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Volumn 180, Issue 3, 2012, Pages 531-538

Reconstitution of the Escherichia coli cell division ZipA-FtsZ complexes in nanodiscs as revealed by electron microscopy

Author keywords

Electron microscopy; EM; FtsZ; Nanodisc; Prokaryotic cell division; ZipA

Indexed keywords

BACTERIAL PROTEIN; CARBON; FTSZ PROTEIN; NANODISC; PHOSPHOLIPID; UNCLASSIFIED DRUG; ZIPA PROTEIN;

EID: 84868504605     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2012.08.013     Document Type: Article
Times cited : (15)

References (41)
  • 1
    • 69249126551 scopus 로고    scopus 로고
    • Bacterial cell division: assembly, maintenance and disassembly of the Z ring
    • Adams D.W., Errington J. Bacterial cell division: assembly, maintenance and disassembly of the Z ring. Nat. Rev. Microbiol. 2009, 7:642-653.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 642-653
    • Adams, D.W.1    Errington, J.2
  • 2
    • 0043007514 scopus 로고    scopus 로고
    • Self-assembly of discoidal phospholipid bilayer nanoparticles with membrane scaffold proteins
    • Bayburt T.H., Grinkova Y.V., Sligar S.G. Self-assembly of discoidal phospholipid bilayer nanoparticles with membrane scaffold proteins. Nano Lett. 2002, 2:853-856.
    • (2002) Nano Lett. , vol.2 , pp. 853-856
    • Bayburt, T.H.1    Grinkova, Y.V.2    Sligar, S.G.3
  • 3
    • 42349110895 scopus 로고    scopus 로고
    • The interplay between size, morphology, stability, and functionality of high-density lipoprotein subclasses
    • Cavigiolio G., Shao B., Geier E.G., Ren G., Heinecke J.W., et al. The interplay between size, morphology, stability, and functionality of high-density lipoprotein subclasses. Biochemistry 2008, 47:4770-4779.
    • (2008) Biochemistry , vol.47 , pp. 4770-4779
    • Cavigiolio, G.1    Shao, B.2    Geier, E.G.3    Ren, G.4    Heinecke, J.W.5
  • 4
    • 0042691480 scopus 로고    scopus 로고
    • Direct solubilization of heterologously expressed membrane proteins by incorporation into nanoscale lipid bilayers
    • (556-560-562-563)
    • Civjan N.R., Bayburt T.H., Schuler M.A., Sligar S.G. Direct solubilization of heterologously expressed membrane proteins by incorporation into nanoscale lipid bilayers. BioTechniques 2003, 35:556-560. (556-560-562-563).
    • (2003) BioTechniques , vol.35 , pp. 556-560
    • Civjan, N.R.1    Bayburt, T.H.2    Schuler, M.A.3    Sligar, S.G.4
  • 6
    • 1642382983 scopus 로고    scopus 로고
    • Directed self-assembly of monodisperse phospholipid bilayer nanodiscs with controlled size
    • Denisov I.G., Grinkova Y.V., Lazarides A.A., Sligar S.G. Directed self-assembly of monodisperse phospholipid bilayer nanodiscs with controlled size. J. Am. Chem. Soc. 2004, 126:3477-3487.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3477-3487
    • Denisov, I.G.1    Grinkova, Y.V.2    Lazarides, A.A.3    Sligar, S.G.4
  • 7
    • 79952403634 scopus 로고    scopus 로고
    • Identification and characterization of ZapC, a stabilizer of the FtsZ ring in Escherichia coli
    • Durand-Heredia J.M., Yu H.H., De Carlo S., Lesser C.F., Janakiraman A. Identification and characterization of ZapC, a stabilizer of the FtsZ ring in Escherichia coli. J. Bacteriol. 2011, 193:1405-1413.
    • (2011) J. Bacteriol. , vol.193 , pp. 1405-1413
    • Durand-Heredia, J.M.1    Yu, H.H.2    De Carlo, S.3    Lesser, C.F.4    Janakiraman, A.5
  • 8
    • 78650078263 scopus 로고    scopus 로고
    • FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one
    • Erickson H.P., Anderson D.E., Osawa M. FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one. Microbiol. Mol. Biol. Rev. 2010, 74:504-528.
    • (2010) Microbiol. Mol. Biol. Rev. , vol.74 , pp. 504-528
    • Erickson, H.P.1    Anderson, D.E.2    Osawa, M.3
  • 10
    • 77953494296 scopus 로고    scopus 로고
    • Spatial resolution of two bacterial cell division proteins: ZapA recruits ZapB to the inner face of the Z-ring
