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Volumn 24, Issue 15, 2013, Pages 2340-2349

Motion of variable-length MreB filaments at the bacterial cell membrane influences cell morphology

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; MREB PROTEIN;

EID: 84881036933     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E12-10-0728     Document Type: Article
Times cited : (75)

References (50)
  • 1
    • 69249126551 scopus 로고    scopus 로고
    • Bacterial cell division: Assembly, maintenance and disassembly of the Z ring
    • Adams DW, Errington J (2009). Bacterial cell division: assembly, maintenance and disassembly of the Z ring. Nat Rev Microbiol 7, 642-653.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 642-653
    • Adams, D.W.1    Errington, J.2
  • 2
    • 82555169596 scopus 로고    scopus 로고
    • Self-assembling enzymes and the origins of the cytoskeleton
    • Barry RM, Gitai Z (2011). Self-assembling enzymes and the origins of the cytoskeleton. Curr Opin Microbiol 14, 704-711.
    • (2011) Curr Opin Microbiol , vol.14 , pp. 704-711
    • Barry, R.M.1    Gitai, Z.2
  • 3
    • 39749142159 scopus 로고    scopus 로고
    • Conditional lethality, division defects, membrane involution, and endocytosis in mre and mrd shape mutants of Escherichia coli
    • Bendezu FO, de Boer PA (2008). Conditional lethality, division defects, membrane involution, and endocytosis in mre and mrd shape mutants of Escherichia coli. J Bacteriol 190, 1792-1811.
    • (2008) J Bacteriol , vol.190 , pp. 1792-1811
    • Bendezu, F.O.1    De Boer, P.A.2
  • 4
    • 59649113418 scopus 로고    scopus 로고
    • RodZ (YfgA) is required for proper assembly of the MreB actin cytoskeleton and cell shape in E. Coli
    • Bendezu FO, Hale CA, Bernhardt TG, de Boer PA (2009). RodZ (YfgA) is required for proper assembly of the MreB actin cytoskeleton and cell shape in E. coli. EMBO J 28, 193-204.
    • (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
  • 7
    • 0037237123 scopus 로고    scopus 로고
    • The bacterial cytoskeleton: In vivo dynamics of the actin-like protein Mbl of Bacillus subtilis
    • Carballido-Lopez R, Errington J (2003). The bacterial cytoskeleton: in vivo dynamics of the actin-like protein Mbl of Bacillus subtilis. Dev Cell 4, 19-28.
    • (2003) Dev Cell , vol.4 , pp. 19-28
    • Carballido-Lopez, R.1    Errington, J.2
  • 8
    • 33747837700 scopus 로고    scopus 로고
    • Actin homolog MreBH governs cell morphogenesis by localization of the cell wall hydrolase LytE
    • Carballido-Lopez R, Formstone A, Li Y, Ehrlich SD, Noirot P, Errington J (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
  • 9
    • 77953509169 scopus 로고    scopus 로고
    • Surface association and the MreB cytoskeleton regulate pilus production, localization and function in Pseudomonas aeruginosa
    • Cowles KN, Gitai Z (2010). Surface association and the MreB cytoskeleton regulate pilus production, localization and function in Pseudomonas aeruginosa. Mol Microbiol 76, 1411-1426.
    • (2010) Mol Microbiol , vol.76 , pp. 1411-1426
    • Cowles, K.N.1    Gitai, Z.2
  • 10
    • 4444285310 scopus 로고    scopus 로고
    • Dynamic movement of actin-like proteins within bacterial cells
    • Defeu Soufo HJ, Graumann PL (2004). Dynamic movement of actin-like proteins within bacterial cells. EMBO Rep 5, 789-794.
    • (2004) EMBO Rep , vol.5 , pp. 789-794
    • Defeu Soufo, H.J.1    Graumann, P.L.2
  • 11
    • 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
    • Defeu Soufo HJ, Graumann PL (2005). 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) BMC Cell Biol , vol.6 , pp. 10
    • Defeu Soufo, H.J.1    Graumann, P.L.2
  • 12
    • 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 HJ, Graumann PL (2006). Dynamic localization and interaction with other Bacillus subtilis actin-like proteins are important for the function of MreB. Mol Microbiol 62, 1340-1356.
    • (2006) Mol Microbiol , vol.62 , pp. 1340-1356
    • Defeu Soufo, H.J.1    Graumann, P.L.2
  • 13
    • 78649543920 scopus 로고    scopus 로고
    • Bacillus subtilis MreB paralogues have different filament architectures and lead to shape remodelling of a heterologous cell system
    • Defeu Soufo HJ, Graumann PL (2010). Bacillus subtilis MreB paralogues have different filament architectures and lead to shape remodelling of a heterologous cell system. Mol Microbiol 78, 1145-1158.
