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Volumn 186, Issue 17, 2004, Pages 5775-5781

Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins

Author keywords

[No Author keywords available]

Indexed keywords

FTSZ PROTEIN; GREEN FLUORESCENT PROTEIN; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; POLYMER; PROTEIN EZRA; PROTEIN MINCD; PROTEIN ZAPA; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 4344652693     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.186.17.5775-5781.2004     Document Type: Article
Times cited : (258)

References (31)
  • 1
    • 0037133943 scopus 로고    scopus 로고
    • Asymmetric cell division in B. subtilis involves a spiral-like intermediate of the cytokinetic protein FtsZ
    • Ben-Yehuda, S., and R. Losick. 2002. Asymmetric cell division in B. subtilis involves a spiral-like intermediate of the cytokinetic protein FtsZ. Cell 109: 257-266.
    • (2002) Cell , vol.109 , pp. 257-266
    • Ben-Yehuda, S.1    Losick, R.2
  • 6
    • 0030068218 scopus 로고    scopus 로고
    • Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers
    • Erickson, H. P., D. W. Taylor, K. A. Taylor, and D. Bramhill. 1996. Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers. Proc. Natl. Acad. Sci. USA 93:519-523.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 519-523
    • Erickson, H.P.1    Taylor, D.W.2    Taylor, K.A.3    Bramhill, D.4
  • 8
    • 0035051322 scopus 로고    scopus 로고
    • Cytological and biochemical characterization of the FtsA cell division protein of Bacillus subtilis
    • Feucht, A., I. Lucet, M. D. Yudkin, and J. Errington. 2001. Cytological and biochemical characterization of the FtsA cell division protein of Bacillus subtilis. Mol. Microbiol. 40:115-125.
    • (2001) Mol. Microbiol. , vol.40 , pp. 115-125
    • Feucht, A.1    Lucet, I.2    Yudkin, M.D.3    Errington, J.4
  • 9
    • 0242584670 scopus 로고    scopus 로고
    • Essential cell division protein FtsZ assembles into one monomer-thick ribbons under conditions resembling the crowded intracellular environment
    • Gonzalez, J. M., M. Jimenez, M. Velez, J. Mingorance, J. M. Andreu, M. Vicente, and G. Rivas. 2003. Essential cell division protein FtsZ assembles into one monomer-thick ribbons under conditions resembling the crowded intracellular environment. J. Biol. Chem. 278:37664-37671.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37664-37671
    • Gonzalez, J.M.1    Jimenez, M.2    Velez, M.3    Mingorance, J.4    Andreu, J.M.5    Vicente, M.6    Rivas, G.7
  • 10
    • 0036791675 scopus 로고    scopus 로고
    • A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ
    • Gueiros-Filho, F. J., and R. Losick. 2002. A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ. Genes Dev. 16:2544-2556.
    • (2002) Genes Dev. , vol.16 , pp. 2544-2556
    • Gueiros-Filho, F.J.1    Losick, R.2
  • 11
    • 0035010154 scopus 로고    scopus 로고
    • Bacterial cell division: Regulating Z-ring formation
    • Harry, E. J. 2001. Bacterial cell division: regulating Z-ring formation. Mol. Microbiol. 40:795-803.
    • (2001) Mol. Microbiol. , vol.40 , pp. 795-803
    • Harry, E.J.1
  • 12
    • 0035216867 scopus 로고    scopus 로고
    • Homogeneous expression of the P(BAD) promoter in Escherichia coli by constitutive expression of the low-affinity high-capacity AraE transporter
    • Khlebnikov, A., K. A. Datsenko, T. Skaug, B. L. Wanner, and J. D. Keasling. 2001. Homogeneous expression of the P(BAD) promoter in Escherichia coli by constitutive expression of the low-affinity high-capacity AraE transporter. Microbiology 147:3241-3247.
    • (2001) Microbiology , vol.147 , pp. 3241-3247
    • Khlebnikov, A.1    Datsenko, K.A.2    Skaug, T.3    Wanner, B.L.4    Keasling, J.D.5
  • 13
    • 0031765193 scopus 로고    scopus 로고
