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Volumn 288, Issue 37, 2013, Pages 26625-26634

Bacterial division proteins FtsZ and ZipA induce vesicle shrinkage and cell membrane invagination

Author keywords

[No Author keywords available]

Indexed keywords

CELL DIVISIONS; E. COLI; IN-VITRO; INNER MEMBRANES; PERMEABILITY BARRIERS;

EID: 84884200102     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.491688     Document Type: Article
Times cited : (64)

References (53)
  • 1
    • 69249126551 scopus 로고    scopus 로고
    • Bacterial cell division: Assembly, maintenance and disassembly of the Z ring
    • Adams, D. W., and 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
    • 33745209434 scopus 로고    scopus 로고
    • The order of the ring: Assembly of Escherichia coli cell division components
    • Vicente, M., and Rico, A. I. (2006) The order of the ring: assembly of Escherichia coli cell division components. Mol. Microbiol. 61, 5-8
    • (2006) Mol. Microbiol. , vol.61 , pp. 5-8
    • Vicente, M.1    Rico, A.I.2
  • 4
    • 0035853803 scopus 로고    scopus 로고
    • Genetic analysis of the Escherichia coli FtsZ-ZipA interaction in the yeast two-hybrid system: Characterization of FtsZ residues essential for the interactions with ZipA and with FtsA
    • Haney, S. A., Glasfeld, E., Hale, C., Keeney, D., He, Z., and de Boer, P. (2001) Genetic analysis of the Escherichia coli FtsZ-ZipA interaction in the yeast two-hybrid system: characterization of FtsZ residues essential for the interactions with ZipA and with FtsA. J. Biol. Chem. 276, 11980-11987
    • (2001) J. Biol. Chem. , vol.276 , pp. 11980-11987
    • Haney, S.A.1    Glasfeld, E.2    Hale, C.3    Keeney, D.4    He, Z.5    De Boer, P.6
  • 5
    • 84455174351 scopus 로고    scopus 로고
    • Physics of bacterial morphogenesis
    • Sun, S. X., and Jiang, H. (2011) Physics of bacterial morphogenesis. Microbiol. Mol. Biol. Rev. 75, 543-565
    • (2011) Microbiol. Mol. Biol. Rev. , vol.75 , pp. 543-565
    • Sun, S.X.1    Jiang, H.2
  • 7
    • 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
  • 8
    • 0036063886 scopus 로고    scopus 로고
    • Structural evidence that the P/Q domain of ZipA is an unstructured, flexible tether between the membrane and the C-terminal FtsZ-binding domain
    • Ohashi, T., Hale, C. A., de Boer, P. A., and Erickson, H. P. (2002) Structural evidence that the P/Q domain of ZipA is an unstructured, flexible tether between the membrane and the C-terminal FtsZ-binding domain. J. Bacteriol. 184, 4313-4315
    • (2002) J. Bacteriol. , vol.184 , pp. 4313-4315
    • Ohashi, T.1    Hale, C.A.2    De Boer, P.A.3    Erickson, H.P.4
  • 9
    • 84880526897 scopus 로고    scopus 로고
    • Intrinsic disorder of the bacterial cell division protein ZipA: Coil-to-brush conformational transition
    • López-Montero, I., López-Navajas, P., Mingorance, J., Rivas, G., Vélez, M., Vicente, M., and Monroy, F. (2013) Intrinsic disorder of the bacterial cell division protein ZipA: coil-to-brush conformational transition. FASEB J. 27, 3363-3375
    • (2013) FASEB J , vol.27 , pp. 3363-3375
    • López-Montero, I.1    López-Navajas, P.2    Mingorance, J.3    Rivas, G.4    Vélez, M.5    Vicente, M.6    Monroy, F.7
  • 10
    • 15744385269 scopus 로고    scopus 로고
    • Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA
    • Pichoff, S., and Lutkenhaus, J. (2005) Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA. Mol. Microbiol. 55, 1722-1734
    • (2005) Mol. Microbiol. , vol.55 , pp. 1722-1734
    • Pichoff, S.1    Lutkenhaus, J.2
  • 11
    • 44049091371 scopus 로고    scopus 로고
