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Volumn 50, Issue 21, 2011, Pages 4675-4684

Conformational changes of FtsZ reported by tryptophan mutants

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONAL CHANGE; DOMAIN BOUNDARY; DOUBLE MUTANTS; E. COLI; N-TERMINALS; PROTOFILAMENTS; SIDE-CHAINS; SUB-DOMAINS; SUBDOMAIN; TRP-FLUORESCENCE; TRYPTOPHAN MUTANT; VAN DER WAALS CONTACTS;

EID: 79958167357     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200106d     Document Type: Article
Times cited : (42)

References (39)
  • 1
    • 78650078263 scopus 로고    scopus 로고
    • FtsZ in bacterial cytokinesis: Cytoskeleton and force generator all in one
    • Erickson, H. P., Anderson, D. E., and Osawa, M. (2010) FtsZ in Bacterial Cytokinesis: Cytoskeleton and Force Generator All in One. Microbiol. Mol. Biol. Rev. 74, 504-528.
    • (2010) Microbiol Mol. Biol. Rev. , vol.74 , pp. 504-528
    • Erickson, H.P.1    Anderson, D.E.2    Osawa, M.3
  • 3
    • 0037495314 scopus 로고    scopus 로고
    • 2+-induced FtsZ sheets
    • DOI 10.1093/emboj/18.9.2364
    • Löwe, J., and Amos, L. A. (1999) Tubulin-like protofilaments in Ca2+-induced FtsZ sheets. EMBO J. 18, 2364-2371. (Pubitemid 29213270)
    • (1999) EMBO Journal , vol.18 , Issue.9 , pp. 2364-2371
    • Lowe, J.1    Amos, L.A.2
  • 4
    • 0035853825 scopus 로고    scopus 로고
    • Polymerization of FtsZ, a bacterial homolog of tubulin. Is assembly cooperative?
    • Romberg, L., Simon, M., and Erickson, H. P. (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
  • 5
    • 11244348910 scopus 로고    scopus 로고
    • A rapid fluorescence assay for FtsZ assembly indicates cooperative assembly with a dimer nucleus
    • DOI 10.1529/biophysj.104.044149
    • Chen, Y., Bjornson, K., Redick, S. D., and Erickson, H. P. (2005) A rapid fluorescence assay for FtsZ assembly indicates cooperative assembly with a dimer nucleus. Biophys. J. 88, 505-514. (Pubitemid 40070696)
    • (2005) Biophysical Journal , vol.88 , Issue.1 , pp. 505-514
    • Chen, Y.1    Bjornson, K.2    Redick, S.D.3    Erickson, H.P.4
  • 6
    • 41449086675 scopus 로고    scopus 로고
    • Energetics and geometry of FtsZ polymers: Nucleated self-assembly of single protofilaments
    • Huecas, S., Llorca, O., Boskovic, J., Martin-Benito, J., Valpuesta, J. M., and Andreu, J. M. (2008) Energetics and geometry of FtsZ polymers: Nucleated self-assembly of single protofilaments. Biophys. J. 94, 1796-1806.
    • (2008) Biophys. J. , vol.94 , pp. 1796-1806
    • Huecas, S.1    Llorca, O.2    Boskovic, J.3    Martin-Benito, J.4    Valpuesta, J.M.5    Andreu, J.M.6
  • 7
    • 20444457941 scopus 로고    scopus 로고
    • Rapid in vitro assembly dynamics and subunit turnover of FtsZ demonstrated by fluorescence resonance energy transfer
    • DOI 10.1074/jbc.M500895200
    • Chen, Y., and Erickson, H. P. (2005) Rapid in vitro assembly dynamics and subunit turnover of FtsZ demonstrated by fluorescence resonance energy transfer. J. Biol. Chem. 280, 22549-22554. (Pubitemid 40827913)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.23 , pp. 22549-22554
    • Chen, Y.1    Erickson, H.P.2
  • 8
    • 0024511257 scopus 로고
    • Co-operativity in protein-protein association. The structure and stability of the actin filament
    • DOI 10.1016/0022-2836(89)90494-4
    • Erickson, H. P. (1989) Cooperativity in protein-protein association: The structure and stability of the actin filament. J. Mol. Biol. 206, 465-474. (Pubitemid 19104986)
    • (1989) Journal of Molecular Biology , vol.206 , Issue.3 , pp. 465-474
    • Erickson, H.P.1
  • 10
    • 39249085850 scopus 로고    scopus 로고
    • MinC spatially controls bacterial cytokinesis by antagonizing the scaffolding function of FtsZ
    • Dajkovic, A., Lan, G., Sun, S. X., Wirtz, D., and Lutkenhaus, J. (2008) MinC spatially controls bacterial cytokinesis by antagonizing the scaffolding function of FtsZ. Curr. Biol. 18, 235-244.
