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Volumn 62, Issue 5, 2006, Pages 1340-1356

Dynamic localization and interaction with other Bacillus subtilis actin-like proteins are important for the function of MreB

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; BACTERIAL PROTEIN; MREB PROTEIN; PROTEIN; PROTEIN MBL; PROTEIN MREC; UNCLASSIFIED DRUG;

EID: 33750713640     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2006.05457.x     Document Type: Article
Times cited : (74)

References (43)
  • 1
    • 0028930564 scopus 로고
    • Bacillus subtilis possesses a second determinant with extensive sequence similarity to the Escherichia coli mreB morphogene
    • Abhayawardhane, Y., and Stewart, G.C. (1995) Bacillus subtilis possesses a second determinant with extensive sequence similarity to the Escherichia coli mreB morphogene. J Bacteriol 177: 765-773.
    • (1995) J Bacteriol , vol.177 , pp. 765-773
    • Abhayawardhane, Y.1    Stewart, G.C.2
  • 2
    • 0037237123 scopus 로고    scopus 로고
    • The bacterial cytoskeleton: In vivo dynamics of the actin-like protein Mbl of Bacillus subtilis
    • Carballido-Lopez, R., and Errington, J. (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
  • 3
    • 0037494988 scopus 로고    scopus 로고
    • Control of cell morphogenesis in bacteria: Two distinct ways to make a rodshaped cell
    • Daniel, R.A., and Errington, J. (2003) Control of cell morphogenesis in bacteria: two distinct ways to make a rodshaped cell. Cell 113: 767-776.
    • (2003) Cell , vol.113 , pp. 767-776
    • Daniel, R.A.1    Errington, J.2
  • 4
    • 0242381270 scopus 로고    scopus 로고
    • Actin-like proteins MreB and Mbl from Bacillus subtilis are required for bipolar positioning of replication origins
    • Defeu Soufo, H.J., and Graumann, P.L. (2003) Actin-like proteins MreB and Mbl from Bacillus subtilis are required for bipolar positioning of replication origins. Curr Biol 13: 1916-1920.
    • (2003) Curr Biol , vol.13 , pp. 1916-1920
    • Defeu Soufo, H.J.1    Graumann, P.L.2
  • 5
    • 4444285310 scopus 로고    scopus 로고
    • Dynamic movement of actin-like proteins within bacterial cells
    • Defeu Soufo, H.J., and Graumann, P.L. (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
  • 6
    • 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, H.J., and Graumann, P.L. (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
  • 7
    • 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., Loo, R.R., Xie, Y., Loo, J.A., and Gober, J.W. (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
  • 8
    • 0037195084 scopus 로고    scopus 로고
    • Does RNA polymerase help drive chromosome segregation in bacteria?
    • Dworkin, J., and Losick, R. (2002) Does RNA polymerase help drive chromosome segregation in bacteria? Proc Natl Acad Sci USA 99: 14089-14094.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14089-14094
    • Dworkin, J.1    Losick, R.2
  • 9
    • 29444457542 scopus 로고    scopus 로고
    • Two independent spiral structures control cell shape in Caulobacter
    • Dye, N.A., Pincus, Z., Theriot, J.A., Shapiro, L., and Gitai, Z. (2005) Two independent spiral structures control cell shape in Caulobacter. Proc Natl Acad Sci USA 102: 18608-18613.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 18608-18613
    • Dye, N.A.1    Pincus, Z.2    Theriot, J.A.3    Shapiro, L.4    Gitai, Z.5
  • 10
    • 0035817819 scopus 로고    scopus 로고
    • Prokaryotic origin of the actin cytoskeleton
    • van den Ent, F., Amos, L.A., and 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
  • 11
    • 0035925058 scopus 로고    scopus 로고
    • Improved plasmid vectors for the production of multiple fluorescent protein fusions in Bacillus subtilis
    • Feucht, A., and Lewis, P.J. (2001) Improved plasmid vectors for the production of multiple fluorescent protein fusions in Bacillus subtilis. Gene 264: 289-297.