    • Reconstitution of contractile FtsZ rings in liposomes
    • Osawa, M., Anderson, D. E., and Erickson, H. P. (2008) Reconstitution of contractile FtsZ rings in liposomes. Science 320, 792-794
    • (2008) Science , vol.320 , pp. 792-794
    • Osawa, M.1    Anderson, D.E.2    Erickson, H.P.3
  • 12
    • 70450224670 scopus 로고    scopus 로고
    • Curved FtsZ protofilaments generate bending forces on liposome membranes
    • Osawa, M., Anderson, D. E., and Erickson, H. P. (2009) Curved FtsZ protofilaments generate bending forces on liposome membranes. EMBO J. 28, 3476-3484
    • (2009) EMBO J , vol.28 , pp. 3476-3484
    • Osawa, M.1    Anderson, D.E.2    Erickson, H.P.3
  • 13
    • 79960160278 scopus 로고    scopus 로고
    • Inside-out Z rings: Constriction with and without GTP hydrolysis
    • Osawa, M., and Erickson, H. P. (2011) Inside-out Z rings: constriction with and without GTP hydrolysis. Mol. Microbiol. 81, 571-579
    • (2011) Mol. Microbiol. , vol.81 , pp. 571-579
    • Osawa, M.1    Erickson, H.P.2
  • 14
    • 79953208071 scopus 로고    scopus 로고
    • Reconstitution and organization of Escherichia coli proto-ring elements (FtsZ and FtsA) inside giant unilamellar vesicles obtained from bacterial inner membranes
    • Jiménez, M., Martos, A., Vicente, M., and Rivas, G. (2011) Reconstitution and organization of Escherichia coli proto-ring elements (FtsZ and FtsA) inside giant unilamellar vesicles obtained from bacterial inner membranes. J. Biol. Chem. 286, 11236-11241
    • (2011) J. Biol. Chem. , vol.286 , pp. 11236-11241
    • Jiménez, M.1    Martos, A.2    Vicente, M.3    Rivas, G.4
  • 15
    • 84862988236 scopus 로고    scopus 로고
    • Isolation, characterization and lipidbinding properties of the recalcitrant FtsA division protein from Escherichia coli
    • Martos, A., Monterroso, B., Zorrilla, S., Reija, B., Alfonso, C., Mingorance, J., Rivas, G., and Jiménez, M. (2012) Isolation, characterization and lipidbinding properties of the recalcitrant FtsA division protein from Escherichia coli. PLoS One 7, e39829
    • (2012) PLoS One , vol.7
    • Martos, A.1    Monterroso, B.2    Zorrilla, S.3    Reija, B.4    Alfonso, C.5    Mingorance, J.6    Rivas, G.7    Jiménez, M.8
  • 16
    • 84870297573 scopus 로고    scopus 로고
    • Membrane reconstitution of FtsZ-ZipA complex inside giant spherical vesicles made of E. Coli lipids: Large membrane dilation and analysis of membrane plasticity
    • López-Montero, I., López-Navajas, P., Mingorance, J., Vélez, M., Vicente, M., and Monroy, F. (2013) Membrane reconstitution of FtsZ-ZipA complex inside giant spherical vesicles made of E. Coli lipids: large membrane dilation and analysis of membrane plasticity. Biochim. Biophys. Acta 1828, 687-698
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 687-698
    • López-Montero, I.1    López-Navajas, P.2    Mingorance, J.3    Vélez, M.4    Vicente, M.5    Monroy, F.6
  • 17
    • 0018956590 scopus 로고
    • Analysis of gene control signals by DNA fusion and cloning in Escherichia coli
    • Casadaban, M. J., and Cohen, S. N. (1980) Analysis of gene control signals by DNA fusion and cloning in Escherichia coli. J. Mol. Biol. 138, 179-207
    • (1980) J. Mol. Biol. , vol.138 , pp. 179-207
    • Casadaban, M.J.1    Cohen, S.N.2
  • 19
    • 0027176669 scopus 로고
    • Transcription of ftsZ oscillates during the cell cycle of Escherichia coli
    • Garrido, T., Sánchez, M., Palacios, P., Aldea, M., and Vicente, M. (1993) Transcription of ftsZ oscillates during the cell cycle of Escherichia coli. EMBO J. 12, 3957-3965
    • (1993) EMBO J , vol.12 , pp. 3957-3965
