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Volumn 4 S, Issue 4, 2012, Pages 1582-1606

The actin-like MreB proteins in Bacillus subtilis: A new turn

Author keywords

Actin cytoskeleton; Bacterial cell shape; Cell wall elongation; Helix localization; MreB; Review

Indexed keywords

DNA; MREB PROTEIN; VIRUS DNA; ACTIN; BACTERIAL PROTEIN; CYTOSKELETON PROTEIN;

EID: 84869433974     PISSN: 19450516     EISSN: 19450524     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (42)

References (141)
  • 3
    • 0024095917 scopus 로고
    • Determinations of the DNA sequence of the mreB gene and of the gene products of the mre region that function in formation of the rod shape of Escherichia coli cells
    • M. Doi, M. Wachi, F. Ishino, S. Tomioka, M. Ito, Y. Sakagami, A. Suzuki & M. Matsuhashi: Determinations of the DNA sequence of the mreB gene and of the gene products of the mre region that function in formation of the rod shape of Escherichia coli cells. J Bacteriol, 170, 4619-24 (1988)
    • (1988) J Bacteriol , vol.170 , pp. 4619-4624
    • Doi, M.1    Wachi, M.2    Ishino, F.3    Tomioka, S.4    Ito, M.5    Sakagami, Y.6    Suzuki, A.7    Matsuhashi, M.8
  • 4
    • 0026768828 scopus 로고
    • Identification of Bacillus subtilis genes for septum placement and shape determination
    • P. A. Levin, P. S. Margolis, P. Setlow, R. Losick & D. Sun: Identification of Bacillus subtilis genes for septum placement and shape determination. J Bacteriol, 174, 6717-28 (1992)
    • (1992) J Bacteriol , vol.174 , pp. 6717-6728
    • Levin, P.A.1    Margolis, P.S.2    Setlow, P.3    Losick, R.4    Sun, D.5
  • 5
    • 0024332035 scopus 로고
    • New mre genes mreC and mreD, responsible for formation of the rod shape of Escherichia coli cells
    • M. Wachi, M. Doi, Y. Okada & M. Matsuhashi: New mre genes mreC and mreD, responsible for formation of the rod shape of Escherichia coli cells. J Bacteriol, 171, 6511-6 (1989) (Pubitemid 20006928)
    • (1989) Journal of Bacteriology , vol.171 , Issue.12 , pp. 6511-6516
    • Wachi, M.1    Doi, M.2    Okada, Y.3    Matsuhashi, M.4
  • 6
    • 0026687729 scopus 로고
    • An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and Hsp70 heat shock proteins
    • P. Bork, C. Sander & A. Valencia: An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and Hsp70 heat shock proteins. Proc Natl Acad Sci U S A, 89, 7290-4 (1992)
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 7290-7294
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 8
    • 0035817819 scopus 로고    scopus 로고
    • Prokaryotic origin of the actin cytoskeleton
    • DOI 10.1038/35092500
    • F. van den Ent, L. A. Amos & J. Lowe: Prokaryotic origin of the actin cytoskeleton. Nature, 413, 39-44 (2001) (Pubitemid 32843480)
    • (2001) Nature , vol.413 , Issue.6851 , pp. 39-44
    • Van Den Ent, F.1    Amos, L.A.2    Lowe, J.3
  • 9
    • 0035937396 scopus 로고    scopus 로고
    • Control of cell shape in bacteria: Helical, actin-like filaments in Bacillus subtilis
    • DOI 10.1016/S0092-8674(01)00287-2
    • L. J. Jones, R. Carballido-López & J. Errington: Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis. Cell, 104, 913-22 (2001) (Pubitemid 32289283)
    • (2001) Cell , vol.104 , Issue.6 , pp. 913-922
    • Jones, L.J.F.1    Carballido-Lopez, R.2    Errington, J.3
  • 10
    • 33747837700 scopus 로고    scopus 로고
    • Actin homolog mrebh governs cell morphogenesis by localization of the cell wall hydrolase lyte
    • DOI 10.1016/j.devcel.2006.07.017, PII S1534580706003467
    • R. Carballido-López, A. Formstone, Y. Li, S. D. Ehrlich, P. Noirot & J. Errington: Actin homolog MreBH governs cell morphogenesis by localization of the cell wall hydrolase LytE. Dev Cell, 11, 399-409 (2006) (Pubitemid 44283948)
    • (2006) Developmental Cell , vol.11 , Issue.3 , pp. 399-409
    • Carballido-Lopez, R.1    Formstone, A.2    Li, Y.3    Ehrlich, S.D.4    Noirot, P.5    Errington, J.6
  • 11
    • 75349104798 scopus 로고    scopus 로고
    • Architecture of peptidoglycan: More data and more models
    • W. Vollmer & S. J. Seligman: Architecture of peptidoglycan: more data and more models. Trends Microbiol, 18, 59-66 (2010)
    • (2010) Trends Microbiol , vol.18 , pp. 59-66
    • Vollmer, W.1    Seligman, S.J.2
  • 12
    • 78649543920 scopus 로고    scopus 로고
    • Bacillus subtilis MreB paralogues have different filament architectures and lead to shape remodelling of a heterologous cell system
    • H. J. Defeu Soufo & P. L. Graumann: Bacillus subtilis MreB paralogues have different filament architectures and lead to shape remodelling of a heterologous cell system. Mol Microbiol, 78, 1145-58 (2010)
    • (2010) Mol Microbiol , vol.78 , pp. 1145-1158
    • Defeu Soufo, H.J.1    Graumann, P.L.2
  • 14
    • 77956164845 scopus 로고    scopus 로고
    • Application of atomic force microscopy in bacterial research
    • L. S. Dorobantu & M. R. Gray: Application of atomic force microscopy in bacterial research. Scanning, 32, 74-96 (2010)
    • (2010) Scanning , vol.32 , pp. 74-96
    • Dorobantu, L.S.1    Gray, M.R.2
  • 15
    • 77954995399 scopus 로고    scopus 로고
    • A guide to super-resolution fluorescence microscopy
    • L. Schermelleh, R. Heintzmann & H. Leonhardt: A guide to super-resolution fluorescence microscopy. J Cell Biol, 190, 165-75 (2010)
    • (2010) J Cell Biol , vol.190 , pp. 165-175
    • Schermelleh, L.1    Heintzmann, R.2    Leonhardt, H.3
  • 16
    • 0037237123 scopus 로고    scopus 로고
    • The bacterial cytoskeleton: In vivo dynamics of the actin-like protein Mbl of Bacillus subtilis
    • DOI 10.1016/S1534-5807(02)00403-3, PII S1534580702004033
    • R. Carballido-López & J. Errington: The bacterial cytoskeleton: in vivo dynamics of the actin-like protein Mbl of Bacillus subtilis. Dev Cell, 4, 19-28 (2003) (Pubitemid 36105332)
    • (2003) Developmental Cell , vol.4 , Issue.1 , pp. 19-28
    • Carballido-Lopez, R.1    Errington, J.2
  • 17
    • 4444285310 scopus 로고    scopus 로고
    • Dynamic movement of actin-like proteins within bacterial cells
    • DOI 10.1038/sj.embor.7400209
    • H. J. Defeu Soufo & P. L. Graumann: Dynamic movement of actin-like proteins within bacterial cells. EMBO Rep, 5, 789-94 (2004) (Pubitemid 39199168)
    • (2004) EMBO Reports , vol.5 , Issue.8 , pp. 789-794
    • Defeu Soufo, H.J.1    Graumann, P.L.2
  • 18
    • 0141864658 scopus 로고    scopus 로고
    • Dysfunctional MreB inhibits chromosome segregation in Escherichia coli
    • DOI 10.1093/emboj/cdg504
