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Volumn 179, Issue 3, 2007, Pages 381-387

Skin and bones: The bacterial cytoskeleton, cell wall, and cell morphogenesis

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATASE; FTSZ PROTEIN; MIND PROTEIN; PENICILLIN BINDING PROTEIN; PEPTIDOGLYCAN; TUBULIN; VANCOMYCIN;

EID: 35948967558     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.200708001     Document Type: Short Survey
Times cited : (67)

References (66)
  • 1
    • 34248364322 scopus 로고    scopus 로고
    • The tubulin homologue FtsZ contributes to cell elongation by guiding cell wall precursor synthesis in Caulobacter crescentus
    • Aaron, M., G. Charbon, H. Lam, H. Schwarz, W. Vollmer, and C. Jacobs-Wagner. 2007. The tubulin homologue FtsZ contributes to cell elongation by guiding cell wall precursor synthesis in Caulobacter crescentus. Mol. Microbiol. 64:938-952.
    • (2007) Mol. Microbiol , vol.64 , pp. 938-952
    • Aaron, M.1    Charbon, G.2    Lam, H.3    Schwarz, H.4    Vollmer, W.5    Jacobs-Wagner, C.6
  • 2
    • 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., F.J. Gueiros-Filho, and H.P. Erickson. 2004. Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins. J. Bacteriol. 186:5775-5781.
    • (2004) J. Bacteriol , vol.186 , pp. 5775-5781
    • Anderson, D.E.1    Gueiros-Filho, F.J.2    Erickson, H.P.3
  • 3
    • 0346020436 scopus 로고    scopus 로고
    • The bacterial cytoskeleton: An intermediate filament-like function in cell shape
    • Ausmees, N., J.R. Kuhn, and C. Jacobs-Wagner. 2003. The bacterial cytoskeleton: an intermediate filament-like function in cell shape. Cell. 115:705-713.
    • (2003) Cell , vol.115 , pp. 705-713
    • Ausmees, N.1    Kuhn, J.R.2    Jacobs-Wagner, C.3
  • 4
    • 0030013043 scopus 로고    scopus 로고
    • Changes in Helicobacter pylori ultrastructure and antigens during conversion from the bacillary to the coccoid form
    • Benaissa, M., P. Babin, N. Quellard, L. Pezennec, Y. Cenatiempo, and J.L. Fauchere. 1996. Changes in Helicobacter pylori ultrastructure and antigens during conversion from the bacillary to the coccoid form. Infect. Immun. 64:2331-2335.
    • (1996) Infect. Immun , vol.64 , pp. 2331-2335
    • Benaissa, M.1    Babin, P.2    Quellard, N.3    Pezennec, L.4    Cenatiempo, Y.5    Fauchere, J.L.6
  • 5
    • 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., and P.A. de Boer. 2005. SlmA, a nucleoid-associated, FtsZ binding protein required for blocking septal ring assembly over chromosomes in E. coli. Mol. Cell. 18:555-564.
    • (2005) Mol. Cell , vol.18 , pp. 555-564
    • Bernhardt, T.G.1    de Boer, P.A.2
  • 6
    • 0026059127 scopus 로고
    • FtsZ ring structure associated with division in Escherichia coli
    • Bi, E.F., and J. Lutkenhaus. 1991. FtsZ ring structure associated with division in Escherichia coli. Nature. 354:161-164.
    • (1991) Nature , vol.354 , pp. 161-164
    • Bi, E.F.1    Lutkenhaus, J.2
  • 7
    • 33845619142 scopus 로고    scopus 로고
    • The bacterial actin-like cytoskeleton
    • Carballido-Lopez, R. 2006. The bacterial actin-like cytoskeleton. Microbiol. Mol. Biol. Rev. 70:888-909.