    • Garrido, T.1    Sánchez, M.2    Palacios, P.3    Aldea, M.4    Vicente, M.5
  • 21
    • 0028052310 scopus 로고
    • Object-Image: An interactive image analysis program using structured point collection
    • Vischer, N. O. E., Huls, P. G., and Woldringh, C. L. (1994) Object-Image: an interactive image analysis program using structured point collection. BINARY 6
    • (1994) BINARY , vol.6
    • Vischer, N.O.E.1    Huls, P.G.2    Woldringh, C.L.3
  • 22
    • 0033522467 scopus 로고    scopus 로고
    • ZipA is a MAP-Tau homolog and is essential for structural integrity of the cytokinetic FtsZ ring during bacterial cell division
    • RayChaudhuri, D. (1999) ZipA is a MAP-Tau homolog and is essential for structural integrity of the cytokinetic FtsZ ring during bacterial cell division. EMBO J. 18, 2372-2383
    • (1999) EMBO J , vol.18 , pp. 2372-2383
    • Raychaudhuri, D.1
  • 23
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman, L. M., Belin, D., Carson, M. J., and Beckwith, J. (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177, 4121-413
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4413
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 25
    • 78650435603 scopus 로고    scopus 로고
    • Characterization of selfassociation and heteroassociation of bacterial cell division proteins FtsZ and ZipA in solution by composition gradient-static light scattering
    • Martos, A., Alfonso, C., López-Navajas, P., Ahijado-Guzmán, R., Mingorance, J., Minton, A. P., and Rivas, G. (2010) Characterization of selfassociation and heteroassociation of bacterial cell division proteins FtsZ and ZipA in solution by composition gradient-static light scattering. Biochemistry 49, 10780-10787
    • (2010) Biochemistry , vol.49 , pp. 10780-10787
    • Martos, A.1    Alfonso, C.2    López-Navajas, P.3    Ahijado-Guzmán, R.4    Mingorance, J.5    Minton, A.P.6    Rivas, G.7
  • 28
    • 0242584670 scopus 로고    scopus 로고
    • Essential cell division protein FtsZ assembles into one monomer-thick ribbons under conditions resembling the crowded intracellular environment
    • González, J. M., Jiménez, M., Vélez, 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
    • (2003) J. Biol. Chem. , vol.278 , pp. 37664-37671
    • González, J.M.1    Jiménez, M.2    Vélez, M.3    Mingorance, J.4    Andreu, J.M.5    Vicente, M.6    Rivas, G.7
  • 29
    • 80052265964 scopus 로고    scopus 로고
    • Development of a homogeneous fluorescence anisotropy assay to monitor and measure FtsZ assembly in solution
    • Reija, B., Monterroso, B., Jiménez, M., Vicente, M., Rivas, G., and Zorrilla, S. (2011) Development of a homogeneous fluorescence anisotropy assay to monitor and measure FtsZ assembly in solution. Anal. Biochem. 418, 89-96
    • (2011) Anal. Biochem. , vol.418 , pp. 89-96
    • Reija, B.1    Monterroso, B.2    Jiménez, M.3    Vicente, M.4    Rivas, G.5    Zorrilla, S.6
  • 30
    • 84863461276 scopus 로고    scopus 로고
    • Giant vesicles "colonies": A model for primitive cell communities
    • Carrara, P., Stano, P., and Luisi, P. L. (2012) Giant vesicles "colonies": a model for primitive cell communities. ChemBiochem 13, 1497-1502
    • (2012) ChemBiochem , vol.13 , pp. 1497-1502
    • Carrara, P.1    Stano, P.2    Luisi, P.L.3
  • 31
    • 0038061507 scopus 로고    scopus 로고
    • Production of unilamellar vesicles using an inverted emulsion
    • Pautot, S., Frisken, B. J., and Weitz, D. A. (2003) Production of unilamellar vesicles using an inverted emulsion. Langmuir 19, 2870-2879
    • (2003) Langmuir , vol.19 , pp. 2870-2879
    • Pautot, S.1    Frisken, B.J.2    Weitz, D.A.3