    • (2008) Curr. Biol , vol.18 , pp. 235-244
    • Dajkovic, A.1    Lan, G.2    Sun, S.X.3    Wirtz, D.4    Lutkenhaus, J.5
  • 11
    • 56049110001 scopus 로고    scopus 로고
    • Polymerization and bundling kinetics of FtsZ filaments
    • Lan, G., Dajkovic, A., Wirtz, D., and Sun, S. X. (2008) Polymerization and bundling kinetics of FtsZ filaments. Biophys. J. 95, 4045-4056.
    • (2008) Biophys. J. , vol.95 , pp. 4045-4056
    • Lan, G.1    Dajkovic, A.2    Wirtz, D.3    Sun, S.X.4
  • 12
    • 51649125772 scopus 로고    scopus 로고
    • Allosteric models for cooperative polymerization of linear polymers
    • Miraldi, E. R., Thomas, P. J., and Romberg, L. (2008) Allosteric models for cooperative polymerization of linear polymers. Biophys. J. 95, 2470-2486.
    • (2008) Biophys. J , vol.95 , pp. 2470-2486
    • Miraldi, E.R.1    Thomas, P.J.2    Romberg, L.3
  • 13
    • 13444274140 scopus 로고    scopus 로고
    • Structural insights into FtsZ protofilament formation
    • Oliva, M. A., Cordell, S. C., and Lowe, J. (2004) Structural insights into FtsZ protofilament formation. Nat. Struct. Mol. Biol. 11, 1243-1250.
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 1243-1250
    • Oliva, M.A.1    Cordell, S.C.2    Lowe, J.3
  • 14
    • 29244436874 scopus 로고    scopus 로고
    • Probing the domain structure of FtsZ by random truncation and insertion of GFP
    • DOI 10.1099/mic.0.28219-0
    • Osawa, M., and Erickson, H. P. (2005) Probing the domain structure of FtsZ by random truncation and insertion of GFP. Microbiology (Reading, England) 151, 4033-4043. (Pubitemid 41829983)
    • (2005) Microbiology , vol.151 , Issue.12 , pp. 4033-4043
    • Osawa, M.1    Erickson, H.P.2
  • 15
    • 35148840132 scopus 로고    scopus 로고
    • Structural Insights into the Conformational Variability of FtsZ
    • DOI 10.1016/j.jmb.2007.08.056, PII S0022283607011382
    • Oliva, M. A., Trambaiolo, D., and Lowe, J. (2007) Structural insights into the conformational variability of FtsZ. J. Mol. Biol. 373, 1229-1242. (Pubitemid 47539485)
    • (2007) Journal of Molecular Biology , vol.373 , Issue.5 , pp. 1229-1242
    • Oliva, M.A.1    Trambaiolo, D.2    Lowe, J.3
  • 16
    • 1642401199 scopus 로고    scopus 로고
    • Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain
    • DOI 10.1038/nature02393
    • Ravelli, R. B., Gigant, B., Curmi, P. A., Jourdain, I., Lachkar, S., Sobel, A., and Knossow, M. (2004) Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain. Nature 428, 198-202. (Pubitemid 38374318)
    • (2004) Nature , vol.428 , Issue.6979 , pp. 198-202
    • Ravelli, R.B.G.1    Gigant, B.2    Curmi, P.A.3    Jourdain, I.4    Lachkar, S.5    Sobel, A.6    Knossow, M.7
  • 17
    • 77954588474 scopus 로고    scopus 로고
    • Mapping flexibility and the assembly switch of cell division protein FtsZ by computational and mutational approaches
    • Martin-Galiano, A. J., Buey, R. M., Cabezas, M., and Andreu, J. M. (2010) Mapping flexibility and the assembly switch of cell division protein FtsZ by computational and mutational approaches. J. Biol. Chem. 285, 22554-22565.
