (ParB) reveals spreading and origin-distal sites on the Bacillus subtilis chromosome. Mol. Microbiol. 64, 703-718 (2007).
    • (2007) Mol. Microbiol , vol.64 , pp. 703-718
    • Breier, A.M.1    Grossman, A.D.2
  • 85
    • 33747067108 scopus 로고    scopus 로고
    • The bacterial chromosome segregation protein SpoOJ spreads along DNA from parS nucleation sites
    • Murray, H., Ferreira, H. & Errington, J. The bacterial chromosome segregation protein SpoOJ spreads along DNA from parS nucleation sites. Mol. Microbiol. 61, 1352-1361 (2006).
    • (2006) Mol. Microbiol , vol.61 , pp. 1352-1361
    • Murray, H.1    Ferreira, H.2    Errington, J.3
  • 86
    • 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. & 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, 673-682 (1999).
    • (1999) Mol. Cell , vol.4 , pp. 673-682
    • Marston, A.L.1    Errington, J.2
  • 87
    • 0034687751 scopus 로고    scopus 로고
    • Active segregation by the Bacillus subtilis partitioning system in Escherichia coli
    • Yamaichi, Y. & Niki, H. Active segregation by the Bacillus subtilis partitioning system in Escherichia coli. Proc. Natl Acad. Sci. USA 97, 14656-14661 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 14656-14661
    • Yamaichi, Y.1    Niki, H.2
  • 88
    • 0036192533 scopus 로고    scopus 로고
    • Godfrin-Estevenon, A. M., Pasta, F. & Lane, D. The parAB gene products of Pseudomonas putida exhibit partition activity in both P. putida and Escherichia coli. Mol. Microbiol. 43, 39-49 (2002).
    • Godfrin-Estevenon, A. M., Pasta, F. & Lane, D. The parAB gene products of Pseudomonas putida exhibit partition activity in both P. putida and Escherichia coli. Mol. Microbiol. 43, 39-49 (2002).
  • 89
    • 0141677790 scopus 로고    scopus 로고
    • RacA and the Soj-SpoOJ system combine to effect polar chromosome segregation in sporulating Bacillus subtilis
    • Wu, L. J. & Errington, J. RacA and the Soj-SpoOJ system combine to effect polar chromosome segregation in sporulating Bacillus subtilis. Mol. Microbiol. 49, 1463-1475 (2003).
    • (2003) Mol. Microbiol , vol.49 , pp. 1463-1475
    • Wu, L.J.1    Errington, J.2
  • 90
    • 20144373037 scopus 로고    scopus 로고
    • Defining a centromere-like element in Bacillus subtilis by identifying the binding sites for the chromosome-anchoring protein RacA
    • Ben-Yehuda, S. et al. Defining a centromere-like element in Bacillus subtilis by identifying the binding sites for the chromosome-anchoring protein RacA. Mol. Cell 17, 773-782 (2005).
    • (2005) Mol. Cell , vol.17 , pp. 773-782
    • Ben-Yehuda, S.1
  • 91
    • 0037462540 scopus 로고    scopus 로고
    • RacA, a bacterial protein that anchors chromosomes to the cell poles
    • Ben-Yehuda, S., Rudner, D. Z. & Losick, R. RacA, a bacterial protein that anchors chromosomes to the cell poles. Science 299, 532-536 (2003).
    • (2003) Science , vol.299 , pp. 532-536
    • Ben-Yehuda, S.1    Rudner, D.Z.2    Losick, R.3
  • 92
    • 33646401543 scopus 로고    scopus 로고
    • The chromosome partitioning proteins Soj (ParA) and SpoOJ (ParB) contribute to accurate chromosome partitioning, separation of replicated sister origins, and regulation of replication initiation in Bacillus subtilis
    • Lee, P. S. & Grossman, A. D. The chromosome partitioning proteins Soj (ParA) and SpoOJ (ParB) contribute to accurate chromosome partitioning, separation of replicated sister origins, and regulation of replication initiation in Bacillus subtilis. Mol. Microbiol. 60, 853-869 (2006).