  • 32
    • 77951716555 scopus 로고    scopus 로고
    • Giant vesicles: Preparations and applications
    • Walde, P., Cosentino, K., Engel, H., and Stano, P. (2010) Giant vesicles: preparations and applications. ChemBiochem 11, 848-865
    • (2010) ChemBiochem , vol.11 , pp. 848-865
    • Walde, P.1    Cosentino, K.2    Engel, H.3    Stano, P.4
  • 33
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcalβ-hemolysin, a heptameric transmembrane pore
    • Song, L., Hobaugh, M. R., Shustak, C., Cheley, S., Bayley, H., and Gouaux, J. E. (1996) Structure of staphylococcalβ-hemolysin, a heptameric transmembrane pore. Science 274, 1859-1866
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 34
    • 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., Vicente, M., and Mingorance, J. (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
  • 35
    • 77951562635 scopus 로고    scopus 로고
    • Role of Escherichia coli FtsN protein in the assembly and stability of the cell division ring
    • Rico, A. I., García-Ovalle, M., Palacios, P., Casanova, M., and Vicente, M. (2010) Role of Escherichia coli FtsN protein in the assembly and stability of the cell division ring. Mol. Microbiol. 76, 760-771
    • (2010) Mol. Microbiol. , vol.76 , pp. 760-771
    • Rico, A.I.1    García-Ovalle, M.2    Palacios, P.3    Casanova, M.4    Vicente, M.5
  • 36
    • 0037495920 scopus 로고    scopus 로고
    • On the organization of self-assembled actin networks in giant vesicles
    • Limozin, L., Bärmann, M., and Sackmann, E. (2003) On the organization of self-assembled actin networks in giant vesicles. Eur. Phys. J. E Soft Matter 10, 319-330
    • (2003) Eur. Phys. J. e Soft Matter , vol.10 , pp. 319-330
    • Limozin, L.1    Bärmann, M.2    Sackmann, E.3
  • 37
  • 38
    • 79960861902 scopus 로고    scopus 로고
    • Oriented reconstitution of a membrane protein in a giant unilamellar vesicle: Experimental verification with the potassium channel KcsA
    • Yanagisawa, M., Iwamoto, M., Kato, A., Yoshikawa, K., and Oiki, S. (2011) Oriented reconstitution of a membrane protein in a giant unilamellar vesicle: experimental verification with the potassium channel KcsA. J. Am. Chem. Soc. 133, 11774-11779
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 11774-11779
    • Yanagisawa, M.1    Iwamoto, M.2    Kato, A.3    Yoshikawa, K.4    Oiki, S.5
  • 39
    • 0032953626 scopus 로고    scopus 로고
    • Recruitment of ZipA to the septal ring of Escherichia coli is dependent on FtsZ and independent of FtsA
    • Hale, C. A., and de Boer, P. A. (1999) Recruitment of ZipA to the septal ring of Escherichia coli is dependent on FtsZ and independent of FtsA. J. Bacteriol. 181, 167-176
    • (1999) J. Bacteriol. , vol.181 , pp. 167-176
    • Hale, C.A.1    De Boer, P.A.2
  • 40
    • 0036229552 scopus 로고    scopus 로고
    • ZipA is required for recruitment of FtsK, FtsQ, FtsL, and FtsN to the septal ring in Escherichia coli
    • Hale, C. A., and de Boer, P. A. (2002) ZipA is required for recruitment of FtsK, FtsQ, FtsL, and FtsN to the septal ring in Escherichia coli. J. Bacteriol. 184, 2552-2556
    • (2002) J. Bacteriol. , vol.184 , pp. 2552-2556
    • Hale, C.A.1    De Boer, P.A.2
  • 41
    • 0031444158 scopus 로고    scopus 로고
    • Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. Coli
    • Hale, C. A., and de Boer, P. A. (1997) Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. Coli. Cell 88, 175-185
    • (1997) Cell , vol.88 , pp. 175-185
    • Hale, C.A.1    De Boer, P.A.2
  • 42
    • 77955449195 scopus 로고    scopus 로고
    • Membrane potential is important for bacterial cell division