    • (2006) Microbiol. Mol. Biol. Rev , vol.70 , pp. 888-909
    • Carballido-Lopez, R.1
  • 8
    • 33747837700 scopus 로고    scopus 로고
    • Actin homolog MreBH governs cell morphogenesis by localization of the cell wall hydrolase LytE
    • Carballido-Lopez, R., A. Formstone, Y. Li, S.D. Ehrlich, P. Noirot, and J. Errington. 2006. Actin homolog MreBH governs cell morphogenesis by localization of the cell wall hydrolase LytE. Dev. Cell. 11:399-409.
    • (2006) Dev. Cell , vol.11 , pp. 399-409
    • Carballido-Lopez, R.1    Formstone, A.2    Li, Y.3    Ehrlich, S.D.4    Noirot, P.5    Errington, J.6
  • 10
    • 0037494988 scopus 로고    scopus 로고
    • Control of cell morphogenesis in bacteria: Two distinct ways to make a rod-shaped cell
    • Daniel, R.A., and J. Errington. 2003. Control of cell morphogenesis in bacteria: two distinct ways to make a rod-shaped cell. Cell. 113:767-776.
    • (2003) Cell , vol.113 , pp. 767-776
    • Daniel, R.A.1    Errington, J.2
  • 12
    • 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., R.R. Loo, Y. Xie, J.A. Loo, and J.W. Gober. 2005. The cell-shape protein MreC interacts with extracytoplasmic proteins including cell wall assembly complexes in Caulobacter crescentus. Proc. Natl. Acad. Sci. USA. 102:18602-18607.
    • (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
  • 13
    • 34548677525 scopus 로고    scopus 로고
    • The cell shape proteins MreB and MreC control cell morphogenesis by positioning cell wall synthetic complexes
    • Divakaruni, A.V., C. Baida, C.L. White, and J.W. Gober. 2007. The cell shape proteins MreB and MreC control cell morphogenesis by positioning cell wall synthetic complexes. Mol. Microbiol. 66:174-188.
    • (2007) Mol. Microbiol , vol.66 , pp. 174-188
    • Divakaruni, A.V.1    Baida, C.2    White, C.L.3    Gober, J.W.4
  • 15
    • 1542616355 scopus 로고    scopus 로고
    • MreB, the cell shape-determining bacterial actin homologue, co-ordinates cell wall morphogenesis in Caulobacter crescentus
    • Figge, R.M., A.V. Divakaruni, and J.W. Gober. 2004. MreB, the cell shape-determining bacterial actin homologue, co-ordinates cell wall morphogenesis in Caulobacter crescentus. Mol. Microbiol. 51:1321-1332.
    • (2004) Mol. Microbiol , vol.51 , pp. 1321-1332
    • Figge, R.M.1    Divakaruni, A.V.2    Gober, J.W.3
  • 16
    • 0141789744 scopus 로고    scopus 로고
    • Essential role of DivIVA in polar growth and morphogenesis in Streptomyces coelicolor A3(2)
    • Flärdh, K. 2003a. Essential role of DivIVA in polar growth and morphogenesis in Streptomyces coelicolor A3(2). Mol. Microbiol. 49:1523-1536.
    • (2003) Mol. Microbiol , vol.49 , pp. 1523-1536
    • Flärdh, K.1
  • 17
    • 0346734224 scopus 로고    scopus 로고
    • Growth polarity and cell division in Streptomyces
    • Flärdh, K. 2003b. Growth polarity and cell division in Streptomyces. Curr. Opin. Microbiol. 6:564-571.
    • (2003) Curr. Opin. Microbiol , vol.6 , pp. 564-571
    • Flärdh, K.1
  • 18
    • 13544274210 scopus 로고    scopus 로고
    • MreB actin-mediated segregation of a specific region of a bacterial chromosome
    • Gitai, Z., N.A. Dye, A. Reisenauer, M. Wachi, and L. Shapiro. 2005. MreB actin-mediated segregation of a specific region of a bacterial chromosome. Cell. 120:329-341.