    • T. Kruse, J. Moller-Jensen, A. Lobner-Olesen & K. Gerdes: Dysfunctional MreB inhibits chromosome segregation in Escherichia coli. Embo J, 22, 5283-92 (2003) (Pubitemid 37222047)
    • (2003) EMBO Journal , vol.22 , Issue.19 , pp. 5283-5292
    • Kruse, T.1    Moeller-Jensen, J.2    Lobner-Olesen, A.3    Gerdes, K.4
  • 19
    • 1542616355 scopus 로고    scopus 로고
    • MreB, the cell shape-determining bacterial actin homologue, co-ordinates cell wall morphogenesis in Caulobacter crescentus
    • DOI 10.1111/j.1365-2958.2003.03936.x
    • R. M. Figge, A. V. Divakaruni & J. W. Gober: MreB, the cell shape-determining bacterial actin homologue, coordinates cell wall morphogenesis in Caulobacter crescentus. Mol Microbiol, 51, 1321-32 (2004) (Pubitemid 38338895)
    • (2004) Molecular Microbiology , vol.51 , Issue.5 , pp. 1321-1332
    • Figge, R.M.1    Divakaruni, A.V.2    Gober, J.W.3
  • 20
    • 43449093719 scopus 로고    scopus 로고
    • Lipid spirals in Bacillus subtilis and their role in cell division
    • DOI 10.1111/j.1365-2958.2008.06236.x
    • I. Barak, K. Muchova, A. J. Wilkinson, P. J. O'Toole & N. Pavlendova: Lipid spirals in Bacillus subtilis and their role in cell division. Mol Microbiol, 68, 1315-27 (2008) (Pubitemid 351670204)
    • (2008) Molecular Microbiology , vol.68 , Issue.5 , pp. 1315-1327
    • Barak, I.1    Muchova, K.2    Wilkinson, A.J.3    O'Toole, P.J.4    Pavlendova, N.5
  • 22
  • 23
    • 79953885641 scopus 로고    scopus 로고
    • The YvcK protein is required for morphogenesis via localization of PBP1 under gluconeogenic growth conditions in Bacillus subtilis
    • E. Foulquier, F. Pompeo, A. Bernadac, L. Espinosa & A. Galinier: The YvcK protein is required for morphogenesis via localization of PBP1 under gluconeogenic growth conditions in Bacillus subtilis. Mol Microbiol, 80, 309-18 (2011)
    • (2011) Mol Microbiol , vol.80 , pp. 309-318
    • Foulquier, E.1    Pompeo, F.2    Bernadac, A.3    Espinosa, L.4    Galinier, A.5
  • 25
    • 2342640965 scopus 로고    scopus 로고
    • Septal localization of forespore membrane proteins during engulfment in Bacillus subtilis
    • DOI 10.1038/sj.emboj.7600171
    • A. Rubio & K. Pogliano: Septal localization of forespore membrane proteins during engulfment in Bacillus subtilis. Embo J, 23, 1636-46 (2004) (Pubitemid 38579524)
    • (2004) EMBO Journal , vol.23 , Issue.7 , pp. 1636-1646
    • Rubio, A.1    Pogliano, K.2
  • 26
    • 29144477176 scopus 로고    scopus 로고
    • Bacterial cell wall synthesis: New insights from localization studies
    • DOI 10.1128/MMBR.69.4.585-607.2005
    • D. J. Scheffers & M. G. Pinho: Bacterial cell wall synthesis: new insights from localization studies. Microbiol Mol Biol Rev, 69, 585-607 (2005) (Pubitemid 41798464)
    • (2005) Microbiology and Molecular Biology Reviews , vol.69 , Issue.4 , pp. 585-607
    • Scheffers, D.-J.1    Pinho, M.G.2
  • 27
    • 67349152920 scopus 로고    scopus 로고
    • Levels and localization of mechanosensitive channel proteins in Bacillus subtilis
    • P. G. Wahome, A. E. Cowan, B. Setlow & P. Setlow: Levels and localization of mechanosensitive channel proteins in Bacillus subtilis. Arch Microbiol, 191, 403-14 (2009)
    • (2009) Arch Microbiol , vol.191 , pp. 403-414
    • Wahome, P.G.1    Cowan, A.E.2    Setlow, B.3    Setlow, P.4
  • 28
    • 52649134462 scopus 로고    scopus 로고
    • The major and minor wall teichoic acids prevent the sidewall localization of vegetative DL-endopeptidase LytF in Bacillus subtilis
    • H. Yamamoto, Y. Miyake, M. Hisaoka, S. Kurosawa & J. Sekiguchi: The major and minor wall teichoic acids prevent the sidewall localization of vegetative DL-endopeptidase LytF in Bacillus subtilis. Mol Microbiol, 70, 297-310 (2008)
    • (2008) Mol Microbiol , vol.70 , pp. 297-310
    • Yamamoto, H.1    Miyake, Y.2    Hisaoka, M.3    Kurosawa, S.4    Sekiguchi, J.5
  • 31
    • 77956292192 scopus 로고    scopus 로고
    • Functional microdomains in bacterial membranes
    • D. Lopez & R. Kolter: Functional microdomains in bacterial membranes. Genes Dev, 24, 1893-902 (2010)
    • (2010) Genes Dev , vol.24 , pp. 1893-1902
    • Lopez, D.1    Kolter, R.2
  • 33
    • 79960075043 scopus 로고    scopus 로고
    • Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B. Subtilis
    • E. C. Garner, R. Bernard, W. Wang, X. Zhuang, D. Z. Rudner & T. Mitchison: Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B. subtilis. Science, 333, 222-5 (2011)
    • (2011) Science , vol.333 , pp. 222-225
    • Garner, E.C.1    Bernard, R.2    Wang, W.3    Zhuang, X.4    Rudner, D.Z.5    Mitchison, T.6
  • 36
    • 15944399775 scopus 로고    scopus 로고
    • A magnesium-dependent mreB null mutant: Implications for the role of mreB in Bacillus subtilis
    • DOI 10.1111/j.1365-2958.2005.04506.x
    • A. Formstone & J. Errington: A magnesium-dependent mreB null mutant: implications for the role of mreB in Bacillus subtilis. Mol Microbiol, 55, 1646-57 (2005) (Pubitemid 40445203)
    • (2005) Molecular Microbiology , vol.55 , Issue.6 , pp. 1646-1657
    • Formstone, A.1    Errington, J.2
  • 37
    • 33750713640 scopus 로고    scopus 로고
    • Dynamic localization and interaction with other Bacillus subtilis actin-like proteins are important for the function of MreB
    • DOI 10.1111/j.1365-2958.2006.05457.x
    • H. J. Defeu Soufo & P. L. Graumann: Dynamic localization and interaction with other Bacillus subtilis actin-like proteins are important for the function of MreB. Mol Microbiol, 62, 1340-56 (2006) (Pubitemid 44707198)
    • (2006) Molecular Microbiology , vol.62 , Issue.5 , pp. 1340-1356
    • Defeu Soufo, H.J.1    Graumann, P.L.2
  • 38
    • 36549019685 scopus 로고    scopus 로고
    • The actin-like cytoskeleton
    • Peter Graumann. Caister academic press, Wymondham
    • R. Carballio-López: The actin-like cytoskeleton. In: Bacillus cellular and molecular biology. Eds: Peter Graumann. Caister academic press, Wymondham (2007)
    • (2007) Bacillus Cellular and Molecular Biology
    • Carballio-López, R.1
  • 39
    • 62649172736 scopus 로고    scopus 로고
    • The cell wall regulator {sigma}I specifically suppresses the lethal phenotype of mbl mutants in Bacillus subtilis
    • K. Schirner & J. Errington: The cell wall regulator {sigma}I specifically suppresses the lethal phenotype of mbl mutants in Bacillus subtilis. J Bacteriol, 191, 1404-13 (2009)
    • (2009) J Bacteriol , vol.191 , pp. 1404-1413
    • Schirner, K.1    Errington, J.2
  • 40
    • 70350139098 scopus 로고    scopus 로고