    • (2010) J. Biol. Chem. , vol.285 , pp. 22554-22565
    • Martin-Galiano, A.J.1    Buey, R.M.2    Cabezas, M.3    Andreu, J.M.4
  • 18
    • 0031968795 scopus 로고    scopus 로고
    • FtsZ from Escherichia coli, Azotobacter vinelandii, and Thermotoga maritima - Quantitation, GTP hydrolysis, and assembly
    • DOI 10.1002/(SICI)1097-0169(1998)40:1<71::AID-CM7>3.0.CO;2-I
    • Lu, C., Stricker, J., and Erickson, H. P. (1998) FtsZ from Escherichia coli, Azotobacter vinelandii, and Thermotoga maritima - quantitation,GTP hydrolysis, and assembly. Cell Motil. Cytoskel. 40, 71-86. (Pubitemid 28225543)
    • (1998) Cell Motility and the Cytoskeleton , vol.40 , Issue.1 , pp. 71-86
    • Lu, C.1    Stricker, J.2    Erickson, H.P.3
  • 19
    • 30544450009 scopus 로고    scopus 로고
    • A continuous, regenerative coupled GTPase assay for dynamin-related proteins
    • DOI 10.1016/S0076-6879(05)04053-X, PII S007668790504053X, 53, GTPases Regulating Membrane Dynamics
    • Ingerman, E., and Nunnari, J. (2005) A continuous, regenerative coupled GTPase assay for dynamin-related proteins. Methods Enzymol. 404, 611-619. (Pubitemid 43082019)
    • (2006) Methods in Enzymology , vol.404 , pp. 611-619
    • Ingerman, E.1    Nunnari, J.2
  • 20
    • 67650069580 scopus 로고    scopus 로고
    • Fluorescence quenching by photoinduced electron transfer: A reporter for conformational dynamics of macromolecules
    • Doose, S., Neuweiler, H., and Sauer, M. (2009) Fluorescence quenching by photoinduced electron transfer: A reporter for conformational dynamics of macromolecules. ChemPhysChem 10, 1389-1398.
    • (2009) ChemPhysChem , vol.10 , pp. 1389-1398
    • Doose, S.1    Neuweiler, H.2    Sauer, M.3
  • 21
    • 78049441725 scopus 로고    scopus 로고
    • Distance mapping in proteins using fluorescence spectroscopy: The tryptophan- induced quenching (TrIQ) method
    • Mansoor, S. E., Dewitt, M. A., and Farrens, D. L. (2010) Distance mapping in proteins using fluorescence spectroscopy: The tryptophan- induced quenching (TrIQ) method. Biochemistry 49, 9722-9731.
    • (2010) Biochemistry , vol.49 , pp. 9722-9731
    • Mansoor, S.E.1    Dewitt, M.A.2    Farrens, D.L.3
  • 23
    • 0032518656 scopus 로고    scopus 로고
    • Dynamic assembly of FtsZ regulated by GTP hydrolysis
    • DOI 10.1093/emboj/17.2.462
    • Mukherjee, A., and Lutkenhaus, J. (1998) Dynamic assembly of FtsZ regulated by GTP hydrolysis. EMBO J. 17, 462-469. (Pubitemid 28045487)
    • (1998) EMBO Journal , vol.17 , Issue.2 , pp. 462-469
    • Mukherjee, A.1    Lutkenhaus, J.2
  • 24
    • 0242584670 scopus 로고    scopus 로고
    • Essential cell division protein FtsZ assembles into one monomer-thick ribbons under conditions resembling the crowded intracellular environment
    • DOI 10.1074/jbc.M305230200
    • Gonzalez, J. M., Jimenez, M., Velez, M., Mingorance, J., Andreu, J. M., Vicente, M., and Rivas, G. (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. (Pubitemid 37175290)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.39 , 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
  • 25
    • 67650508425 scopus 로고    scopus 로고
    • FtsZ filament dynamics at steady state: Subunit exchange with and without nucleotide hydrolysis
    • Chen, Y., and Erickson, H. P. (2009) FtsZ filament dynamics at steady state: Subunit exchange with and without nucleotide hydrolysis. Biochemistry 48, 6664-6673.
    • (2009) Biochemistry , vol.48 , pp. 6664-6673
    • Chen, Y.1    Erickson, H.P.2
  • 27
    • 0035907236 scopus 로고    scopus 로고
    • Activation of Cell Division Protein FtsZ. Control of switch loop T3 conformation by the nucleotide gammaphosphate
    • Diaz, J. F., Kralicek, A., Mingorance, J., Palacios, J. M., Vicente, M., and Andreu, J. M. (2001) Activation of Cell Division Protein FtsZ. Control of switch loop T3 conformation by the nucleotide gammaphosphate. J. Biol. Chem. 276, 17307-17315.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17307-17315
    • Diaz, J.F.1    Kralicek, A.2    Mingorance, J.3    Palacios, J.M.4    Vicente, M.5    Andreu, J.M.6
  • 28
    • 0017288499 scopus 로고
    • Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies
    • Eftink, M. R., and Ghiron, C. A. (1976) Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies. Biochemistry 15, 672-680.