    • Effect of minCD on FtsZ ring position and polar septation in Bacillus subtilis
    • Levin, P. A., J. J. Shim, and A. D. Grossman. 1998. Effect of minCD on FtsZ ring position and polar septation in Bacillus subtilis. J. Bacteriol. 180:6048-6051.
    • (1998) J. Bacteriol. , vol.180 , pp. 6048-6051
    • Levin, P.A.1    Shim, J.J.2    Grossman, A.D.3
  • 14
    • 0033578438 scopus 로고    scopus 로고
    • Identification and characterization of a negative regulator of FtsZ ring formation in Bacillus subtilis
    • Levin, P. A., I. G. Kurtser, and A. D. Grossman. 1999. Identification and characterization of a negative regulator of FtsZ ring formation in Bacillus subtilis. Proc. Natl. Acad. Sci. USA 96:9642-9647.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9642-9647
    • Levin, P.A.1    Kurtser, I.G.2    Grossman, A.D.3
  • 15
    • 2642593025 scopus 로고    scopus 로고
    • Crystal structure of the bacterial cell-division protein FtsZ
    • Lowe, J., and L. A. Amos. 1998. Crystal structure of the bacterial cell-division protein FtsZ. Nature 391:203-206.
    • (1998) Nature , vol.391 , pp. 203-206
    • Lowe, J.1    Amos, L.A.2
  • 16
    • 0031968795 scopus 로고    scopus 로고
    • FtsZ from Escherichia coli, Azotobacter vinelandii, and Thermotoga maritima-quantitation, GTP hydrolysis, and assembly
    • Lu, C., J. Stricker, and H. P. Erickson. 1998. FtsZ from Escherichia coli, Azotobacter vinelandii, and Thermotoga maritima-quantitation, GTP hydrolysis, and assembly. Cell Motil. Cytoskelet. 40:71-86.
    • (1998) Cell Motil. Cytoskelet. , vol.40 , pp. 71-86
    • Lu, C.1    Stricker, J.2    Erickson, H.P.3
  • 17
    • 0018972825 scopus 로고
    • Organization of genes in the ftsA-envA region of the Escherichia coli genetic map and identification of a new fts locus (ftsZ)
    • Lutkenhaus, J. F., H. Wolf-Watz, and W. D. Donachie. 1980. Organization of genes in the ftsA-envA region of the Escherichia coli genetic map and identification of a new fts locus (ftsZ). J. Bacteriol. 142:615-620.
    • (1980) J. Bacteriol. , vol.142 , pp. 615-620
    • Lutkenhaus, J.F.1    Wolf-Watz, H.2    Donachie, W.D.3
  • 18
    • 0033793087 scopus 로고    scopus 로고
    • The polarity and dynamics of microtubule assembly in the budding yeast Saccharomyces cerevisiae
    • Maddox, P. S., K. S. Bloom, and E. D. Salmon. 2000. The polarity and dynamics of microtubule assembly in the budding yeast Saccharomyces cerevisiae. Nat. Cell Biol. 2:36-41.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 36-41
    • Maddox, P.S.1    Bloom, K.S.2    Salmon, E.D.3
  • 19
    • 0035196036 scopus 로고    scopus 로고
    • Spatial regulation of cytokinesis in bacteria
    • Margolin, W. 2001. Spatial regulation of cytokinesis in bacteria. Curr. Opin. Microbiol. 4:647-652.
    • (2001) Curr. Opin. Microbiol. , vol.4 , pp. 647-652
    • Margolin, W.1
  • 20
    • 0027500054 scopus 로고
    • Escherichia coli cell division protein FtsZ is a guanine nucleotide binding protein
    • Mukherjee, A., K. Dai, and J. Lutkenhaus. 1993. Escherichia coli cell division protein FtsZ is a guanine nucleotide binding protein. Proc. Natl. Acad. Sci. USA 90:1053-1057.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1053-1057
    • Mukherjee, A.1    Dai, K.2    Lutkenhaus, J.3
  • 21
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the alpha beta tubulin dimer by electron crystallography
    • Nogales, E., S. G. Wolf, and K. H. Downing. 1998. Structure of the alpha beta tubulin dimer by electron crystallography. Nature 391:199-203.
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 22
    • 0026607545 scopus 로고
    • Kinetics of protein-protein association explained by Brownian dynamics computer simulation
    • Northrup, S. H., and H. P. Erickson. 1992. Kinetics of protein-protein association explained by Brownian dynamics computer simulation. Proc. Natl. Acad. Sci. USA 89:3338-3342.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3338-3342