    • Partial functional redundancy of MreB isoforms, MreB, Mbl and MreBH, in cell morphogenesis of Bacillus subtilis
    • Y. Kawai, K. Asai & J. Errington: Partial functional redundancy of MreB isoforms, MreB, Mbl and MreBH, in cell morphogenesis of Bacillus subtilis. Mol Microbiol, 73, 719-31 (2009)
    • (2009) Mol Microbiol , vol.73 , pp. 719-731
    • Kawai, Y.1    Asai, K.2    Errington, J.3
  • 41
    • 23844444807 scopus 로고    scopus 로고
    • Roles for MreC and MreD proteins in helical growth of the cylindrical cell wall in Bacillus subtilis
    • DOI 10.1111/j.1365-2958.2005.04736.x
    • M. Leaver & J. Errington: Roles for MreC and MreD proteins in helical growth of the cylindrical cell wall in Bacillus subtilis. Mol Microbiol, 57, 1196-209 (2005) (Pubitemid 41176518)
    • (2005) Molecular Microbiology , vol.57 , Issue.5 , pp. 1196-1209
    • Leaver, M.1    Errington, J.2
  • 42
    • 0242381270 scopus 로고    scopus 로고
    • Actin-like Proteins MreB and MbI from Bacillus subtilis Are Required for Bipolar Positioning of Replication Origins
    • DOI 10.1016/j.cub.2003.10.024
    • H. J. Defeu Soufo & P. L. Graumann: Actin-like proteins MreB and Mbl from Bacillus subtilis are required for bipolar positioning of replication origins. Curr Biol, 13, 1916-20 (2003) (Pubitemid 37347937)
    • (2003) Current Biology , vol.13 , Issue.21 , pp. 1916-1920
    • Defeu Soufo, H.J.1    Graumann, P.L.2
  • 43
    • 22944489133 scopus 로고    scopus 로고
    • Bacillus subtilis actin-like protein MreB influences the positioning of the replication machinery and requires membrane proteins MreC/D and other actin-like proteins for proper localization
    • H. J. Defeu Soufo & P. L. Graumann: Bacillus subtilis actin-like protein MreB influences the positioning of the replication machinery and requires membrane proteins MreC/D and other actin-like proteins for proper localization. BMC Cell Biol, 6, 10 (2005)
    • (2005) BMC Cell Biol , vol.6 , pp. 10
    • Defeu Soufo, H.J.1    Graumann, P.L.2
  • 44
    • 0028930564 scopus 로고
    • Bacillus subtilis possesses a second determinant with extensive sequence similarity to the Escherichia coli mreB morphogene
    • Y. Abhayawardhane & G. C. Stewart: Bacillus subtilis possesses a second determinant with extensive sequence similarity to the Escherichia coli mreB morphogene. J Bacteriol, 177, 765-73 (1995)
    • (1995) J Bacteriol , vol.177 , pp. 765-773
    • Abhayawardhane, Y.1    Stewart, G.C.2
  • 46
    • 60649104907 scopus 로고    scopus 로고
    • Regulation of cell wall morphogenesis in Bacillus subtilis by recruitment of PBP1 to the MreB helix
    • Y. Kawai, R. A. Daniel & J. Errington: Regulation of cell wall morphogenesis in Bacillus subtilis by recruitment of PBP1 to the MreB helix. Mol Microbiol, 71, 1131-44 (2009)
    • (2009) Mol Microbiol , vol.71 , pp. 1131-1144
    • Kawai, Y.1    Daniel, R.A.2    Errington, J.3
  • 47
    • 36548999439 scopus 로고    scopus 로고
    • Shape determination in Bacillus subtilis
    • DOI 10.1016/j.mib.2007.09.008, PII S1369527407001336, Growth and Development
    • R. Carballido-Lopez & A. Formstone: Shape determination in Bacillus subtilis. Curr Opin Microbiol, 10, 611-6 (2007) (Pubitemid 350180587)
    • (2007) Current Opinion in Microbiology , vol.10 , Issue.6 , pp. 611-616
    • Carballido-Lopez, R.1    Formstone, A.2
  • 48
    • 65449173646 scopus 로고    scopus 로고
    • Distinct and essential morphogenic functions for wall-and lipo-teichoic acids in Bacillus subtilis
    • K. Schirner, J. Marles-Wright, R. J. Lewis & J. Errington: Distinct and essential morphogenic functions for wall-and lipo-teichoic acids in Bacillus subtilis. Embo J, 28, 830-42 (2009)
    • (2009) Embo J , vol.28 , pp. 830-842
    • Schirner, K.1    Marles-Wright, J.2    Lewis, R.J.3    Errington, J.4
  • 49
    • 0347479228 scopus 로고    scopus 로고
    • A continuum of anionic charge: Structures and functions of d-alanyl-teichoic acids in gram-positive bacteria
    • DOI 10.1128/MMBR.67.4.686-723.2003
    • F. C. Neuhaus & J. Baddiley: A continuum of anionic charge: structures and functions of D-alanyl-teichoic acids in gram-positive bacteria. Microbiol Mol Biol Rev, 67, 686-723 (2003) (Pubitemid 37549774)
    • (2003) Microbiology and Molecular Biology Reviews , vol.67 , Issue.4 , pp. 686-723
    • Neuhaus, F.C.1    Baddiley, J.2
  • 51
    • 27744479572 scopus 로고    scopus 로고
    • YvcK of Bacillus subtilis is required for a normal cell shape and for growth on Krebs cycle intermediates and substrates of the pentose phosphate pathway
    • DOI 10.1099/mic.0.28172-0
    • B. Gorke, E. Foulquier & A. Galinier: YvcK of Bacillus subtilis is required for a normal cell shape and for growth on Krebs cycle intermediates and substrates of the pentose phosphate pathway. Microbiology, 151, 3777-91 (2005) (Pubitemid 41632088)
    • (2005) Microbiology , vol.151 , Issue.11 , pp. 3777-3791
    • Gorke, B.1    Foulquier, E.2    Galinier, A.3
  • 52
    • 0035139973 scopus 로고    scopus 로고
    • Putative sigma factor sigI (ykoZ) of Bacillus subtilis is induced by heat shock
    • DOI 10.1128/JB.183.4.1472-1475.2001
    • U. Zuber, K. Drzewiecki & M. Hecker: Putative sigma factor SigI (YkoZ) of Bacillus subtilis is induced by heat shock. J Bacteriol, 183, 1472-5 (2001) (Pubitemid 32107747)
    • (2001) Journal of Bacteriology , vol.183 , Issue.4 , pp. 1472-1475
    • Zuber, U.1    Drzewiecki, K.2    Hecker, M.3
  • 53
    • 39749193958 scopus 로고    scopus 로고
    • Genetic evidence for the actin homolog gene mreBH and the bacitracin resistance gene bcrC as targets of the alternative sigma factor SigI of Bacillus subtilis
    • C. L. Tseng & G. C. Shaw: Genetic evidence for the actin homolog gene mreBH and the bacitracin resistance gene bcrC as targets of the alternative sigma factor SigI of Bacillus subtilis. J Bacteriol, 190, 1561-7 (2008)
    • (2008) J Bacteriol , vol.190 , pp. 1561-1567
    • Tseng, C.L.1    Shaw, G.C.2
  • 54
    • 80054708828 scopus 로고    scopus 로고
    • Genetic evidence for involvement of the alternative sigma factor SigI in controlling expression of the cell wall hydrolase gene lytE and contribution of LytE to heat survival of Bacillus subtilis
    • C. L. Tseng, J. T. Chen, J. H. Lin, W. Z. Huang & G. C. Shaw: Genetic evidence for involvement of the alternative sigma factor SigI in controlling expression of the cell wall hydrolase gene lytE and contribution of LytE to heat survival of Bacillus subtilis. Arch Microbiol, 193, 677-85 (2011)