    • Strahl, H., and Hamoen, L. W. (2010) Membrane potential is important for bacterial cell division. Proc. Natl. Acad. Sci. U.S.A. 107, 12281-12286
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 12281-12286
    • Strahl, H.1    Hamoen, L.W.2
  • 43
    • 0037090539 scopus 로고    scopus 로고
    • Exploring intracellular space: Function of the Min system in round-shaped Escherichia coli
    • Corbin, B. D., Yu, X. C., and Margolin, W. (2002) Exploring intracellular space: function of the Min system in round-shaped Escherichia coli. EMBO J. 21, 1998-2008
    • (2002) EMBO J , vol.21 , pp. 1998-2008
    • Corbin, B.D.1    Yu, X.C.2    Margolin, W.3
  • 44
    • 0029806478 scopus 로고    scopus 로고
    • FtsZ-spirals and -arcs determine the shape of the invaginating septa in some mutants of Escherichia coli
    • Addinall, S. G., and Lutkenhaus, J. (1996) FtsZ-spirals and -arcs determine the shape of the invaginating septa in some mutants of Escherichia coli. Mol. Microbiol. 22, 231-237
    • (1996) Mol. Microbiol. , vol.22 , pp. 231-237
    • Addinall, S.G.1    Lutkenhaus, J.2
  • 45
    • 0033492807 scopus 로고    scopus 로고
    • Giant liposomes: From membrane dynamics to cell morphogenesis
    • Hotani, H., Nomura, F., and Suzuki, Y. (1999) Giant liposomes: from membrane dynamics to cell morphogenesis. Curr. Opin. Colloid Interface Sci. 4, 358-368
    • (1999) Curr. Opin. Colloid Interface Sci. , vol.4 , pp. 358-368
    • Hotani, H.1    Nomura, F.2    Suzuki, Y.3
  • 47
    • 77952896939 scopus 로고    scopus 로고
    • Control of actin filament treadmilling in cell motility
    • Bugyi, B., and Carlier, M. F. (2010) Control of actin filament treadmilling in cell motility. Annu. Rev. Biophys. 39, 449-470
    • (2010) Annu. Rev. Biophys. , vol.39 , pp. 449-470
    • Bugyi, B.1    Carlier, M.F.2
  • 48
    • 73949118739 scopus 로고    scopus 로고
    • Molecular mechanisms of Escherichia coli pathogenicity
    • Croxen, M. A., and Finlay, B. B. (2010) Molecular mechanisms of Escherichia coli pathogenicity. Nat. Rev. Microbiol. 8, 26-38
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 26-38
    • Croxen, M.A.1    Finlay, B.B.2
  • 50
    • 84869878393 scopus 로고    scopus 로고
    • Towards a bottom-up reconstitution of bacterial cell division
    • Martos, A., Jiménez, M., Rivas, G., and Schwille, P. (2012) Towards a bottom-up reconstitution of bacterial cell division. Trends Cell Biol. 22, 634-643
    • (2012) Trends Cell Biol. , vol.22 , pp. 634-643
    • Martos, A.1    Jiménez, M.2    Rivas, G.3    Schwille, P.4
  • 51
    • 39749142159 scopus 로고    scopus 로고
    • Conditional lethality, division defects, membrane involution, and endocytosis in mre and mrd shape mutants of Escherichia coli
    • Bendezú, F. O., and de Boer, P. A. (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
    • Bendezú, F.O.1    De Boer, P.A.2
  • 52
    • 84874768439 scopus 로고    scopus 로고
    • Excess membrane synthesis drives a primitive mode of cell proliferation
    • Mercier, R., Kawai, Y., and Errington, J. (2013) Excess membrane synthesis drives a primitive mode of cell proliferation. Cell 152, 997-1007
    • (2013) Cell , vol.152 , pp. 997-1007
    • Mercier, R.1    Kawai, Y.2    Errington, J.3
  • 53
    • 84861151969 scopus 로고    scopus 로고
    • FtsA forms actin-like protofilaments
    • Szwedziak, P., Wang, Q., Freund, S. M., and Löwe, J. (2012) FtsA forms actin-like protofilaments. EMBO J. 31, 2249-2260
    • (2012) EMBO J , vol.31 , pp. 2249-2260
    • Szwedziak, P.1    Wang, Q.2    Freund, S.M.3    Löwe, J.4


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