    • (2001) Gene , vol.264 , pp. 289-297
    • Feucht, A.1    Lewis, P.J.2
  • 12
    • 1542616355 scopus 로고    scopus 로고
    • MreB, the cell shape-determining bacterial actin homologue, co-ordinates cell wall morphogenesis in Caulobacter crescentus
    • Figge, R.M., Divakaruni, A.V., and Gober, J.W. (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
  • 13
    • 15944399775 scopus 로고    scopus 로고
    • A magnesium-dependent mreB null mutant: Implications for the role of mreB. Bacillus subtilis
    • Formstone, A., and Errington, J. (2005) A magnesium-dependent mreB null mutant: implications for the role of mreB. Bacillus subtilis. Mol Microbiol 55: 1646-1657.
    • (2005) Mol Microbiol , vol.55 , pp. 1646-1657
    • Formstone, A.1    Errington, J.2
  • 14
    • 2942588534 scopus 로고    scopus 로고
    • An actin-like gene can determine cell polarity in bacteria
    • Gitai, Z., Dye, N., and 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
  • 15
    • 13544274210 scopus 로고    scopus 로고
    • MreB actin-mediated segregation of a specific region of a bacterial chromosome
    • Gitai, Z., Dye, N.A., Reisenauer, A., Wachi, M., and Shapiro, L. (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
  • 16
    • 8844268461 scopus 로고    scopus 로고
    • Cytoskeletal elements in bacteria
    • Graumann, P.L. (2004) Cytoskeletal elements in bacteria. Curr Opin Microbiol 7: 565-571.
    • (2004) Curr Opin Microbiol , vol.7 , pp. 565-571
    • Graumann, P.L.1
  • 17
    • 0036241055 scopus 로고    scopus 로고
    • Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation
    • Hu, C.D., Chinenov, Y., and Kerppola, T.K. (2002) Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation. Mol Cell 9: 789-798.
    • (2002) Mol Cell , vol.9 , pp. 789-798
    • Hu, C.D.1    Chinenov, Y.2    Kerppola, T.K.3
  • 18
    • 0017876998 scopus 로고
    • Mapping of the mecillinam-resistant, round morphological mutants of Escherichia coli
    • Iwaya, M., Jones, C.W., Khorana, J., and Strominger, J.L. (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
  • 19
    • 0024720167 scopus 로고
    • Identification and characterization of genes controlled by the sporulation regulatory gene spo0H. Bacillus subtilis
    • Jaacks, K.J., Healy, J., Losick, R., and Grossman, A.D. (1989) Identification and characterization of genes controlled by the sporulation regulatory gene spo0H. 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
  • 20
    • 0035937396 scopus 로고    scopus 로고
    • Control of cell shape in bacteria: Helical, actin-like filaments in Bacillus subtilis
    • Jones, L.J., Carballido-Lopez, R., and 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
  • 21
    • 0028944687 scopus 로고
    • The actin fold
    • Kabsch, W., and Holmes, K.C. (1995) The actin fold. FASEB J 9: 167-174.
    • (1995) FASEB J , vol.9 , pp. 167-174
    • Kabsch, W.1    Holmes, K.C.2
  • 22
    • 3042651097 scopus 로고    scopus 로고
    • Visualization of DNA double-strand break repair in live bacteria reveals dynamic recruitment of Bacillus subtilis RecF, RecO and RecN proteins to distinct sites on the nucleoids
    • Kidane, D., Sanchez, H., Alonso, J.C., and Graumann, P.L. (2004) Visualization of DNA double-strand break repair in live bacteria reveals dynamic recruitment of Bacillus subtilis RecF, RecO and RecN proteins to distinct sites on the nucleoids. Mol Microbiol 52: 1627-1639.
    • (2004) Mol Microbiol , vol.52 , pp. 1627-1639
    • Kidane, D.1    Sanchez, H.2    Alonso, J.C.3    Graumann, P.L.4
  • 23
    • 0141864658 scopus 로고    scopus 로고
    • Dysfunctional MreB inhibits chromosome segregation in Escherichia coli
    • Kruse, T., Moller-Jensen, J., Lobner-Olesen, A., and 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
  • 24
    • 12344306119 scopus 로고    scopus 로고
    • The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex
    • Kruse, T., Bork-Jensen, J., and 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
  • 25
    • 29944438325 scopus 로고    scopus 로고
    • Actin homolog MreB and RNA polymerase interact and are both required for chromosome segregation in Escherichia coli
    • Kruse, T., Blagoev, B., Lobner-Olesen, A., Wachi, M., Sasaki, K., Iwai, N., et al. (2006) Actin homolog MreB and RNA polymerase interact and are both required for chromosome segregation in Escherichia coli. Genes Dev 20: 113-124.