    • (2011) Arch Microbiol , vol.193 , pp. 677-685
    • Tseng, C.L.1    Chen, J.T.2    Lin, J.H.3    Huang, W.Z.4    Shaw, G.C.5
  • 55
    • 0037494988 scopus 로고    scopus 로고
    • Control of cell morphogenesis in bacteria: Two distinct ways to make a rod-shaped cell
    • DOI 10.1016/S0092-8674(03)00421-5
    • R. A. Daniel & J. Errington: Control of cell morphogenesis in bacteria: two distinct ways to make a rod-shaped cell. Cell, 113, 767-76 (2003) (Pubitemid 36724940)
    • (2003) Cell , vol.113 , Issue.6 , pp. 767-776
    • Daniel, R.A.1    Errington, J.2
  • 57
    • 33745278528 scopus 로고    scopus 로고
    • Cell wall assembly in Bacillus subtilis: How spirals and spaces challenge paradigms
    • A. P. Bhavsar & E. D. Brown: Cell wall assembly in Bacillus subtilis: how spirals and spaces challenge paradigms. Mol Microbiol, 60, 1077-90 (2006)
    • (2006) Mol Microbiol , vol.60 , pp. 1077-1090
    • Bhavsar, A.P.1    Brown, E.D.2
  • 58
    • 39749184735 scopus 로고    scopus 로고
    • Localization and interactions of teichoic acid synthetic enzymes in Bacillus subtilis
    • DOI 10.1128/JB.01394-07
    • A. Formstone, R. Carballido-López, P. Noirot, J. Errington & D. J. Scheffers: Localization and interactions of teichoic acid synthetic enzymes in Bacillus subtilis. J Bacteriol, 190, 1812-21 (2008) (Pubitemid 351304036)
    • (2008) Journal of Bacteriology , vol.190 , Issue.5 , pp. 1812-1821
    • Formstone, A.1    Carballido-Lopez, R.2    Noirot, P.3    Errington, J.4    Scheffers, D.-J.5
  • 59
    • 39149088656 scopus 로고    scopus 로고
    • The penicillin-binding proteins: Structure and role in peptidoglycan biosynthesis
    • DOI 10.1111/j.1574-6976.2008.00105.x
    • E. Sauvage, F. Kerff, M. Terrak, J. A. Ayala & P. Charlier: The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis. FEMS Microbiol Rev, 32, 234-58 (2008) (Pubitemid 351257821)
    • (2008) FEMS Microbiology Reviews , vol.32 , Issue.2 , pp. 234-258
    • Sauvage, E.1    Kerff, F.2    Terrak, M.3    Ayala, J.A.4    Charlier, P.5
  • 60
    • 0037315095 scopus 로고    scopus 로고
    • Peptidoglycan synthesis in the absence of class A penicillin-binding proteins in Bacillus subtilis
    • DOI 10.1128/JB.185.4.1423-1431.2003
    • D. C. McPherson & D. L. Popham: Peptidoglycan synthesis in the absence of class A penicillin-binding proteins in Bacillus subtilis. J Bacteriol, 185, 1423-31 (2003) (Pubitemid 36176876)
    • (2003) Journal of Bacteriology , vol.185 , Issue.4 , pp. 1423-1431
    • McPherson, D.C.1    Popham, D.L.2
  • 61
    • 39149144016 scopus 로고    scopus 로고
    • Bacterial peptidoglycan (murein) hydrolases
    • DOI 10.1111/j.1574-6976.2007.00099.x
    • W. Vollmer, B. Joris, P. Charlier & S. Foster: Bacterial peptidoglycan (murein) hydrolases. FEMS Microbiol Rev, 32, 259-86 (2008) (Pubitemid 351257818)
    • (2008) FEMS Microbiology Reviews , vol.32 , Issue.2 , pp. 259-286
    • Vollmer, W.1    Joris, B.2    Charlier, P.3    Foster, S.4
  • 62
    • 0037858060 scopus 로고    scopus 로고
    • Growth of the stress-bearing and shapemaintaining murein sacculus of Escherichia coli
    • J. V. Holtje: Growth of the stress-bearing and shapemaintaining murein sacculus of Escherichia coli. Microbiol Mol Biol Rev, 62, 181-203 (1998)
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 181-203
    • Holtje, J.V.1
  • 63
    • 0024788767 scopus 로고
    • The origin of the rotation of one end of a cell relative to the other end during growth of gram-positive rods
    • A. L. Koch: The origin of the rotation of one end of a cell relative to the other end during growth of grampositive rods. J Theor Biol, 141, 391-402 (1989) (Pubitemid 20023099)
    • (1989) Journal of Theoretical Biology , vol.141 , Issue.3 , pp. 391-402
    • Koch, A.L.1
  • 65
    • 0029692069 scopus 로고    scopus 로고
    • Lytic transglycosylases
    • J. V. Holtje: Lytic transglycosylases. Exs, 75, 425-9 (1996)
    • (1996) Exs , vol.75 , pp. 425-429
    • Holtje, J.V.1
  • 67
    • 0017802490 scopus 로고
    • Structure of vancomycin and its complex with acetyl-D-alanyl-D-alanine
    • G. M. Sheldrick, P. G. Jones, O. Kennard, D. H. Williams & G. A. Smith: Structure of vancomycin and its complex with acetyl-D-alanyl-D-alanine. Nature, 271, 223-5 (1978) (Pubitemid 8256534)
    • (1978) Nature , vol.271 , Issue.5642 , pp. 223-225
    • Sheldrick, G.M.1    Jones, P.G.2    Kennard, O.3
  • 68
    • 0030971549 scopus 로고    scopus 로고
    • Identification and characterization of pbpA encoding Bacillus subtilis penicillin-binding protein 2A
    • T. Murray, D. L. Popham & P. Setlow: Identification and characterization of pbpA encoding Bacillus subtilis penicillinbinding protein 2A. J Bacteriol, 179, 3021-9 (1997) (Pubitemid 27194453)
    • (1997) Journal of Bacteriology , vol.179 , Issue.9 , pp. 3021-3029
    • Murray, T.1    Popham, D.L.2    Setlow, P.3
  • 69
    • 0042561877 scopus 로고    scopus 로고
    • Rod shape determination by the Bacillus subtilis class B penicillin-binding proteins encoded by pbpA and pbpH
    • DOI 10.1128/JB.185.16.4717-4726.2003
    • Y. Wei, T. Havasy, D. C. McPherson & D. L. Popham: Rod shape determination by the Bacillus subtilis class B penicillin-binding proteins encoded by pbpA and pbpH. J Bacteriol, 185, 4717-26 (2003) (Pubitemid 36962278)
    • (2003) Journal of Bacteriology , vol.185 , Issue.16 , pp. 4717-4726
    • Wei, Y.1    Havasy, T.2    McPherson, D.C.3    Popham, D.L.4
  • 70
    • 0038782140 scopus 로고    scopus 로고
    • Essential nature of the mreC determinant of Bacillus subtilis
    • DOI 10.1128/JB.185.15.4490-4498.2003
    • J. C. Lee & G. C. Stewart: Essential nature of the mreC determinant of Bacillus subtilis. J Bacteriol, 185, 4490-8 (2003) (Pubitemid 36890496)
    • (2003) Journal of Bacteriology , vol.185 , Issue.15 , pp. 4490-4498
    • Lee, J.-C.1    Stewart, G.C.2
  • 71
    • 33751363915 scopus 로고    scopus 로고
    • Dimeric structure of the cell shape protein MreC and its functional implications
    • DOI 10.1111/j.1365-2958.2006.05485.x
    • F. van den Ent, M. Leaver, F. Bendezu, J. Errington, P. de Boer & J. Lowe: Dimeric structure of the cell shape protein MreC and its functional implications. Mol Microbiol, 62, 1631-42 (2006) (Pubitemid 44813809)
    • (2006) Molecular Microbiology , vol.62 , Issue.6 , pp. 1631-1642
    • Van Den Ent, F.1    Leaver, M.2    Bendezu, F.3    Errington, J.4    De Boer, P.5    Lowe, J.6
  • 72
    • 12344306119 scopus 로고    scopus 로고