    • (2005) Cell , vol.120 , pp. 329-341
    • Gitai, Z.1    Dye, N.A.2    Reisenauer, A.3    Wachi, M.4    Shapiro, L.5
  • 19
    • 0036440952 scopus 로고    scopus 로고
    • Force and compliance: Rethinking morphogenesis in walled cells
    • Harold, F.M. 2002. Force and compliance: rethinking morphogenesis in walled cells. Fungal Genet. Biol. 37:271-282.
    • (2002) Fungal Genet. Biol , vol.37 , pp. 271-282
    • Harold, F.M.1
  • 20
    • 33645306591 scopus 로고    scopus 로고
    • Three-dimensional structure of Mycoplasma pneumoniae's attachment organelle and a model for its role in gliding motility
    • Henderson, G.P., and G.J. Jensen. 2006. Three-dimensional structure of Mycoplasma pneumoniae's attachment organelle and a model for its role in gliding motility. Mol. Microbiol. 60:376-385.
    • (2006) Mol. Microbiol , vol.60 , pp. 376-385
    • Henderson, G.P.1    Jensen, G.J.2
  • 21
    • 0037858060 scopus 로고    scopus 로고
    • Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli
    • Höltje, J.V. 1998. Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli. Microbiol. Mol. Biol. Rev. 62:181-203.
    • (1998) Microbiol. Mol. Biol. Rev , vol.62 , pp. 181-203
    • Höltje, J.V.1
  • 22
    • 0033592949 scopus 로고    scopus 로고
    • The MinC component of the division site selection system in Escherichia coli interacts with FtsZ to prevent polymerization
    • Hu, Z., A. Mukherjee, S. Pichoff, and J. Lutkenhaus. 1999. The MinC component of the division site selection system in Escherichia coli interacts with FtsZ to prevent polymerization. Proc. Natl. Acad. Sci. USA. 96:14819-14824.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14819-14824
    • Hu, Z.1    Mukherjee, A.2    Pichoff, S.3    Lutkenhaus, J.4
  • 23
    • 0035937396 scopus 로고    scopus 로고
    • Control of cell shape in bacteria: Helical, actin-like filaments in Bacillus subtilis
    • Jones, L.J., R. Carballido-Lopez, and J. Errington. 2001. Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis. Cell. 104:913-922.
    • (2001) Cell , vol.104 , pp. 913-922
    • Jones, L.J.1    Carballido-Lopez, R.2    Errington, J.3
  • 24
    • 33845933694 scopus 로고    scopus 로고
    • Filamentation by Escherichia coli subverts innate defenses during urinary tract infection
    • Justice, S.S., D.A. Hunstad, P.C. Seed, and S.J. Hultgren. 2006. Filamentation by Escherichia coli subverts innate defenses during urinary tract infection. Proc. Natl. Acad. Sci. USA. 103:19884-19889.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 19884-19889
    • Justice, S.S.1    Hunstad, D.A.2    Seed, P.C.3    Hultgren, S.J.4
  • 25
    • 0022339288 scopus 로고
    • How bacteria grow and divide in spite of internal hydrostatic pressure
    • Koch, A.L. 1985. How bacteria grow and divide in spite of internal hydrostatic pressure. Can. J. Microbiol. 31:1071-1084.
    • (1985) Can. J. Microbiol , vol.31 , pp. 1071-1084
    • Koch, A.L.1
  • 26
    • 12344306119 scopus 로고    scopus 로고
    • The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex
    • Kruse, T., J. Bork-Jensen, and K. Gerdes. 2005. The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex. Mol. Microbiol. 55:78-89.
    • (2005) Mol. Microbiol , vol.55 , pp. 78-89
    • Kruse, T.1    Bork-Jensen, J.2    Gerdes, K.3
  • 27
    • 0034934967 scopus 로고    scopus 로고
    • Stabilization of friable sandstone surfaces in a desiccating, wind-abraded environment of south-central Utah by rock surface microorganisms
    • Kurtz, H.D., and D.I. Netoff. 2001. Stabilization of friable sandstone surfaces in a desiccating, wind-abraded environment of south-central Utah by rock surface microorganisms. Journal of Arid Environments. 48:89-100.