    • (2006) Mol. Microbiol , vol.60 , pp. 853-869
    • Lee, P.S.1    Grossman, A.D.2
  • 93
    • 12344338949 scopus 로고    scopus 로고
    • Distinct segregation dynamics of the two Vibrio cholerae chromosomes
    • Fogel, M. A. & Waldor, M. K. Distinct segregation dynamics of the two Vibrio cholerae chromosomes. Mol. Microbiol. 55, 125-136 (2005).
    • (2005) Mol. Microbiol , vol.55 , pp. 125-136
    • Fogel, M.A.1    Waldor, M.K.2
  • 94
    • 33845460999 scopus 로고    scopus 로고
    • A dynamic, mitotic-like mechanism for bacterial chromosome segregation
    • Fogel, M. A. & Waldor, M. K. A dynamic, mitotic-like mechanism for bacterial chromosome segregation. Genes Dev. 20, 3269-3282 (2006).
    • (2006) Genes Dev , vol.20 , pp. 3269-3282
    • Fogel, M.A.1    Waldor, M.K.2
  • 95
    • 2642593025 scopus 로고    scopus 로고
    • Crystal structure of the bacterial cell-division protein FtsZ
    • Löwe, J. Amos, L. A. Crystal structure of the bacterial cell-division protein FtsZ. Nature 391. 203-206(1998).
    • (1998) Nature , vol.391 , pp. 203-206
    • Löwe, J.1    Amos, L.A.2
  • 96
    • 34548630230 scopus 로고    scopus 로고
    • Assembly dynamics of the bacterial MinCDE system and spatial regulation of the Z ring
    • Lutkenhaus, J. Assembly dynamics of the bacterial MinCDE system and spatial regulation of the Z ring. Annu. Rev. Biochem. 76, 539-562 (2007).
    • (2007) Annu. Rev. Biochem , vol.76 , pp. 539-562
    • Lutkenhaus, J.1
  • 97
    • 7644219685 scopus 로고    scopus 로고
    • Bacterial cell division and the septal ring
    • Weiss, D. S. Bacterial cell division and the septal ring. Mol. Microbiol. 54, 588-597 (2004).
    • (2004) Mol. Microbiol , vol.54 , pp. 588-597
    • Weiss, D.S.1
  • 98
    • 0024977391 scopus 로고
    • A division inhibitor and a topological specificity factor coded for by the minicell locus determine proper placement of the division septum in E. coli
    • de Boer, P. A., Crossley, R. E. & Rothfield, L I. A division inhibitor and a topological specificity factor coded for by the minicell locus determine proper placement of the division septum in E. coli. Cell 56, 641-649 (1989).
    • (1989) Cell , vol.56 , pp. 641-649
    • de Boer, P.A.1    Crossley, R.E.2    Rothfield, L.I.3
  • 99
    • 0026039677 scopus 로고
    • The MinD protein is a membrane ATPase required for the correct placement of the Escherichia coli division site
    • de Boer, P. A. Crossley R. E., Hand, A. R. & Rothfield. L I. The MinD protein is a membrane ATPase required for the correct placement of the Escherichia coli division site. EMBO J. 10, 4371-4380 (1991).
    • (1991) EMBO J , vol.10 , pp. 4371-4380
    • de Boer, P.A.1    Crossley, R.E.2    Hand, A.R.3    Rothfield, L.I.4
  • 100
    • 0026585155 scopus 로고
    • Roles of MinC and MinD in the site-specific septation block mediated by the MinCDE system of Escherichia coli
    • de Boer, P. A., Crossley, R. E. & Rothfield, L I. Roles of MinC and MinD in the site-specific septation block mediated by the MinCDE system of Escherichia coli. J. Bacteriool. 174, 63-70 (1992).
    • (1992) J. Bacteriool , vol.174 , pp. 63-70
    • de Boer, P.A.1    Crossley, R.E.2    Rothfield, L.I.3
  • 101
    • 0030780085 scopus 로고    scopus 로고
    • The MinE ring: An FtsZ-independent cell structure required for selection of the correct division site in E. coli
    • Raskin, D. M. & de Boer, P. A. The MinE ring: An FtsZ-independent cell structure required for selection of the correct division site in E. coli. Cell 91, 685-694 (1997).