    • The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex
    • DOI 10.1111/j.1365-2958.2004.04367.x
    • T. Kruse, J. Bork-Jensen & K. Gerdes: The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex. Mol Microbiol, 55, 78-89 (2005) (Pubitemid 40127886)
    • (2005) Molecular Microbiology , vol.55 , Issue.1 , pp. 78-89
    • Kruse, T.1    Bork-Jensen, J.2    Gerdes, K.3
  • 73
    • 42549145631 scopus 로고    scopus 로고
    • Control of the cell elongation-division cycle by shuttling of PBP1 protein in Bacillus subtilis
    • DOI 10.1111/j.1365-2958.2008.06210.x
    • D. Claessen, R. Emmins, L. W. Hamoen, R. A. Daniel, J. Errington & D. H. Edwards: Control of the cell elongationdivision cycle by shuttling of PBP1 protein in Bacillus subtilis. Mol Microbiol, 68, 1029-46 (2008) (Pubitemid 351581066)
    • (2008) Molecular Microbiology , vol.68 , Issue.4 , pp. 1029-1046
    • Claessen, D.1    Emmins, R.2    Hamoen, L.W.3    Daniel, R.A.4    Errington, J.5    Edwards, D.H.6
  • 74
    • 23844436270 scopus 로고    scopus 로고
    • Taking shape: Control of bacterial cell wall biosynthesis
    • DOI 10.1111/j.1365-2958.2005.04760.x
    • G. C. Stewart: Taking shape: control of bacterial cell wall biosynthesis. Mol Microbiol, 57, 1177-81 (2005) (Pubitemid 41176516)
    • (2005) Molecular Microbiology , vol.57 , Issue.5 , pp. 1177-1181
    • Stewart, G.C.1
  • 75
    • 0031944802 scopus 로고    scopus 로고
    • Control of cell shape and elongation by the rodA gene in Bacillus subtilis
    • DOI 10.1046/j.1365-2958.1998.00766.x
    • A. O. Henriques, P. Glaser, P. J. Piggot & C. P. Moran, Jr.: Control of cell shape and elongation by the rodA gene in Bacillus subtilis. Mol Microbiol, 28, 235-47 (1998) (Pubitemid 28182248)
    • (1998) Molecular Microbiology , vol.28 , Issue.2 , pp. 235-247
    • Henriques, A.O.1    Glaser, P.2    Piggot, P.J.3    Moran Jr., C.P.4
  • 80
    • 15744378137 scopus 로고    scopus 로고
    • Chromosomal replication and the cell membrane
    • DOI 10.1016/j.mib.2005.02.006, Cell Regulation
    • K. Boeneman & E. Crooke: Chromosomal replication and the cell membrane. Curr Opin Microbiol, 8, 143-8 (2005) (Pubitemid 40417954)
    • (2005) Current Opinion in Microbiology , vol.8 , Issue.2 , pp. 143-148
    • Boeneman, K.1    Crooke, E.2
  • 81
    • 11844289696 scopus 로고    scopus 로고
    • Compartmentalization of prokaryotic DNA replication
    • DOI 10.1016/j.femsre.2004.06.003, PII S0168644504000488
    • A. Bravo, G. Serrano-Heras & M. Salas: Compartmentalization of prokaryotic DNA replication. FEMS Microbiol Rev, 29, 25-47 (2005) (Pubitemid 40094764)
    • (2005) FEMS Microbiology Reviews , vol.29 , Issue.1 , pp. 25-47
    • Bravo, A.1    Serrano-Heras, G.2    Salas, M.3
  • 83
    • 59949103493 scopus 로고    scopus 로고
    • Assembly properties of the Bacillus subtilis actin, MreB
    • J. A. Mayer & K. J. Amann: Assembly properties of the Bacillus subtilis actin, MreB. Cell Motil Cytoskeleton, 66, 109-18 (2009)
    • (2009) Cell Motil Cytoskeleton , vol.66 , pp. 109-118
    • Mayer, J.A.1    Amann, K.J.2
  • 85
    • 13244278205 scopus 로고    scopus 로고
    • The assembly of MreB, a prokaryotic homolog of actin
    • DOI 10.1074/jbc.M410298200
    • O. Esue, M. Cordero, D. Wirtz & Y. Tseng: The assembly of MreB, a prokaryotic homolog of Actin. J Biol Chem, 280, 2628-35 (2005) (Pubitemid 40189366)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.4 , pp. 2628-2635
    • Esue, O.1    Cordero, M.2    Wirtz, D.3    Tseng, Y.4
  • 86
    • 31344480941 scopus 로고    scopus 로고
    • GTPase activity, structure, and mechanical properties of filaments assembled from bacterial cytoskeleton protein MreB
    • DOI 10.1128/JB.188.3.968-976.2006
    • O. Esue, D. Wirtz & Y. Tseng: GTPase activity, structure, and mechanical properties of filaments assembled from bacterial cytoskeleton protein MreB. J Bacteriol, 188, 968-76 (2006) (Pubitemid 43146413)
    • (2006) Journal of Bacteriology , vol.188 , Issue.3 , pp. 968-976
    • Esue, O.1    Wirtz, D.2    Tseng, Y.3
  • 87
    • 38849114991 scopus 로고    scopus 로고
    • Polymerization properties of the Thermotoga maritima actin MreB: Roles of temperature, nucleotides, and ions
    • DOI 10.1021/bi701538e
    • G. J. Bean & K. J. Amann: Polymerization properties of the Thermotoga maritima actin MreB: roles of temperature, nucleotides, and ions. Biochemistry, 47, 826-35 (2008) (Pubitemid 351195454)
    • (2008) Biochemistry , vol.47 , Issue.2 , pp. 826-835
    • Bean, G.J.1    Amann, K.J.2
  • 90
    • 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
    • DOI 10.1073/pnas.1232225100
    • Y. L. Shih, T. Le & L. Rothfield: 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, 7865-70 (2003) (Pubitemid 36760061)
    • (2003) Proceedings of the National Academy of Sciences of the United States of America , vol.100 , Issue.13 , pp. 7865-7870
    • Shih, Y.-L.1    Le, T.2    Rothfield, L.3
  • 91
    • 77955449195 scopus 로고    scopus 로고
    • Membrane potential is important for bacterial cell division
    • H. Strahl & L. W. Hamoen: Membrane potential is important for bacterial cell division. Proc Natl Acad Sci U S A, 107, 12281-6 (2010)
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 12281-12286
    • Strahl, H.1    Hamoen, L.W.2
  • 93
    • 62949149564 scopus 로고    scopus 로고
    • Assembly of the MreB-associated cytoskeletal ring of Escherichia coli
    • P. Vats, Y. L. Shih & L. Rothfield: Assembly of the MreB-associated cytoskeletal ring of Escherichia coli. Mol Microbiol, 72, 170-82 (2009)
    • (2009) Mol Microbiol , vol.72 , pp. 170-182
    • Vats, P.1    Shih, Y.L.2    Rothfield, L.3
  • 94
    • 33745000523 scopus 로고    scopus 로고
    • Visualization of cellulose synthase demonstrates functional association with microtubules
    • DOI 10.1126/science.1126551
    • A. R. Paredez, C. R. Somerville & D. W. Ehrhardt: Visualization of cellulose synthase demonstrates functional association with microtubules. Science, 312, 1491-5 (2006) (Pubitemid 43865881)
    • (2006) Science , vol.312 , Issue.5779 , pp. 1491-1495
    • Paredez, A.R.1    Somerville, C.R.2    Ehrhardt, D.W.3
  • 95
    • 34548677525 scopus 로고    scopus 로고
    • The cell shape proteins MreB and MreC control cell morphogenesis by positioning cell wall synthetic complexes
    • DOI 10.1111/j.1365-2958.2007.05910.x
    • A. V. Divakaruni, C. Baida, C. L. White & J. W. Gober: The cell shape proteins MreB and MreC control cell morphogenesis by positioning cell wall synthetic complexes. Mol Microbiol, 66, 174-88 (2007) (Pubitemid 47414799)