    • (2001) Journal of Arid Environments , vol.48 , pp. 89-100
    • Kurtz, H.D.1    Netoff, D.I.2
  • 28
    • 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 J. Errington. 2005. Roles for MreC and MreD proteins in helical growth of the cylindrical cell wall in Bacillus subtilis. Mol. Microbiol. 57:1196-1209.
    • (2005) Mol. Microbiol , vol.57 , pp. 1196-1209
    • Leaver, M.1    Errington, J.2
  • 29
    • 0033986992 scopus 로고    scopus 로고
    • Straight and curved conformations of FtsZ are regulated by GTP hydrolysis
    • Lu, C., M. Reedy, and H.P. Erickson. 2000. Straight and curved conformations of FtsZ are regulated by GTP hydrolysis. J. Bacteriol. 182:164-170.
    • (2000) J. Bacteriol , vol.182 , pp. 164-170
    • Lu, C.1    Reedy, M.2    Erickson, H.P.3
  • 30
    • 27644540151 scopus 로고    scopus 로고
    • FtsZ and the division of prokaryotic cells and organelles
    • Margolin, W. 2005. FtsZ and the division of prokaryotic cells and organelles. Nat. Rev. Mol. Cell Biol. 6:862-871.
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 862-871
    • Margolin, W.1
  • 31
    • 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., H.B. Thomaides, D.H. Edwards, M.E. Sharpe, and J. Errington. 1998. 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) 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
  • 33
    • 0021191674 scopus 로고
    • Insertion and fate of the cell wall in Bacillus subtilis
    • Mobley, H.L., A.L. Koch, R.J. Doyle, and U.N. Streips. 1984. Insertion and fate of the cell wall in Bacillus subtilis. J. Bacteriol. 158:169-179.
    • (1984) J. Bacteriol , vol.158 , pp. 169-179
    • Mobley, H.L.1    Koch, A.L.2    Doyle, R.J.3    Streips, U.N.4
  • 34
    • 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., A. Karczmarek, M. Crouvoisier, A. Bouhss, D. Mengin-Lecreulx, and T. den Blaauwen. 2007. 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) Mol. Microbiol , vol.65 , pp. 1106-1121
    • Mohammadi, T.1    Karczmarek, A.2    Crouvoisier, M.3    Bouhss, A.4    Mengin-Lecreulx, D.5    den Blaauwen, T.6
  • 35
    • 1642442760 scopus 로고    scopus 로고
    • The D,D-carboxypeptidase PBP3 organizes the division process of Streptococcus pneumoniae
    • Morlot, C., M. Noirclerc-Savoye, A. Zapun, O. Dideberg, and T. Vernet. 2004. The D,D-carboxypeptidase PBP3 organizes the division process of Streptococcus pneumoniae. Mol. Microbiol. 51:1641-1648.
    • (2004) Mol. Microbiol , vol.51 , pp. 1641-1648
    • Morlot, C.1    Noirclerc-Savoye, M.2    Zapun, A.3    Dideberg, O.4    Vernet, T.5
  • 37
    • 14644412812 scopus 로고    scopus 로고
    • Phosphat idylethanolamine domains and localization of phospholipid synthases in Bacillus subtilis membranes
    • Nishibori, A., J. Kusaka, H. Hara, M. Umeda, and K. Matsumoto. 2005. Phosphat idylethanolamine domains and localization of phospholipid synthases in Bacillus subtilis membranes. J. Bacteriol. 187:2163-2174.
    • (2005) J. Bacteriol , vol.187 , pp. 2163-2174
    • Nishibori, A.1    Kusaka, J.2    Hara, H.3    Umeda, M.4    Matsumoto, K.5
  • 38
    • 33745000523 scopus 로고    scopus 로고
    • Visualization of cellulose synthase demonstrates functional association with microtubules
    • Paredez, A.R., C.R. Somerville, and D.W. Ehrhardt. 2006. Visualization of cellulose synthase demonstrates functional association with microtubules. Science. 312:1491-1495.