    • (2010) Mol Microbiol , vol.78 , pp. 1145-1158
    • Defeu Soufo, H.J.1    Graumann, P.L.2
  • 14
    • 84858181839 scopus 로고    scopus 로고
    • Bacillus subtilis MreB orthologs self-organize into filamentous structures underneath the cell membrane in a heterologous cell system
    • Dempwolff F, Reimold C, Reth M, Graumann PL (2011). Bacillus subtilis MreB orthologs self-organize into filamentous structures underneath the cell membrane in a heterologous cell system. PLoS One 6, e27035.
    • (2011) PLoS One , vol.6
    • Dempwolff, F.1    Reimold, C.2    Reth, M.3    Graumann, P.L.4
  • 15
    • 29344476196 scopus 로고    scopus 로고
    • The cell-shape protein MreC interacts with extracytoplasmic proteins including cell wall assembly complexes in Caulobacter crescentus
    • Divakaruni AV, Loo RR, Xie Y, Loo JA, Gober JW (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
  • 17
    • 79960194325 scopus 로고    scopus 로고
    • Mutations in the nucleotide binding pocket of MreB can alter cell curvature and polar morphology in Caulobacter
    • Dye NA, Pincus Z, Fisher IC, Shapiro L, Theriot JA (2011). Mutations in the nucleotide binding pocket of MreB can alter cell curvature and polar morphology in Caulobacter. Mol Microbiol 81, 368-394.
    • (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
  • 18
    • 38449121941 scopus 로고    scopus 로고
    • The bacillus subtilis sigma(M) regulon and its contribution to cell envelope stress responses
    • Eiamphungporn W, Helmann JD (2008). The Bacillus subtilis sigma(M) regulon and its contribution to cell envelope stress responses. Mol Microbiol 67, 830-848.
    • (2008) Mol Microbiol , vol.67 , pp. 830-848
    • Eiamphungporn, W.1    Helmann, J.D.2
  • 19
    • 15944399775 scopus 로고    scopus 로고
    • A magnesium-dependent mreB null mutant: Implications for the role of mreB in Bacillus subtilis
    • Formstone A, Errington J (2005). A magnesium-dependent mreB null mutant: implications for the role of mreB in Bacillus subtilis. Mol Microbiol 55, 1646-1657.
    • (2005) Mol Microbiol , vol.55 , pp. 1646-1657
    • Formstone, A.1    Errington, J.2
  • 20
    • 79960075043 scopus 로고    scopus 로고
    • Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B. Subtilis
    • Garner EC, Bernard R, Wang W, Zhuang X, Rudner DZ, Mitchison T (2011). Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B. subtilis. Science 333, 222-225.
    • (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
  • 21
    • 2942588534 scopus 로고    scopus 로고
    • An actin-like gene can determine cell polarity in bacteria
    • Gitai Z, Dye N, Shapiro L (2004). An actin-like gene can determine cell polarity in bacteria. Proc Natl Acad Sci USA 101, 8643-8648.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 8643-8648
    • Gitai, Z.1    Dye, N.2    Shapiro, L.3
  • 22
    • 35848966372 scopus 로고    scopus 로고
    • Cytoskeletal elements in bacteria
    • Graumann PL (2007). Cytoskeletal elements in bacteria. Annu Rev Microbiol 61, 589-618.
    • (2007) Annu Rev Microbiol , vol.61 , pp. 589-618
    • Graumann, P.L.1
  • 23
    • 0031944802 scopus 로고    scopus 로고
    • Control of cell shape and elongation by the rodA gene in Bacillus subtilis
    • Henriques AO, Glaser P, Piggot PJ, Moran CP, Jr (1998). Control of cell shape and elongation by the rodA gene in Bacillus subtilis. Mol Microbiol 28, 235-247.
    • (1998) Mol Microbiol , vol.28 , pp. 235-247
    • Henriques, A.O.1    Glaser, P.2    Piggot, P.J.3    Moran Jr., C.P.4
  • 24
    • 0017876998 scopus 로고
    • Mapping of the mecillinam-resistant, round morphological mutants of Escherichia coli
    • Iwaya M, Jones CW, Khorana J, Strominger JL (1978). Mapping of the mecillinam-resistant, round morphological mutants of Escherichia coli. J Bacteriol 133, 196-202.
    • (1978) J Bacteriol , vol.133 , pp. 196-202
    • Iwaya, M.1    Jones, C.W.2    Khorana, J.3    Strominger, J.L.4
  • 25
    • 0024720167 scopus 로고
    • Identification and characterization of genes controlled by the sporulation regulatory gene spo0H in Bacillus subtilis
    • Jaacks KJ, Healy J, Losick R, Grossman AD (1989). Identification and characterization of genes controlled by the sporulation regulatory gene spo0H in Bacillus subtilis. J Bacteriol 171, 4121-4129.