    • (2007) Molecular Microbiology , vol.66 , Issue.1 , pp. 174-188
    • Divakaruni, A.V.1    Baida, C.2    White, C.L.3    Gober, J.W.4
  • 96
    • 77951608842 scopus 로고    scopus 로고
    • Positioning cell wall synthetic complexes by the bacterial morphogenetic proteins MreB and MreD
    • C. L. White, A. Kitich & J. W. Gober: Positioning cell wall synthetic complexes by the bacterial morphogenetic proteins MreB and MreD. Mol Microbiol, 76, 616-33 (2010)
    • (2010) Mol Microbiol , vol.76 , pp. 616-633
    • White, C.L.1    Kitich, A.2    Gober, J.W.3
  • 97
    • 79960194325 scopus 로고    scopus 로고
    • Mutations in the nucleotide binding pocket of MreB can alter cell curvature and polar morphology in Caulobacter
    • N. A. Dye, Z. Pincus, I. C. Fisher, L. Shapiro & J. A. Theriot: Mutations in the nucleotide binding pocket of MreB can alter cell curvature and polar morphology in Caulobacter. Mol Microbiol, 81, 368-94 (2011)
    • (2011) Mol Microbiol , vol.81 , pp. 368-394
    • Dye, N.A.1    Pincus, Z.2    Fisher, I.C.3    Shapiro, L.4    Theriot, J.A.5
  • 98
    • 27844566174 scopus 로고    scopus 로고
    • Towards a comprehensive view of the bacterial cell wall
    • DOI 10.1016/j.tim.2005.10.001, PII S0966842X05002593
    • B. Dmitriev, F. Toukach & S. Ehlers: Towards a comprehensive view of the bacterial cell wall. Trends Microbiol, 13, 569-74 (2005) (Pubitemid 41661337)
    • (2005) Trends in Microbiology , vol.13 , Issue.12 , pp. 569-574
    • Dmitriev, B.1    Toukach, F.2    Ehlers, S.3
  • 99
    • 77949421358 scopus 로고    scopus 로고
    • MreB drives de novo rod morphogenesis in Caulobacter crescentus via remodeling of the cell wall
    • C. N. Takacs, S. Poggio, G. Charbon, M. Pucheault, W. Vollmer & C. Jacobs-Wagner: MreB drives de novo rod morphogenesis in Caulobacter crescentus via remodeling of the cell wall. J Bacteriol, 192, 1671-84 (2010)
    • (2010) J Bacteriol , vol.192 , pp. 1671-1684
    • Takacs, C.N.1    Poggio, S.2    Charbon, G.3    Pucheault, M.4    Vollmer, W.5    Jacobs-Wagner, C.6
  • 100
    • 36249024229 scopus 로고    scopus 로고
    • Cytokinesis: Placing and making the final cut
    • DOI 10.1016/j.cell.2007.11.011, PII S0092867407014638
    • F. A. Barr & U. Gruneberg: Cytokinesis: placing and making the final cut. Cell, 131, 847-60 (2007) (Pubitemid 350138092)
    • (2007) Cell , vol.131 , Issue.5 , pp. 847-860
    • Barr, F.A.1    Gruneberg, U.2
  • 101
    • 34548160002 scopus 로고    scopus 로고
    • Control of actin assembly dynamics in cell motility
    • DOI 10.1074/jbc.R700020200
    • M. F. Carlier & D. Pantaloni: Control of actin assembly dynamics in cell motility. J Biol Chem, 282, 23005-9 (2007) (Pubitemid 47311896)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.32 , pp. 23005-23009
    • Carlier, M.-F.1    Pantaloni, D.2
  • 102
    • 34547959158 scopus 로고    scopus 로고
    • Actin in membrane trafficking
    • DOI 10.1016/j.ceb.2007.04.017, PII S0955067407000786
    • L. Lanzetti: Actin in membrane trafficking. Curr Opin Cell Biol, 19, 453-8 (2007) (Pubitemid 47268758)
    • (2007) Current Opinion in Cell Biology , vol.19 , Issue.4 , pp. 453-458
    • Lanzetti, L.1
  • 103
    • 46449093431 scopus 로고    scopus 로고
    • Molecular mechanisms of phagocytic uptake in mammalian cells
    • E. Groves, A. E. Dart, V. Covarelli & E. Caron: Molecular mechanisms of phagocytic uptake in mammalian cells. Cell Mol Life Sci, 65, 1957-76 (2008)
    • (2008) Cell Mol Life Sci , vol.65 , pp. 1957-1976
    • Groves, E.1    Dart, A.E.2    Covarelli, V.3    Caron, E.4
  • 104
    • 42049092972 scopus 로고    scopus 로고
    • Regulation of actin assembly associated with protrusion and adhesion in cell migration
    • DOI 10.1152/physrev.00021.2007
    • C. Le Clainche & M. F. Carlier: Regulation of actin assembly associated with protrusion and adhesion in cell migration. Physiol Rev, 88, 489-513 (2008) (Pubitemid 351520086)
    • (2008) Physiological Reviews , vol.88 , Issue.2 , pp. 489-513
    • Le Clainche, C.1    Carlier, M.-F.2
  • 105
    • 34248531149 scopus 로고    scopus 로고
    • Translocation of mRNAs by molecular motors: Think complex?
    • DOI 10.1016/j.semcdb.2007.01.004, PII S1084952107000262, Mechanisms and biological significance of RNA localization AND Development of ectodermal appendages
    • S. L. Bullock: Translocation of mRNAs by molecular motors: think complex? Semin Cell Dev Biol, 18, 194-201 (2007) (Pubitemid 46756362)
    • (2007) Seminars in Cell and Developmental Biology , vol.18 , Issue.2 , pp. 194-201
    • Bullock, S.L.1
  • 106
    • 35948978460 scopus 로고    scopus 로고
    • Moving mitochondria: Establishing distribution of an essential organelle
    • DOI 10.1111/j.1600-0854.2007.00644.x
    • R. L. Frederick & J. M. Shaw: Moving mitochondria: establishing distribution of an essential organelle. Traffic, 8, 1668-75 (2007) (Pubitemid 350066679)
    • (2007) Traffic , vol.8 , Issue.12 , pp. 1668-1675
    • Frederick, R.L.1    Shaw, J.M.2
  • 107
    • 39149138988 scopus 로고    scopus 로고
    • Cargo transport: Molecular motors navigate a complex cytoskeleton
    • J. L. Ross, M. Y. Ali & D. M. Warshaw: Cargo transport: molecular motors navigate a complex cytoskeleton. Curr Opin Cell Biol, 20, 41-7 (2008)
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 41-47
    • Ross, J.L.1    Ali, M.Y.2    Warshaw, D.M.3
  • 108
    • 77956020315 scopus 로고    scopus 로고
    • Regulation of actin cytoskeleton dynamics in cells
    • S. H. Lee & R. Dominguez: Regulation of actin cytoskeleton dynamics in cells. Mol Cells, 29, 311-25 (2010)
    • (2010) Mol Cells , vol.29 , pp. 311-325
    • Lee, S.H.1    Dominguez, R.2
  • 109
    • 78649658087 scopus 로고    scopus 로고
    • Bridging cell wall biosynthesis and bacterial morphogenesis
    • P. J. Mattei, D. Neves & A. Dessen: Bridging cell wall biosynthesis and bacterial morphogenesis. Curr Opin Struct Biol, 20, 749-55 (2010)
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 749-755
    • Mattei, P.J.1    Neves, D.2    Dessen, A.3
  • 110
    • 79952114513 scopus 로고    scopus 로고
    • The structure and function of bacterial actin homologs
    • J. W. Shaevitz & Z. Gitai: The structure and function of bacterial actin homologs. Cold Spring Harb Perspect Biol, 2, a000364 (2010)
    • (2010) Cold Spring Harb Perspect Biol , vol.2
    • Shaevitz, J.W.1    Gitai, Z.2
  • 111
    • 59649113418 scopus 로고    scopus 로고