    • (1976) Biochemistry , vol.15 , pp. 672-680
    • Eftink, M.R.1    Ghiron, C.A.2
  • 29
    • 0033986992 scopus 로고    scopus 로고
    • Straight and curved conformations of FtsZ are regulated by GTP hydrolysis
    • Lu, C., Reedy, M., and Erickson, H. P. (2000) Straight and curved conformations of FtsZ are regulated by GTP hydrolysis. J. Bacteriol. 182, 164-170. (Pubitemid 30004571)
    • (2000) Journal of Bacteriology , vol.182 , Issue.1 , pp. 164-170
    • Lu, C.1    Reedy, M.2    Erickson, H.P.3
  • 30
    • 0030266954 scopus 로고    scopus 로고
    • Protofilaments and rings, two conformations of the tubulin family conserved from bacterial FtsZ to alpha/beta and gamma tubulin
    • Erickson, H. P., and Stoffler, D. (1996) Protofilaments and rings, two conformations of the tubulin family conserved from bacterial FtsZ to alpha/beta and gamma tubulin. J. Cell Biol. 135, 5-8.
    • (1996) J. Cell Biol , vol.135 , pp. 5-8
    • Erickson, H.P.1    Stoffler, D.2
  • 31
    • 0027177102 scopus 로고
    • Interaction of barnase with its polypeptide inhibitor barstar studied by protein engineering
    • DOI 10.1021/bi00070a025
    • Schreiber, G., and Fersht, A. R. (1993) Interaction of barnase with its polypeptide inhibitor barstar studied by protein engineering. Biochemistry 32, 5145-5150. (Pubitemid 23162083)
    • (1993) Biochemistry , vol.32 , Issue.19 , pp. 5145-5150
    • Schreiber, G.1    Fersht, A.R.2
  • 32
    • 0032516433 scopus 로고    scopus 로고
    • Toward understanding tryptophan fluorescence in proteins
    • DOI 10.1021/bi980274n
    • Chen, Y., and Barkley, M. D. (1998) Toward understanding tryptophan fluorescence in proteins. Biochemistry 37, 9976-9982. (Pubitemid 28366351)
    • (1998) Biochemistry , vol.37 , Issue.28 , pp. 9976-9982
    • Chen, Y.1    Barkley, M.D.2
  • 33
    • 34547567840 scopus 로고    scopus 로고
    • Domain folding and flexibility of Escherichia coli FtsZ determined by tryptophan site-directed mutagenesis
    • DOI 10.1110/ps.072807607
    • Diaz-Espinoza, R., Garces, A. P., Arbildua, J. J., Montecinos, F., Brunet, J. E., Lagos, R., and Monasterio, O. (2007) Domain folding and flexibility of Escherichia coli FtsZ determined by tryptophan sitedirected mutagenesis. Protein Sci. 16, 1543-1556. (Pubitemid 47195682)
    • (2007) Protein Science , vol.16 , Issue.8 , pp. 1543-1556
    • Diaz-Espinoza, R.1    Garces, A.P.2    Arbildua, J.J.3    Montecinos, F.4    Brunet, J.E.5    Lagos, R.6    Monasterio, O.7
  • 34
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the αβ tubulin dimer by electron crystallography
    • DOI 10.1038/34465
    • Nogales, E., Wolf, S. G., and Downing, K. H. (1998) Structure of the Rß tubulin dimer by electron crystallography. Nature 391, 199-203. (Pubitemid 28092482)
    • (1998) Nature , vol.391 , Issue.6663 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 36
    • 19544384914 scopus 로고    scopus 로고
    • Insights into microtubule nucleation from the crystal structure of human γ-tubulin
    • DOI 10.1038/nature03586
    • Aldaz, H., Rice, L. M., Stearns, T., and Agard, D. A. (2005) Insights into microtubule nucleation from the crystal structure of human gamma-tubulin. Nature 435, 523-527. (Pubitemid 40734251)
    • (2005) Nature , vol.435 , Issue.7041 , pp. 523-527
    • Aldaz, H.1    Rice, L.M.2    Stearns, T.3    Agard, D.A.4
  • 37
    • 44449170797 scopus 로고    scopus 로고
    • The lattice as allosteric effector: Structural studies of αβ- and γ-tubulin clarify the role of GTP in microtubule assembly
    • DOI 10.1073/pnas.0801155105
    • Rice, L. M., Montabana, E. A., and Agard, D. A. (2008) The lattice as allosteric effector: Structural studies of alphabeta- and gammatubulin clarify the role of GTP in microtubule assembly. Proc. Natl. Acad. Sci. U.S.A. 105, 5378-5383. (Pubitemid 351753871)
    • (2008) Proceedings of the National Academy of Sciences of the United States of America , vol.105 , Issue.14 , pp. 5378-5383
    • Rice, L.M.1    Montabana, E.A.2    Agard, D.A.3


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