    • (1997) Cell , vol.91 , pp. 685-694
    • Raskin, D.M.1    de Boer, P.A.2
  • 102
    • 0036154068 scopus 로고    scopus 로고
    • A dynamic model for determining the middle of Escherichia coli
    • Kruse, K. A dynamic model for determining the middle of Escherichia coli. Biophys. J. 82, 618-627 (2002).
    • (2002) Biophys. J , vol.82 , pp. 618-627
    • Kruse, K.1
  • 103
    • 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. & 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. USA 96, 4971-4976 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 4971-4976
    • Raskin, D.M.1    de Boer, P.A.2
  • 104
    • 0032743092 scopus 로고    scopus 로고
    • MinDE-dependent pole-to-pole oscillation of division inhibitor MinC in Escherichia coli
    • Raskin. D. M. & de Boer, P. A. MinDE-dependent pole-to-pole oscillation of division inhibitor MinC in Escherichia coli. J. Bacteriol. 181. 6419-6424 (1999).
    • (1999) J. Bacteriol , vol.181 , pp. 6419-6424
    • Raskin, D.M.1    de Boer, P.A.2
  • 105
    • 0032846485 scopus 로고    scopus 로고
    • Topological regulation of cell division in Escherichia coli involves rapid pole to pole oscillation of the division inhibitor MinC under the control of MinD and MinE
    • Hu, Z. & Lutkenhaus. J. Topological regulation of cell division in Escherichia coli involves rapid pole to pole oscillation of the division inhibitor MinC under the control of MinD and MinE. Mol. Microbiol. 34, 82-90 (1999).
    • (1999) Mol. Microbiol , vol.34 , pp. 82-90
    • Hu, Z.1    Lutkenhaus, J.2
  • 106
    • 0035794706 scopus 로고    scopus 로고
    • Dynamic localization cycle of the cell division regulator MinE in Escherichia coli
    • Hale, C. A., Meinhardt, H. & de Boer, P. A. Dynamic localization cycle of the cell division regulator MinE in Escherichia coli. EMBO J. 20, 1563-1572 (2001).
    • (2001) EMBO J , vol.20 , pp. 1563-1572
    • Hale, C.A.1    Meinhardt, H.2    de Boer, P.A.3
  • 107
    • 0032973292 scopus 로고    scopus 로고
    • Selection of the midcell division site in Bacillus subtilis through MinD-dependent polar localization and activation of MinC
    • Marston, A. L. & ErringtDn, J. Selection of the midcell division site in Bacillus subtilis through MinD-dependent polar localization and activation of MinC. Mol. Microbiol. 33, 84-96 (1999).
    • (1999) Mol. Microbiol , vol.33 , pp. 84-96
    • Marston, A.L.1    ErringtDn, J.2
  • 108
    • 0032213104 scopus 로고    scopus 로고
    • Polar localization of the MinD protein of Bacillus subtilis and its role in selection of the mid-cell division site
    • Marston, A. L. Thomaides, H. B., Edwards, D. H., Sharpe, M. E. & Errington, J. Polar localization of the MinD protein of Bacillus subtilis and its role in selection of the mid-cell division site. Genes Dev. 12, 3419-3430 (1998).
    • (1998) Genes Dev , vol.12 , pp. 3419-3430
    • Marston, A.L.1    Thomaides, H.B.2    Edwards, D.H.3    Sharpe, M.E.4    Errington, J.5
  • 109
    • 30544445654 scopus 로고    scopus 로고
    • Rothfield, L, Taghbalout, & Shih. Y. L. Spatial control of bacterial division-site-placement. Nature Rev. Microbiol. 3, 959-968 (2005).
    • Rothfield, L, Taghbalout, & Shih. Y. L. Spatial control of bacterial division-site-placement. Nature Rev. Microbiol. 3, 959-968 (2005).