    • (2006) Genes Dev , vol.20 , pp. 113-124
    • Kruse, T.1    Blagoev, B.2    Lobner-Olesen, A.3    Wachi, M.4    Sasaki, K.5    Iwai, N.6
  • 26
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: A physically integrated molecular process
    • Lauffenburger, D.A., and Horwitz, A.F. (1996) Cell migration: a physically integrated molecular process. Cell 84: 359-369.
    • (1996) Cell , vol.84 , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 27
    • 23844444807 scopus 로고    scopus 로고
    • Roles for MreC and MreD proteins in helical growth of the cylindrical cell wall in Bacillus subtilis
    • Leaver, M., and Errington, J. (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
  • 28
    • 0038782140 scopus 로고    scopus 로고
    • Essential nature of the mreC determinant of Bacillus subtilis
    • Lee, J.C., and Stewart, G.C. (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
  • 29
    • 0033521857 scopus 로고    scopus 로고
    • GFP vectors for controlled expression and dual labelling of protein fusions in Bacillus subtilis
    • Lewis, P.J., and Marston, A.L. (1999) GFP vectors for controlled expression and dual labelling of protein fusions in Bacillus subtilis. Gene 227: 101-110.
    • (1999) Gene , vol.227 , pp. 101-110
    • Lewis, P.J.1    Marston, A.L.2
  • 30
    • 0141889980 scopus 로고    scopus 로고
    • How cells step out
    • Marx, J. (2003) How cells step out. Science 302: 214-216.
    • (2003) Science , vol.302 , pp. 214-216
    • Marx, J.1
  • 31
    • 0030049170 scopus 로고    scopus 로고
    • Actin-based cell motility and cell locomotion
    • Mitchison, T.J., and Cramer, L.P. (1996) Actin-based cell motility and cell locomotion. Cell 84: 371-379.
    • (1996) Cell , vol.84 , pp. 371-379
    • Mitchison, T.J.1    Cramer, L.P.2
  • 32
    • 0141504153 scopus 로고    scopus 로고
    • Polymer motors: Pushing out the front and pulling up the back
    • Mogilner, A., and Oster, G. (2003) Polymer motors: pushing out the front and pulling up the back. Curr Biol 13: R721-R733.
    • (2003) Curr Biol , vol.13
    • Mogilner, A.1    Oster, G.2
  • 33
    • 0037124325 scopus 로고    scopus 로고
    • Prokaryotic DNA segregation by an actin-like filament
    • Moller-Jensen, J., Jensen, R.B., Lowe, J., and Gerdes, K. (2002) Prokaryotic DNA segregation by an actin-like filament. EMBO J 21: 3119-3127.
    • (2002) EMBO J , vol.21 , pp. 3119-3127
    • Moller-Jensen, J.1    Jensen, R.B.2    Lowe, J.3    Gerdes, K.4
  • 34
    • 0346980557 scopus 로고    scopus 로고
    • Bacterial mitosis. ParM of plasmid R1 moves plasmid DNA by an actin-like insertional polymerization mechanism
    • Moller-Jensen, J., Borch, J., Dam, M., Jensen, R.B., Roepstorff, P., and Gerdes, K. (2003) Bacterial mitosis. ParM of plasmid R1 moves plasmid DNA by an actin-like insertional polymerization mechanism. Mol Cell 12: 1477-1487.
    • (2003) Mol Cell , vol.12 , pp. 1477-1487
    • Moller-Jensen, J.1    Borch, J.2    Dam, M.3    Jensen, R.B.4    Roepstorff, P.5    Gerdes, K.6
  • 35
    • 0036906627 scopus 로고    scopus 로고
    • Mutant actins demonstrate a role for unpolymerized actin in control of transcription by serum response factor
    • Posern, G., Sotiropoulos, A., and Treisman, R. (2002) Mutant actins demonstrate a role for unpolymerized actin in control of transcription by serum response factor. Mol Biol Cell 13: 4167-4178.