    • (1989) J Bacteriol , vol.171 , pp. 4121-4129
    • Jaacks, K.J.1    Healy, J.2    Losick, R.3    Grossman, A.D.4
  • 26
    • 80455131023 scopus 로고    scopus 로고
    • The long journey: Actin on the road to pro-and eukaryotic cells
    • Jockusch BM, Graumann PL (2011). The long journey: actin on the road to pro-and eukaryotic cells. Rev Physiol Biochem Pharmacol 161, 67-85.
    • (2011) Rev Physiol Biochem Pharmacol , vol.161 , pp. 67-85
    • Jockusch, B.M.1    Graumann, P.L.2
  • 27
    • 0035937396 scopus 로고    scopus 로고
    • Control of cell shape in bacteria: Helical, actin-like filaments in Bacillus subtilis
    • Jones LJ, Carballido-Lopez R, Errington J (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
  • 28
    • 60649104907 scopus 로고    scopus 로고
    • Regulation of cell wall morphogenesis in Bacillus subtilis by recruitment of PBP1 to the MreB helix
    • Kawai Y, Daniel RA, Errington J (2009). Regulation of cell wall morphogenesis in Bacillus subtilis by recruitment of PBP1 to the MreB helix. Mol Microbiol 71, 1131-1144.
    • (2009) Mol Microbiol , vol.71 , pp. 1131-1144
    • Kawai, Y.1    Daniel, R.A.2    Errington, J.3
  • 29
    • 29144501313 scopus 로고    scopus 로고
    • Cell population heterogeneity during growth of Bacillus subtilis
    • Kearns DB, Losick R (2005). Cell population heterogeneity during growth of Bacillus subtilis. Genes Dev 19, 3083-3094.
    • (2005) Genes Dev , vol.19 , pp. 3083-3094
    • Kearns, D.B.1    Losick, R.2
  • 30
    • 33746655349 scopus 로고    scopus 로고
    • Single molecules of the bacterial actin MreB undergo directed treadmilling motion in Caulobacter crescentus
    • Kim SY, Gitai Z, Kinkhabwala A, Shapiro L, Moerner WE (2006). Single molecules of the bacterial actin MreB undergo directed treadmilling motion in Caulobacter crescentus. Proc Natl Acad Sci USA 103, 10929-10934.
    • (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
  • 31
    • 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 (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
  • 32
    • 0141864658 scopus 로고    scopus 로고
    • Dysfunctional MreB inhibits chromosome segregation in Escherichia coli
    • Kruse T, Moller-Jensen J, Lobner-Olesen A, Gerdes K (2003). Dysfunctional MreB inhibits chromosome segregation in Escherichia coli. EMBO J 22, 5283-5292.
    • (2003) EMBO J , vol.22 , pp. 5283-5292
    • Kruse, T.1    Moller-Jensen, J.2    Lobner-Olesen, A.3    Gerdes, K.4
  • 33
    • 0038782140 scopus 로고    scopus 로고
    • Essential nature of the mreC determinant of Bacillus subtilis
    • Lee JC, Stewart GC (2003). Essential nature of the mreC determinant of Bacillus subtilis. J Bacteriol 185, 4490-4498.
    • (2003) J Bacteriol , vol.185 , pp. 4490-4498
    • Lee, J.C.1    Stewart, G.C.2
  • 34
    • 0015850976 scopus 로고
    • Characterization and genetic analysis of a mutant of Escherichia coli K-12 with rounded morphology
    • Matsuzawa H, Hayakawa K, Sato T, Imahori K (1973). Characterization and genetic analysis of a mutant of Escherichia coli K-12 with rounded morphology. J Bacteriol 115, 436-442.
    • (1973) J Bacteriol , vol.115 , pp. 436-442
    • Matsuzawa, H.1    Hayakawa, K.2    Sato, T.3    Imahori, K.4
  • 35
    • 59949103493 scopus 로고    scopus 로고
    • Assembly properties of the Bacillus subtilis actin, MreB
    • Mayer JA, Amann KJ (2009). Assembly properties of the Bacillus subtilis actin, MreB. Cell Motil Cytoskeleton 66, 109-118.
    • (2009) Cell Motil Cytoskeleton , vol.66 , pp. 109-118
    • Mayer, J.A.1    Amann, K.J.2
  • 36
    • 1142302663 scopus 로고
    • Twisted states of Bacillus subtilis macrofibers reflect structural states of the cell wall
    • Mendelson NH, Favre D, Thwaites JJ (1984). Twisted states of Bacillus subtilis macrofibers reflect structural states of the cell wall. Proc Natl Acad Sci USA 81, 3562-3566.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 3562-3566
    • Mendelson, N.H.1    Favre, D.2    Thwaites, J.J.3
  • 39
    • 41749088673 scopus 로고    scopus 로고
    • Bacitracin sensing in Bacillus subtilis
    • Rietkotter E, Hoyer D, Mascher T (2008). Bacitracin sensing in Bacillus subtilis. Mol Microbiol 68, 768-785.