    • Galli E., Gerdes K. Spatial resolution of two bacterial cell division proteins: ZapA recruits ZapB to the inner face of the Z-ring. Mol. Microbiol. 2010, 76:1514-1526.
    • (2010) Mol. Microbiol. , vol.76 , pp. 1514-1526
    • Galli, E.1    Gerdes, K.2
  • 11
    • 0037386678 scopus 로고    scopus 로고
    • A gain-of-function mutation in ftsA bypasses the requirement for the essential cell division gene zipA in Escherichia coli
    • Geissler B., Elraheb D., Margolin W. A gain-of-function mutation in ftsA bypasses the requirement for the essential cell division gene zipA in Escherichia coli. Proc. Natl. Acad. Sci. USA 2003, 100:4197-4202.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4197-4202
    • Geissler, B.1    Elraheb, D.2    Margolin, W.3
  • 12
    • 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., et al. Essential cell division protein FtsZ assembles into one monomer-thick ribbons under conditions resembling the crowded intracellular environment. J. Biol. Chem. 2003, 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
  • 13
    • 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., Losick R. A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ. Genes Dev. 2002, 16:2544-2556.
    • (2002) Genes Dev. , vol.16 , pp. 2544-2556
    • Gueiros-Filho, F.J.1    Losick, R.2
  • 14
    • 0033810918 scopus 로고    scopus 로고
    • ZipA-induced bundling of FtsZ polymers mediated by an interaction between C-terminal domains
    • Hale C.A., Rhee A.C., de Boer P.A. ZipA-induced bundling of FtsZ polymers mediated by an interaction between C-terminal domains. J. Bacteriol. 2000, 182:5153-5166.
    • (2000) J. Bacteriol. , vol.182 , pp. 5153-5166
    • Hale, C.A.1    Rhee, A.C.2    de Boer, P.A.3
  • 15
    • 79952401787 scopus 로고    scopus 로고
    • Identification of Escherichia coli ZapC (YcbW) as a component of the division apparatus that binds and bundles FtsZ polymers
    • Hale C.A., Shiomi D., Liu B., Bernhardt T.G., Margolin W., et al. Identification of Escherichia coli ZapC (YcbW) as a component of the division apparatus that binds and bundles FtsZ polymers. J. Bacteriol. 2011, 193:1393-1404.
    • (2011) J. Bacteriol. , vol.193 , pp. 1393-1404
    • Hale, C.A.1    Shiomi, D.2    Liu, B.3    Bernhardt, T.G.4    Margolin, W.5
  • 16
    • 33846246039 scopus 로고    scopus 로고
    • Bacterial cell division: the mechanism and its precison
    • Harry E., Monahan L., Thompson L. Bacterial cell division: the mechanism and its precison. Int. Rev. Cytol. 2006, 253:27-94.
    • (2006) Int. Rev. Cytol. , vol.253 , pp. 27-94
    • Harry, E.1    Monahan, L.2    Thompson, L.3
  • 17
    • 84865737007 scopus 로고    scopus 로고
    • Dynamic interaction of the Escherichia coli cell division ZipA and FtsZ proteins evidenced in nanodiscs
    • Hernandez-Rocamora V.M., Reija B., Garcia C., Natale P., Alfonso C., et al. Dynamic interaction of the Escherichia coli cell division ZipA and FtsZ proteins evidenced in nanodiscs. J. Biol. Chem. 2012, 387:30097-30104.
    • (2012) J. Biol. Chem. , vol.387 , pp. 30097-30104
    • Hernandez-Rocamora, V.M.1    Reija, B.2    Garcia, C.3    Natale, P.4    Alfonso, C.5
  • 18
    • 77649244670 scopus 로고    scopus 로고
    • Three-dimensional structure of the anthrax toxin pore inserted into lipid nanodiscs and lipid vesicles
    • Katayama H., Wang J., Tama F., Chollet L., Gogol E.P., et al. Three-dimensional structure of the anthrax toxin pore inserted into lipid nanodiscs and lipid vesicles. Proc. Natl. Acad. Sci. USA 2010, 107:3453-3457.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 3453-3457
    • Katayama, H.1    Wang, J.2    Tama, F.3    Chollet, L.4    Gogol, E.P.5
  • 19
    • 82555203013 scopus 로고    scopus 로고
    • ZipA binds to FtsZ with high affinity and enhances the stability of FtsZ protofilaments
    • Kuchibhatla A., Bhattacharya A., Panda D. ZipA binds to FtsZ with high affinity and enhances the stability of FtsZ protofilaments. PLoS ONE 2011, 6:e28262.
    • (2011) PLoS ONE , vol.6
    • Kuchibhatla, A.1    Bhattacharya, A.2    Panda, D.3
  • 20