    • (2006) Science , vol.312 , pp. 1491-1495
    • Paredez, A.R.1    Somerville, C.R.2    Ehrhardt, D.W.3
  • 39
    • 4444297890 scopus 로고    scopus 로고
    • Structural determinants required to target penicillin-binding protein 3 to the septum of Escherichia coli
    • Piette, A., C. Fraipont, T. Den Blaauwen, M.E. Aarsman, S. Pastoret, and M. Nguyen-Disteche. 2004. Structural determinants required to target penicillin-binding protein 3 to the septum of Escherichia coli. J. Bacteriol. 186:6110-6117.
    • (2004) J. Bacteriol , vol.186 , pp. 6110-6117
    • Piette, A.1    Fraipont, C.2    Den Blaauwen, T.3    Aarsman, M.E.4    Pastoret, S.5    Nguyen-Disteche, M.6
  • 40
    • 0242606152 scopus 로고    scopus 로고
    • Dispersed mode of Staphylococcus aureus cell wall synthesis in the absence of the division machinery
    • Pinho, M.G., and J. Errington. 2003. Dispersed mode of Staphylococcus aureus cell wall synthesis in the absence of the division machinery. Mol. Microbiol. 50:871-881.
    • (2003) Mol. Microbiol , vol.50 , pp. 871-881
    • Pinho, M.G.1    Errington, J.2
  • 41
    • 13444259776 scopus 로고    scopus 로고
    • Recruitment of penicillin-binding protein PBP2 to the division site of Staphylococcus aureus is dependent on its transpeptidation substrates
    • Pinho, M.G., and J. Errington. 2005. Recruitment of penicillin-binding protein PBP2 to the division site of Staphylococcus aureus is dependent on its transpeptidation substrates. Mol. Microbiol. 55:799-807.
    • (2005) Mol. Microbiol , vol.55 , pp. 799-807
    • Pinho, M.G.1    Errington, J.2
  • 42
    • 33645063725 scopus 로고    scopus 로고
    • Mechanism of polarization of Listeria monocytogenes surface protein ActA
    • Rafelski, S.M., and J.A. Theriot. 2006. Mechanism of polarization of Listeria monocytogenes surface protein ActA. Mol. Microbiol. 59:1262-1279.
    • (2006) Mol. Microbiol , vol.59 , pp. 1262-1279
    • Rafelski, S.M.1    Theriot, J.A.2
  • 43
    • 0348143172 scopus 로고    scopus 로고
    • Involvement of DivIVA in the morphology of the rod-shaped actinomycete Brevibacterium lactofermentum
    • Ramos, A., M.P. Honrubia, N. Valbuena, J. Vaquera, L.M. Mateos, and J.A. Gil. 2003. Involvement of DivIVA in the morphology of the rod-shaped actinomycete Brevibacterium lactofermentum. Microbiology. 149:3531-3542.
    • (2003) Microbiology , vol.149 , pp. 3531-3542
    • Ramos, A.1    Honrubia, M.P.2    Valbuena, N.3    Vaquera, J.4    Mateos, L.M.5    Gil, J.A.6
  • 44
    • 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 P.A. de Boer. 1999. 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) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4971-4976
    • Raskin, D.M.1    de Boer, P.A.2
  • 45
    • 0028016512 scopus 로고
    • Specific interaction of penicillin-binding proteins 3 and 7/8 with soluble lytic transglycosylase in Escherichia coli
    • Romeis, T., and J.V. Höltje. 1994. Specific interaction of penicillin-binding proteins 3 and 7/8 with soluble lytic transglycosylase in Escherichia coli. J. Biol. Chem. 269:21603-21607.