    • RodZ (YfgA) is required for proper assembly of the MreB actin cytoskeleton and cell shape in E. Coli
    • F. O. Bendezu, C. A. Hale, T. G. Bernhardt & P. A. de Boer: RodZ (YfgA) is required for proper assembly of the MreB actin cytoskeleton and cell shape in E. coli. Embo J, 28, 193-204 (2009)
    • (2009) Embo J , vol.28 , pp. 193-204
    • Bendezu, F.O.1    Hale, C.A.2    Bernhardt, T.G.3    De Boer, P.A.4
  • 112
    • 27944489446 scopus 로고    scopus 로고
    • The MreB and Min cytoskeletal-like systems play independent roles in prokaryotic polar differentiation
    • DOI 10.1111/j.1365-2958.2005.04841.x
    • Y. L. Shih, I. Kawagishi & L. Rothfield: The MreB and Min cytoskeletal-like systems play independent roles in prokaryotic polar differentiation. Mol Microbiol, 58, 917-28 (2005) (Pubitemid 41667215)
    • (2005) Molecular Microbiology , vol.58 , Issue.4 , pp. 917-928
    • Shih, Y.-L.1    Kawagishi, I.2    Rothfield, L.3
  • 113
    • 57149120088 scopus 로고    scopus 로고
    • Determination of bacterial rod shape by a novel cytoskeletal membrane protein
    • D. Shiomi, M. Sakai & H. Niki: Determination of bacterial rod shape by a novel cytoskeletal membrane protein. Embo J, 27, 3081-91 (2008)
    • (2008) Embo J , vol.27 , pp. 3081-3091
    • Shiomi, D.1    Sakai, M.2    Niki, H.3
  • 114
    • 77949567575 scopus 로고    scopus 로고
    • Bacterial actin MreB assembles in complex with cell shape protein RodZ
    • F. van den Ent, C. M. Johnson, L. Persons, P. de Boer & J. Lowe: Bacterial actin MreB assembles in complex with cell shape protein RodZ. Embo J, 29, 1081-90 (2010)
    • (2010) Embo J , vol.29 , pp. 1081-1090
    • Van Den Ent, F.1    Johnson, C.M.2    Persons, L.3    De Boer, P.4    Lowe, J.5
  • 115
    • 0022839488 scopus 로고
    • Peptidoglycan synthetic activities in membranes of Escherichia coli caused by overproduction of penicillin-binding protein 2 and RodA protein
    • F. Ishino, W. Park, S. Tomioka, S. Tamaki, I. Takase, K. Kunugita, H. Matsuzawa, S. Asoh, T. Ohta, B. G. Spratt & et al.: Peptidoglycan synthetic activities in membranes of Escherichia coli caused by overproduction of penicillinbinding protein 2 and RodA protein. J Biol Chem, 261, 7024-31 (1986) (Pubitemid 17219476)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.15 , pp. 7024-7031
    • Ishino, F.1    Park, W.2    Tomioka, S.3
  • 116
    • 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
    • DOI 10.1111/j.1365-2958.2007.05851.x
    • T. Mohammadi, A. Karczmarek, M. Crouvoisier, A. Bouhss, D. Mengin-Lecreulx & T. den Blaauwen: 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, 1106-21 (2007) (Pubitemid 47221085)
    • (2007) Molecular Microbiology , vol.65 , Issue.4 , pp. 1106-1121
    • Mohammadi, T.1    Karczmarek, A.2    Crouvoisier, M.3    Bouhss, A.4    Mengin-Lecreulx, D.5    Den Blaauwen, T.6
  • 117
    • 34250627500 scopus 로고    scopus 로고
    • DNA and origin region segregation are not affected by the transition from rod to sphere after inhibition of Escherichia coli MreB by A22
    • DOI 10.1111/j.1365-2958.2007.05777.x
    • A. Karczmarek, R. Martinez-Arteaga, S. Alexeeva, F. G. Hansen, M. Vicente, N. Nanninga & T. den Blaauwen: DNA and origin region segregation are not affected by the transition from rod to sphere after inhibition of Escherichia coli MreB by A22. Mol Microbiol, 65, 51-63 (2007) (Pubitemid 46934491)
    • (2007) Molecular Microbiology , vol.65 , Issue.1 , pp. 51-63
    • Karczmarek, A.1    Baselga, R.M.-A.2    Alexeeva, S.3    Hansen, F.G.4    Vicente, M.5    Nanninga, N.6    Den Blaauwen, T.7
  • 118
    • 29944438325 scopus 로고    scopus 로고
    • Actin homolog MreB and RNA polymerase interact and are both required for chromosome segregation in Escherichia coli
    • DOI 10.1101/gad.366606
    • T. Kruse, B. Blagoev, A. Lobner-Olesen, M. Wachi, K. Sasaki, N. Iwai, M. Mann & K. Gerdes: Actin homolog MreB and RNA polymerase interact and are both required for chromosome segregation in Escherichia coli. Genes Dev, 20, 113-24 (2006) (Pubitemid 43042672)
    • (2006) Genes and Development , vol.20 , Issue.1 , pp. 113-124
    • Kruse, T.1    Blagoev, B.2    Lobner-Olesen, A.3    Wachi, M.4    Sasaki, K.5    Iwai, N.6    Mann, M.7    Gerdes, K.8
  • 119
    • 58649111971 scopus 로고    scopus 로고
    • Actin homolog MreB affects chromosome segregation by regulating topoisomerase IV in Escherichia coli
    • R. Madabhushi & K. J. Marians: Actin homolog MreB affects chromosome segregation by regulating topoisomerase IV in Escherichia coli. Mol Cell, 33, 171-80 (2009)
    • (2009) Mol Cell , vol.33 , pp. 171-180
    • Madabhushi, R.1    Marians, K.J.2
  • 120
    • 78649369567 scopus 로고    scopus 로고
    • Independent segregation of the two arms of the Escherichia coli ori region requires neither RNA synthesis nor MreB dynamics
    • X. Wang & D. J. Sherratt: Independent segregation of the two arms of the Escherichia coli ori region requires neither RNA synthesis nor MreB dynamics. J Bacteriol, 192, 6143-53 (2010)
    • (2010) J Bacteriol , vol.192 , pp. 6143-6153
    • Wang, X.1    Sherratt, D.J.2
  • 125
    • 63449129067 scopus 로고    scopus 로고
    • Growth conditions regulate the requirements for Caulobacter chromosome segregation
    • C. W. Shebelut, R. B. Jensen & Z. Gitai: Growth conditions regulate the requirements for Caulobacter chromosome segregation. J Bacteriol, 191, 1097-100 (2009)
    • (2009) J Bacteriol , vol.191 , pp. 1097-1100
    • Shebelut, C.W.1    Jensen, R.B.2    Gitai, Z.3
  • 126
    • 55749095037 scopus 로고    scopus 로고
    • Caulobacter requires a dedicated mechanism to initiate chromosome segregation
    • E. Toro, S. H. Hong, H. H. McAdams & L. Shapiro: Caulobacter requires a dedicated mechanism to initiate chromosome segregation. Proc Natl Acad Sci U S A, 105, 15435-40 (2008)
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 15435-15440
    • Toro, E.1    Hong, S.H.2    McAdams, H.H.3    Shapiro, L.4
  • 127
    • 11844281590 scopus 로고    scopus 로고
    • Caulobacter crescentus requires RodA and MreB for stalk synthesis and prevention of ectopic pole formation
    • DOI 10.1128/JB.187.2.544-553.2005
    • J. K. Wagner, C. D. Galvani & Y. V. Brun: Caulobacter crescentus requires RodA and MreB for stalk synthesis and prevention of ectopic pole formation. J Bacteriol, 187, 544-53 (2005) (Pubitemid 40096243)
    • (2005) Journal of Bacteriology , vol.187 , Issue.2 , pp. 544-553
    • Wagner, J.K.1    Galvani, C.D.2    Brun, Y.V.3
  • 128