  • 110
    • 0032895234 scopus 로고    scopus 로고
    • FtsZ ring dusters in min and partition mutants: Role of both the Min system and the nucleoid in regulating FtsZ ring localization
    • Yu, X. C. & Margolin, W. FtsZ ring dusters in min and partition mutants: role of both the Min system and the nucleoid in regulating FtsZ ring localization. Mol. Microbiol. 32, 315-326 (1999).
    • (1999) Mol. Microbiol , vol.32 , pp. 315-326
    • Yu, X.C.1    Margolin, W.2
  • 111
    • 2942752105 scopus 로고    scopus 로고
    • Coordination of cell division and chromosome segregation by a nugleoid occlusion protein in Bacillus subtilis
    • Wu, L. J. & Errington, J. Coordination of cell division and chromosome segregation by a nugleoid occlusion protein in Bacillus subtilis. Cell 117, 915-925 (2004).
    • (2004) Cell , vol.117 , pp. 915-925
    • Wu, L.J.1    Errington, J.2
  • 112
    • 19444386428 scopus 로고    scopus 로고
    • SlmA, a nucleoid associated, FtsZ binding protein required for blocking septal ring assembly over chromosomes in E. coli
    • Bernhardt, T. G. & de Boer, P. A. SlmA, a nucleoid associated, FtsZ binding protein required for blocking septal ring assembly over chromosomes in E. coli. Mol. Cell 18, 555-564 (2005).
    • (2005) Mol. Cell , vol.18 , pp. 555-564
    • Bernhardt, T.G.1    de Boer, P.A.2
  • 113
    • 33745699284 scopus 로고    scopus 로고
    • L MipZ, a spatial regulator coordinating chromosome segregation with cell division in Coulobacter
    • Thanbichler, M. & Shapiro, L MipZ, a spatial regulator coordinating chromosome segregation with cell division in Coulobacter. Cell 126, 147-162 (2006).
    • (2006) Cell , vol.126 , pp. 147-162
    • Thanbichler, M.1    Shapiro2
  • 114
    • 0037341855 scopus 로고    scopus 로고
    • Productive interaction between the chromosome partitioning proteins, ParA and ParB. is required for the progression of the cell cycle in Coulobacter crescentus
    • Figge, R. M., Easter, J. & Gober, J. W. Productive interaction between the chromosome partitioning proteins, ParA and ParB. is required for the progression of the cell cycle in Coulobacter crescentus. Mol. Microbiol. 47, 1225-1237 (2003).
    • (2003) Mol. Microbiol , vol.47 , pp. 1225-1237
    • Figge, R.M.1    Easter, J.2    Gober, J.W.3
  • 115
    • 0030901361 scopus 로고    scopus 로고
    • Cell cycle-dependent polar localization of chromosome partitioning proteins in Coulabacter crescentus
    • Mohl, D. A. & Gober, J. W. Cell cycle-dependent polar localization of chromosome partitioning proteins in Coulabacter crescentus. Cell 88, 675-684 (1997).
    • (1997) Cell , vol.88 , pp. 675-684
    • Mohl, D.A.1    Gober, J.W.2
  • 116
    • 0034671792 scopus 로고    scopus 로고
    • Global analysis of the genetic network controlling a bacterial cell cycle
    • Laub. M. T., McAdams. H. H., Feldblyum, T., Fraser, C. M. & Shapiro, L Global analysis of the genetic network controlling a bacterial cell cycle. Science 290, 2144-2148 (2000).
    • (2000) Science , vol.290 , pp. 2144-2148
    • Laub, M.T.1    McAdams, H.H.2    Feldblyum, T.3    Fraser, C.M.4    Shapiro, L.5
  • 117
  • 118
    • 33644753905 scopus 로고    scopus 로고
    • A landmark protein essential for establishing and perpetuating the polarity of a bacterial cell
    • Lam, H., Schofield, W. B. & Jacobs-Wagner, C. A landmark protein essential for establishing and perpetuating the polarity of a bacterial cell. Cell 124. 1011-1023 (2006)
    • (2006) Cell , vol.124 , pp. 1011-1023
    • Lam, H.1    Schofield, W.B.2    Jacobs-Wagner, C.3
  • 119
    • 33751395400 scopus 로고    scopus 로고
    • A curvature-mediated mechanism for localization of lipids to bacterial poles
    • Huang. K. C., Mukhopadhyay, R. & Wingreen, N. S. A curvature-mediated mechanism for localization of lipids to bacterial poles. PLoS Comput. Biol. 2, e151 (2006).