    • (1994) J. Biol. Chem , vol.269 , pp. 21603-21607
    • Romeis, T.1    Höltje, J.V.2
  • 46
    • 1242320297 scopus 로고    scopus 로고
    • Several distinct localization patterns for penicillin-binding proteins in Bacillus subtilis
    • Scheffers, D.J., L.J. Jones, and J. Errington. 2004. Several distinct localization patterns for penicillin-binding proteins in Bacillus subtilis. Mol. Microbiol. 51:749-764.
    • (2004) Mol. Microbiol , vol.51 , pp. 749-764
    • Scheffers, D.J.1    Jones, L.J.2    Errington, J.3
  • 47
    • 0040205694 scopus 로고    scopus 로고
    • Cloning and characterization of PBP 1C, a third member of the multimodular class A penicillin-binding proteins of Escherichia coli
    • Schiffer, G., and J.V. Höltje. 1999. Cloning and characterization of PBP 1C, a third member of the multimodular class A penicillin-binding proteins of Escherichia coli. J. Biol. Chem. 274:32031-32039.
    • (1999) J. Biol. Chem , vol.274 , pp. 32031-32039
    • Schiffer, G.1    Höltje, J.V.2
  • 48
    • 0013883373 scopus 로고
    • The development of cellular stalks in bacteria
    • Schmidt, J.M., and R.Y. Stanier. 1966. The development of cellular stalks in bacteria. J. Cell Biol. 28:423-436.
    • (1966) J. Cell Biol , vol.28 , pp. 423-436
    • Schmidt, J.M.1    Stanier, R.Y.2
  • 49
    • 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., T. Le, and L. Rothfield. 2003. 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) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 7865-7870
    • Shih, Y.L.1    Le, T.2    Rothfield, L.3
  • 50
    • 25844456826 scopus 로고    scopus 로고
    • Controlling the shape of filamentous cells of Escherichia coli
    • Takeuchi, S., W.R. DiLuzio, D.B. Weibel, and G.M. Whitesides. 2005. Controlling the shape of filamentous cells of Escherichia coli. Nano Lett. 5:1819-1823.
    • (2005) Nano Lett , vol.5 , pp. 1819-1823
    • Takeuchi, S.1    DiLuzio, W.R.2    Weibel, D.B.3    Whitesides, G.M.4
  • 51
    • 33745699284 scopus 로고    scopus 로고
    • MipZ, a spatial regulator coordinating chromosome segregation with cell division in Caulobacter
    • Thanbichler, M., and L. Shapiro. 2006. MipZ, a spatial regulator coordinating chromosome segregation with cell division in Caulobacter. Cell. 126:147-162.
    • (2006) Cell , vol.126 , pp. 147-162
    • Thanbichler, M.1    Shapiro, L.2
  • 54
    • 0021082772 scopus 로고
    • Growth of the surface of Corynebacterium diphtheriae
    • Umeda, A., and K. Amako. 1983. Growth of the surface of Corynebacterium diphtheriae. Microbiol. Immunol. 27:663-671.
    • (1983) Microbiol. Immunol , vol.27 , pp. 663-671
    • Umeda, A.1    Amako, K.2
  • 55
    • 0024730353 scopus 로고
    • Developmental regulation of a Rhizobium cell surface antigen during growth of pea root nodules
    • VandenBosch, K.A., N.J. Brewin, and E.L. Kannenberg. 1989. Developmental regulation of a Rhizobium cell surface antigen during growth of pea root nodules. J. Bacteriol. 171:4537-4542.
    • (1989) J. Bacteriol , vol.171 , pp. 4537-4542
    • VandenBosch, K.A.1    Brewin, N.J.2    Kannenberg, E.L.3
  • 56
    • 34547618469 scopus 로고    scopus 로고
    • FtsZ directs a second mode of peptidoglycan synthesis in Escherichia coli
    • Varma, A., M. de Pedro, and K.D. Young. 2007. FtsZ directs a second mode of peptidoglycan synthesis in Escherichia coli. J. Bacteriol. 189:5692-704.