    • Northrup, S.H.1    Erickson, H.P.2
  • 23
    • 0242693139 scopus 로고    scopus 로고
    • Assembly dynamics of the bacterial cell division protein FtsZ: Poised at the edge of stability
    • Romberg, L., and P. A. Levin. 2003. Assembly dynamics of the bacterial cell division protein FtsZ: poised at the edge of stability. Annu. Rev. Microbiol. 57:125-154.
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 125-154
    • Romberg, L.1    Levin, P.A.2
  • 24
    • 0035853825 scopus 로고    scopus 로고
    • Polymerization of Ftsz, a bacterial homolog of tubulin. is assembly cooperative?
    • Romberg, L., M. Simon, and H. P. Erickson. 2001. Polymerization of Ftsz, a bacterial homolog of tubulin. is assembly cooperative? J. Biol. Chem. 276: 11743-11753.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11743-11753
    • Romberg, L.1    Simon, M.2    Erickson, H.P.3
  • 25
    • 0038191051 scopus 로고    scopus 로고
    • Concentration and assembly of the division ring proteins FtsZ, FtsA, and ZipA during the Escherichia coli cell cycle
    • Rueda, S., M. Vicente, and J. Mingorance. 2003. Concentration and assembly of the division ring proteins FtsZ, FtsA, and ZipA during the Escherichia coli cell cycle. J. Bacteriol. 185:3344-3351.
    • (2003) J. Bacteriol. , vol.185 , pp. 3344-3351
    • Rueda, S.1    Vicente, M.2    Mingorance, J.3
  • 26
    • 0008753357 scopus 로고
    • Fluorescence studies of tubulin and microtubule dynamics in living cells
    • D. L. Taylor, A. S. Waggoner, R. F. Murphy, F. Lanni, and R. R. Birge (ed.). Alan R. Liss, Inc., New York
    • Salmon, E. D., and P. Wadsworth. 1986. Fluorescence studies of tubulin and microtubule dynamics in living cells, p. 377-403. In D. L. Taylor, A. S. Waggoner, R. F. Murphy, F. Lanni, and R. R. Birge (ed.), Applications of fluorescence in the biomedical sciences. Alan R. Liss, Inc., New York.
    • (1986) Applications of Fluorescence in the Biomedical Sciences , pp. 377-403
    • Salmon, E.D.1    Wadsworth, P.2
  • 28
    • 0043062671 scopus 로고    scopus 로고
    • In vivo characterization of Escherichia coli ftsZ mutants: Effects on Z-ring structure and function
    • Stricker, J., and H. P. Erickson. 2003. In vivo characterization of Escherichia coli ftsZ mutants: effects on Z-ring structure and function. J. Bacteriol. 185:4796-4805.
    • (2003) J. Bacteriol. , vol.185 , pp. 4796-4805
    • Stricker, J.1    Erickson, H.P.2
  • 29
    • 0037022642 scopus 로고    scopus 로고
    • Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching
    • Stricker, J., P. Maddox, E. D. Salmon, and H. P. Erickson. 2002. Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching. Proc. Natl. Acad. Sci. USA 99:3171-3175.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3171-3175
    • Stricker, J.1    Maddox, P.2    Salmon, E.D.3    Erickson, H.P.4
  • 30
    • 0035145619 scopus 로고    scopus 로고
    • Influence of the nucleoid on placement of FtsZ and MinE rings in Escherichia coli
    • Sun, Q., and W. Margolin. 2001. Influence of the nucleoid on placement of FtsZ and MinE rings in Escherichia coli. J. Bacteriol. 183:1413-1422.
    • (2001) J. Bacteriol. , vol.183 , pp. 1413-1422
    • Sun, Q.1    Margolin, W.2
  • 31
    • 0027257145 scopus 로고
    • The FtsZ protein of Bacillus subtilis is localized at the division site and has GTPase activity that is dependent upon FtsZ concentration
    • Wang, X., and J. Lutkenhaus. 1993. The FtsZ protein of Bacillus subtilis is localized at the division site and has GTPase activity that is dependent upon FtsZ concentration. Mol. Microbiol. 9:435-442.
    • (1993) Mol. Microbiol. , vol.9 , pp. 435-442
    • Wang, X.1    Lutkenhaus, J.2


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