    • (2008) Mol Microbiol , vol.68 , pp. 768-785
    • Rietkotter, E.1    Hoyer, D.2    Mascher, T.3
  • 40
    • 0017813603 scopus 로고
    • Double mutants of Bacillus subtilis growing as helices
    • Rogers HJ, Thurman PF (1978). Double mutants of Bacillus subtilis growing as helices. J Bacteriol 133, 1508-1509.
    • (1978) J Bacteriol , vol.133 , pp. 1508-1509
    • Rogers, H.J.1    Thurman, P.F.2
  • 41
    • 79960913936 scopus 로고    scopus 로고
    • Direct membrane binding by bacterial actin MreB
    • Salje J, van den Ent F, de Boer P, Lowe J (2011). Direct membrane binding by bacterial actin MreB. Mol Cell 43, 478-487.
    • (2011) Mol Cell , vol.43 , pp. 478-487
    • Salje, J.1    Van Den Ent, F.2    De Boer, P.3    Lowe, J.4
  • 42
    • 58849121358 scopus 로고    scopus 로고
    • Electron cryomicroscopy of E. Coli reveals filament bundles involved in plasmid DNA segregation
    • Salje J, Zuber B, Lowe J (2009). Electron cryomicroscopy of E. coli reveals filament bundles involved in plasmid DNA segregation. Science 323, 509-512.
    • (2009) Science , vol.323 , pp. 509-512
    • Salje, J.1    Zuber, B.2    Lowe, J.3
  • 43
    • 84871055385 scopus 로고    scopus 로고
    • The helical MreB cytoskeleton in E. Coli MC1000/pLE7 is an artifact of the N-terminal YFP tag
    • Swulius MT, Jensen GJ (2012). The helical MreB cytoskeleton in E. coli MC1000/pLE7 is an artifact of the N-terminal YFP tag. J Bacteriol 194, 6382-6386.
    • (2012) J Bacteriol , vol.194 , pp. 6382-6386
    • Swulius, M.T.1    Jensen, G.J.2
  • 44
    • 84861151969 scopus 로고    scopus 로고
    • FtsA forms actin-like protofilaments
    • Szwedziak P, Wang Q, Freund SM, Lowe J (2012). FtsA forms actin-like protofilaments. EMBO J 31, 2249-22460.
    • (2012) EMBO J , vol.31 , pp. 2249-22460
    • Szwedziak, P.1    Wang, Q.2    Freund, S.M.3    Lowe, J.4
  • 45
    • 0017594780 scopus 로고
    • Helical shape and wall synthesis in a bacterium
    • Tilby MJ (1977). Helical shape and wall synthesis in a bacterium. Nature 266, 450-452.
    • (1977) Nature , vol.266 , pp. 450-452
    • Tilby, M.J.1
  • 46
    • 0035817819 scopus 로고    scopus 로고
    • Prokaryotic origin of the actin cytoskeleton
    • van den Ent F, Amos LA, Lowe J (2001). Prokaryotic origin of the actin cytoskeleton. Nature 413, 39-44.
    • (2001) Nature , vol.413 , pp. 39-44
    • Van Den Ent, F.1    Amos, L.A.2    Lowe, J.3
  • 47
    • 12244298896 scopus 로고    scopus 로고
    • F-actin-like filaments formed by plasmid segregation protein ParM
    • van den Ent F, Moller-Jensen J, Amos LA, Gerdes K, Lowe J (2002). F-actin-like filaments formed by plasmid segregation protein ParM. EMBO J 21, 6935-6943.
    • (2002) EMBO J , vol.21 , pp. 6935-6943
    • Van Den Ent, F.1    Moller-Jensen, J.2    Amos, L.A.3    Gerdes, K.4    Lowe, J.5
  • 50
    • 84863229704 scopus 로고    scopus 로고
    • Helical insertion of peptidoglycan produces chiral ordering of the bacterial cell wall
    • Wang S, Furchtgott L, Huang KC, Shaevitz JW (2012). Helical insertion of peptidoglycan produces chiral ordering of the bacterial cell wall. Proc Natl Acad Sci USA 109, E595-E604.
    • (2012) Proc Natl Acad Sci USA , vol.109
    • Wang, S.1    Furchtgott, L.2    Huang, K.C.3    Shaevitz, J.W.4


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