    • (2007) J. Bacteriol , vol.189 , pp. 5692-5704
    • Varma, A.1    de Pedro, M.2    Young, K.D.3
  • 57
    • 0033525526 scopus 로고    scopus 로고
    • Demonstration of molecular interactions between the murein polymerase PBP1B, the lytic transglycosylase MltA, and the scaffolding protein MipA of Escherichia coli
    • Vollmer, W., M. von Rechenberg, and J.V. Höltje. 1999. Demonstration of molecular interactions between the murein polymerase PBP1B, the lytic transglycosylase MltA, and the scaffolding protein MipA of Escherichia coli. J. Biol. Chem. 274:6726-6734.
    • (1999) J. Biol. Chem , vol.274 , pp. 6726-6734
    • Vollmer, W.1    von Rechenberg, M.2    Höltje, J.V.3
  • 58
    • 0032453738 scopus 로고    scopus 로고
    • FtsI and FtsW are localized to the septum in Escherichia coli
    • Wang, L., M.K. Khattar, W.D. Donachie, and J. Lutkenhaus. 1998. FtsI and FtsW are localized to the septum in Escherichia coli. J. Bacteriol. 180:2810-2816.
    • (1998) J. Bacteriol , vol.180 , pp. 2810-2816
    • Wang, L.1    Khattar, M.K.2    Donachie, W.D.3    Lutkenhaus, J.4
  • 59
    • 0029919949 scopus 로고    scopus 로고
    • Characterization of the ftsZ gene from Mycoplasma pulmonis, an organism lacking a cell wall
    • Wang, X., and J. Lutkenhaus. 1996. Characterization of the ftsZ gene from Mycoplasma pulmonis, an organism lacking a cell wall. J. Bacteriol. 178:2314-2319.
    • (1996) J. Bacteriol , vol.178 , pp. 2314-2319
    • Wang, X.1    Lutkenhaus, J.2
  • 61
    • 11144318755 scopus 로고    scopus 로고
    • The transmembrane helix of the Escherichia coli division protein FtsI localizes to the septal ring
    • Wissel, M.C., J.L. Wendt, C.J. Mitchell, and D.S. Weiss. 2005. The transmembrane helix of the Escherichia coli division protein FtsI localizes to the septal ring. J. Bacteriol. 187:320-328.
    • (2005) J. Bacteriol , vol.187 , pp. 320-328
    • Wissel, M.C.1    Wendt, J.L.2    Mitchell, C.J.3    Weiss, D.S.4
  • 62
    • 0019120818 scopus 로고
    • Dimensional rearrangement of rod-shaped bacteria following nutritional shift-up. II. Experiments with Escherichia coli B/r
    • Woldringh, C.L., N.B. Grover, R.F. Rosenberger, and A. Zaritsky. 1980. Dimensional rearrangement of rod-shaped bacteria following nutritional shift-up. II. Experiments with Escherichia coli B/r. J. Theor. Biol. 86:441-454.
    • (1980) J. Theor. Biol , vol.86 , pp. 441-454
    • Woldringh, C.L.1    Grover, N.B.2    Rosenberger, R.F.3    Zaritsky, A.4
  • 65
    • 2942752105 scopus 로고    scopus 로고
    • Coordination of cell division and chromosome segregation by a nucleoid occlusion protein in Bacillus subtilis
    • Wu, L.J., and J. Errington. 2004. Coordination of cell division and chromosome segregation by a nucleoid occlusion protein in Bacillus subtilis. Cell. 117:915-925.
    • (2004) Cell , vol.117 , pp. 915-925
    • Wu, L.J.1    Errington, J.2
  • 66
    • 33749257121 scopus 로고    scopus 로고
    • The selective value of bacterial shape
    • Young, K.D. 2006. The selective value of bacterial shape. Microbiol. Mol. Biol. Rev. 70:660-703.
    • (2006) Microbiol. Mol. Biol. Rev , vol.70 , pp. 660-703
    • Young, K.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.