    • (2006) PLoS Comput. Biol , vol.2
    • Huang, K.C.1    Mukhopadhyay, R.2    Wingreen, N.S.3
  • 120
    • 0033956407 scopus 로고    scopus 로고
    • Visualization of phosphollpid domains in Escherichia coli by using the cardiolipin-specific fluorescent dye 10-N-nonyl acridine orange
    • Mileykavskaya, E. & Dowhan. W. Visualization of phosphollpid domains in Escherichia coli by using the cardiolipin-specific fluorescent dye 10-N-nonyl acridine orange. J. Bacteriol. 182, 1172-1175 (2000).
    • (2000) J. Bacteriol , vol.182 , pp. 1172-1175
    • Mileykavskaya, E.1    Dowhan, W.2
  • 121
    • 1342282997 scopus 로고    scopus 로고
    • Cardiolipin domains in Bacillus subtilis Marburg membranes
    • Kawai, F. et al. Cardiolipin domains in Bacillus subtilis Marburg membranes. J. Bacteriol. 186, 1475-1483 (2004).
    • (2004) J. Bacteriol , vol.186 , pp. 1475-1483
    • Kawai, F.1
  • 122
    • 34250016257 scopus 로고    scopus 로고
    • Cardiolipin promotes polar localization of osmosensory transporter ProP in Escherichia coli
    • Romantsov, T. et al. Cardiolipin promotes polar localization of osmosensory transporter ProP in Escherichia coli. Mol. Microbiol. 64, 1455-1465 (2007).
    • (2007) Mol. Microbiol , vol.64 , pp. 1455-1465
    • Romantsov, T.1
  • 123
    • 30844471175 scopus 로고    scopus 로고
    • Magnetosomes are cell membrane invaginations organized by the actin-like protein MamK
    • Komeili, A., Li, Z., Newman, D. K. & Jensen, G. J. Magnetosomes are cell membrane invaginations organized by the actin-like protein MamK. Science 311, 242-245 (2006).
    • (2006) Science , vol.311 , pp. 242-245
    • Komeili, A.1    Li, Z.2    Newman, D.K.3    Jensen, G.J.4
  • 125
    • 33644763960 scopus 로고    scopus 로고
    • An acidic protein aligns magnetosomes along a filamentous structure in magnetotactic bacteria
    • Scheffel, A. et al. An acidic protein aligns magnetosomes along a filamentous structure in magnetotactic bacteria. Nature 440, 110-114 (2006).
    • (2006) Nature , vol.440 , pp. 110-114
    • Scheffel, A.1
  • 126
    • 0032484202 scopus 로고    scopus 로고
    • Magnetic microstructure of magnetotactic bacteria by electron holography
    • Dunin-Borkowski. R. E. et al. Magnetic microstructure of magnetotactic bacteria by electron holography Science 282, 1868-1870 (1998).
    • (1998) Science , vol.282 , pp. 1868-1870
    • Dunin-Borkowski, R.E.1
  • 127
    • 33751257193 scopus 로고    scopus 로고
    • Biogenesis of actin-like bacterial cytoskeletal filaments destined for positioning prokaryotic magnetic organelles
    • Pradel, N., Santini, C. L. Bernadac. A., Fukumori, Y. & Wu, L. F. Biogenesis of actin-like bacterial cytoskeletal filaments destined for positioning prokaryotic magnetic organelles. Proc. Natl Acad. Sci. USA 103, 17485-17489 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 17485-17489
    • Pradel, N.1    Santini, C.L.2    Bernadac, A.3    Fukumori, Y.4    Wu, L.F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.