    • 0027518411 scopus 로고
    • Round-cell mutants of Salmonella typhimurium produced by transposition mutagenesis: Lethality of rodA and mre mutations
    • DOI 10.1007/BF00277138
    • C. S. Costa & D. N. Anton: Round-cell mutants of Salmonella typhimurium produced by transposition mutagenesis: lethality of rodA and mre mutations. Mol Gen Genet, 236, 387-94 (1993) (Pubitemid 23055581)
    • (1993) Molecular and General Genetics , vol.236 , Issue.2-3 , pp. 387-394
    • Costa, C.S.1    Anton, D.N.2
  • 129
    • 4344586377 scopus 로고    scopus 로고
    • Extended phenotype of an mreB-like mutant in Azospirillum brasilense
    • E. G. Biondi, F. Marini, F. Altieri, L. Bonzi, M. Bazzicalupo & M. del Gallo: Extended phenotype of an mreB-like mutant in Azospirillum brasilense. Microbiology, 150, 2465-74 (2004) (Pubitemid 39117658)
    • (2004) Microbiology , vol.150 , Issue.7 , pp. 2465-2474
    • Biondi, E.G.1    Marini, F.2    Altieri, F.3    Bonzi, L.4    Bazzicalupo, M.5    Del Gallo, M.6
  • 130
    • 33947211308 scopus 로고    scopus 로고
    • MreB is important for cell shape but not for chromosome segregation of the filamentous cyanobacterium Anabaena sp. PCC 7120
    • DOI 10.1111/j.1365-2958.2007.05618.x
    • B. Hu, G. Yang, W. Zhao, Y. Zhang & J. Zhao: MreB is important for cell shape but not for chromosome segregation of the filamentous cyanobacterium Anabaena sp. PCC 7120. Mol Microbiol, 63, 1640-52 (2007) (Pubitemid 46426700)
    • (2007) Molecular Microbiology , vol.63 , Issue.6 , pp. 1640-1652
    • Hu, B.1    Yang, G.2    Zhao, W.3    Zhang, Y.4    Zhao, J.5
  • 131
    • 55049102938 scopus 로고    scopus 로고
    • Dynamic localization of MreB in Vibrio parahaemolyticus and in the ectopic host bacterium Escherichia coli
    • S. W. Chiu, S. Y. Chen & H. C. Wong: Dynamic localization of MreB in Vibrio parahaemolyticus and in the ectopic host bacterium Escherichia coli. Appl Environ Microbiol, 74, 6739-45 (2008)
    • (2008) Appl Environ Microbiol , vol.74 , pp. 6739-6745
    • Chiu, S.W.1    Chen, S.Y.2    Wong, H.C.3
  • 133
    • 77749288955 scopus 로고    scopus 로고
    • Manipulating each MreB of Bdellovibrio bacteriovorus gives diverse morphological and predatory phenotypes
    • A. K. Fenton, C. Lambert, P. C. Wagstaff & R. E. Sockett: Manipulating each MreB of Bdellovibrio bacteriovorus gives diverse morphological and predatory phenotypes. J Bacteriol, 192, 1299-311 (2010)
    • (2010) J Bacteriol , vol.192 , pp. 1299-1311
    • Fenton, A.K.1    Lambert, C.2    Wagstaff, P.C.3    Sockett, R.E.4
  • 134
    • 11144257131 scopus 로고    scopus 로고
    • Localization of MreB in Rhodobacter sphaeroides under conditions causing changes in cell shape and membrane structure
    • DOI 10.1128/JB.187.1.54-64.2005
    • P. M. Slovak, G. H. Wadhams & J. P. Armitage: Localization of MreB in Rhodobacter sphaeroides under conditions causing changes in cell shape and membrane structure. J Bacteriol, 187, 54-64 (2005) (Pubitemid 40024180)
    • (2005) Journal of Bacteriology , vol.187 , Issue.1 , pp. 54-64
    • Slovak, P.M.1    Wadhams, G.H.2    Armitage, J.P.3
  • 136
    • 77953509169 scopus 로고    scopus 로고
    • Surface association and the MreB cytoskeleton regulate pilus production, localization and function in Pseudomonas aeruginosa
    • K. N. Cowles & Z. Gitai: Surface association and the MreB cytoskeleton regulate pilus production, localization and function in Pseudomonas aeruginosa. Mol Microbiol, 76, 1411-26 (2010)
    • (2010) Mol Microbiol , vol.76 , pp. 1411-1426
    • Cowles, K.N.1    Gitai, Z.2
  • 137
    • 75049084936 scopus 로고    scopus 로고
    • Bacterial motility complexes require the actin-like protein, MreB and the Ras homologue, MglA
    • E. M. Mauriello, F. Mouhamar, B. Nan, A. Ducret, D. Dai, D. R. Zusman & T. Mignot: Bacterial motility complexes require the actin-like protein, MreB and the Ras homologue, MglA. Embo J, 29, 315-26 (2010)
    • (2010) Embo J , vol.29 , pp. 315-326
    • Mauriello, E.M.1    Mouhamar, F.2    Nan, B.3    Ducret, A.4    Dai, D.5    Zusman, D.R.6    Mignot, T.7
  • 138
    • 35048848634 scopus 로고    scopus 로고
    • Changes in nucleoid morphology and origin localization upon inhibition or alteration of the actin homolog, MreB, of Vibrio cholerae
    • DOI 10.1128/JB.00362-07
    • P. Srivastava, G. Demarre, T. S. Karpova, J. McNally & D. K. Chattoraj: Changes in nucleoid morphology and origin localization upon inhibition or alteration of the actin homolog, MreB, of Vibrio cholerae. J Bacteriol, 189, 7450-63 (2007) (Pubitemid 47557362)
    • (2007) Journal of Bacteriology , vol.189 , Issue.20 , pp. 7450-7463
    • Srivastava, P.1    Demarre, G.2    Karpova, T.S.3    McNally, J.4    Chattoraj, D.K.5
  • 139
    • 66649138900 scopus 로고    scopus 로고
    • A22 disrupts the bacterial actin cytoskeleton by directly binding and inducing a low-affinity state in MreB
    • G. J. Bean, S. T. Flickinger, W. M. Westler, M. E. McCully, D. Sept, D. B. Weibel & K. J. Amann: A22 disrupts the bacterial actin cytoskeleton by directly binding and inducing a low-affinity state in MreB. Biochemistry, 48, 4852-7 (2009)
    • (2009) Biochemistry , vol.48 , pp. 4852-4857
    • Bean, G.J.1    Flickinger, S.T.2    Westler, W.M.3    McCully, M.E.4    Sept, D.5    Weibel, D.B.6    Amann, K.J.7
  • 140
    • 13544274210 scopus 로고    scopus 로고
    • MreB actin-mediated segregation of a specific region of a bacterial chromosome
    • DOI 10.1016/j.cell.2005.01.007
    • Z. Gitai, N. A. Dye, A. Reisenauer, M. Wachi & L. Shapiro: MreB actin-mediated segregation of a specific region of a bacterial chromosome. Cell, 120, 329-41 (2005) (Pubitemid 40222428)
    • (2005) Cell , vol.120 , Issue.3 , pp. 329-341
    • Gitai, Z.1    Dye, N.A.2    Reisenauer, A.3    Wachi, M.4    Shapiro, L.5
  • 141
    • 0041701451 scopus 로고    scopus 로고
    • Novel S-benzylisothiourea compound that induces spherical cells in Escherichia coli probably by acting on a rod-shape-determining protein(s) other than penicillin-binding protein 2
    • N. Iwai, K. Nagai & M. Wachi: Novel Sbenzylisothiourea compound that induces spherical cells in Escherichia coli probably by acting on a rod-shapedetermining protein (s) other than penicillin-binding protein 2. Biosci Biotechnol Biochem, 66, 2658-62 (2002) (Pubitemid 39251140)
    • (2002) Bioscience, Biotechnology and Biochemistry , vol.66 , Issue.12 , pp. 2658-2662
    • Iwai, N.1    Nagai, K.2    Wachi, M.3


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