    • (2002) Mol Biol Cell , vol.13 , pp. 4167-4178
    • Posern, G.1    Sotiropoulos, A.2    Treisman, R.3
  • 36
    • 1842424983 scopus 로고    scopus 로고
    • An improved cyan fluorescent protein variant useful for FRET
    • Rizzo, M.A., Springer, G.H., Granada, B., and Piston, D.W. (2004) An improved cyan fluorescent protein variant useful for FRET. Nat Biotechnol 22: 445-449.
    • (2004) Nat Biotechnol , vol.22 , pp. 445-449
    • Rizzo, M.A.1    Springer, G.H.2    Granada, B.3    Piston, D.W.4
  • 37
    • 1242320297 scopus 로고    scopus 로고
    • Several distinct localization patterns for penicillin-binding proteins in Bacillus subtilis
    • Scheffers, D.J., Jones, L.J., and Errington, J. (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
  • 38
    • 0037699937 scopus 로고    scopus 로고
    • Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles
    • Shih, Y.-L., Le, T., and Rothfield, L. (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
  • 39
    • 11144257131 scopus 로고    scopus 로고
    • Localization of MreB in Rhodobacter sphaeroides under conditions causing changes in cell shape and membrane structure
    • Slovak, P.M., Wadhams, G.H., and Armitage, J.P. (2005) Localization of MreB in Rhodobacter sphaeroides under conditions causing changes in cell shape and membrane structure. J Bacteriol 187: 54-64.
    • (2005) J Bacteriol , vol.187 , pp. 54-64
    • Slovak, P.M.1    Wadhams, G.H.2    Armitage, J.P.3
  • 40
    • 33746639594 scopus 로고    scopus 로고
    • Imaging peptidoglycan biosynthesis in Bacillus subtilis with fluorescent antibiotics
    • Tiyanont, K., Doan, T., Lazarus, M.B., Fang, X., Rudner, D.Z., and Walker, S. (2006) Imaging peptidoglycan biosynthesis in Bacillus subtilis with fluorescent antibiotics. Proc Natl Acad Sci USA 103: 11033-11038.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 11033-11038
    • Tiyanont, K.1    Doan, T.2    Lazarus, M.B.3    Fang, X.4    Rudner, D.Z.5    Walker, S.6
  • 41
    • 0141838877 scopus 로고    scopus 로고
    • Biomimetic systems for studying actin-based motility
    • Upadhyaya, A., and van Oudenaarden, A. (2003) Biomimetic systems for studying actin-based motility. Curr Biol 13: R734-R744.
    • (2003) Curr Biol , vol.13
    • Upadhyaya, A.1    Van Oudenaarden, A.2
  • 42
    • 8744302067 scopus 로고    scopus 로고
    • Visualization of differential gene expression by improved cyan fluorescent protein and yellow fluorescent protein production in Bacillus subtilis
    • Veening, J.-W., Smits, W.K., Hamoen, L.W., Jongbloed, J.D.H., and Kuipers, O.P. (2004) Visualization of differential gene expression by improved cyan fluorescent protein and yellow fluorescent protein production in Bacillus subtilis. Appl Environ Microbiol 70: 6809-6815.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 6809-6815
    • Veening, J.-W.1    Smits, W.K.2    Hamoen, L.W.3    Jongbloed, J.D.H.4    Kuipers, O.P.5
  • 43
    • 0042132009 scopus 로고    scopus 로고
    • A prokaryotic condensin/cohesin-like complex can actively compact chromosomes from a single position on the nucleoid and binds to DNA as a ring-like structure
    • Volkov, A., Mascarenhas, J., Andrei-Selmer, C., Ulrich, H.D., and Graumann, P.L. (2003) A prokaryotic condensin/cohesin-like complex can actively compact chromosomes from a single position on the nucleoid and binds to DNA as a ring-like structure. Mol Cell Biol 23: 5638-5650.
    • (2003) Mol Cell Biol , vol.23 , pp. 5638-5650
    • Volkov, A.1    Mascarenhas, J.2    Andrei-Selmer, C.3    Ulrich, H.D.4    Graumann, P.L.5


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