    • 36248938686 scopus 로고    scopus 로고
    • The structure of FtsZ filaments in vivo suggests a force-generating role in cell division
    • Li Z., Trimble M.J., Brun Y.V., Jensen G.J. The structure of FtsZ filaments in vivo suggests a force-generating role in cell division. EMBO J. 2007, 26:4694-4708.
    • (2007) EMBO J. , vol.26 , pp. 4694-4708
    • Li, Z.1    Trimble, M.J.2    Brun, Y.V.3    Jensen, G.J.4
  • 21
    • 2642593025 scopus 로고    scopus 로고
    • Crystal structure of the bacterial cell-division protein FtsZ
    • Löwe J., Amos L.A. Crystal structure of the bacterial cell-division protein FtsZ. Nature 1998, 391:203-206.
    • (1998) Nature , vol.391 , pp. 203-206
    • Löwe, J.1    Amos, L.A.2
  • 22
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: semiautomated software for high-resolution single-particle reconstructions
    • Ludtke S.J., Baldwin P.R., Chiu W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 1999, 128:82-97.
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 23
    • 0033823009 scopus 로고    scopus 로고
    • Themes and variations in prokaryotic cell division
    • Margolin W. Themes and variations in prokaryotic cell division. FEMS Microbiol. Rev. 2000, 24:531-548.
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 531-548
    • Margolin, W.1
  • 24
    • 78650435603 scopus 로고    scopus 로고
    • Characterization of self-association 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-Guzmn R., Mingorance J., et al. Characterization of self-association and heteroassociation of bacterial cell division proteins FtsZ and ZipA in solution by composition gradient-static light scattering. Biochemistry 2010, 49:10780-10787.
    • (2010) Biochemistry , vol.49 , pp. 10780-10787
    • Martos, A.1    Alfonso, C.2    López-Navajas, P.3    Ahijado-Guzmn, R.4    Mingorance, J.5
  • 26
    • 72749125802 scopus 로고    scopus 로고
    • The GTPase activity of Escherichia coli FtsZ determines the magnitude of the FtsZ polymer bundling by ZapA in vitro
    • Mohammadi T., Ploeger G.E.J., Verheul J., Comvalius A.D., Martos A., et al. The GTPase activity of Escherichia coli FtsZ determines the magnitude of the FtsZ polymer bundling by ZapA in vitro. Biochemistry 2009, 48:11056-11066.
    • (2009) Biochemistry , vol.48 , pp. 11056-11066
    • Mohammadi, T.1    Ploeger, G.E.J.2    Verheul, J.3    Comvalius, A.D.4    Martos, A.5
  • 27
    • 0034622589 scopus 로고    scopus 로고
    • Solution structure of ZipA, a crucial component of Escherichia coli cell division
    • Moy F.J., Glasfeld E., Mosyak L., Powers R. Solution structure of ZipA, a crucial component of Escherichia coli cell division. Biochemistry 2000, 39:9146-9156.
    • (2000) Biochemistry , vol.39 , pp. 9146-9156
    • Moy, F.J.1    Glasfeld, E.2    Mosyak, L.3    Powers, R.4
  • 28
    • 33847639732 scopus 로고    scopus 로고
    • Applications of phospholipid bilayer nanodiscs in the study of membranes and membrane proteins
    • Nath A., Atkins W.M., Sligar S.G. Applications of phospholipid bilayer nanodiscs in the study of membranes and membrane proteins. Biochemistry 2007, 46:2059-2069.
    • (2007) Biochemistry , vol.46 , pp. 2059-2069
    • Nath, A.1    Atkins, W.M.2    Sligar, S.G.3
  • 29
    • 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.J., Erickson H.P. 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. 2002, 184:4313-4315.
    • (2002) J. Bacteriol. , vol.184 , pp. 4313-4315
    • Ohashi, T.1    Hale, C.A.2    de Boer, P.A.J.3    Erickson, H.P.4
  • 30
  • 31
    • 71749095971 scopus 로고    scopus 로고
    • Structural and functional characterization of the integral membrane protein VDAC-1 in lipid bilayer nanodiscs
    • Raschle T., Hiller S., Yu T.-Y., Rice A.J., Walz T., et al. Structural and functional characterization of the integral membrane protein VDAC-1 in lipid bilayer nanodiscs. J. Am. Chem. Soc. 2009, 131:17777-17779.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 17777-17779
    • Raschle, T.1    Hiller, S.2    Yu, T.-Y.3    Rice, A.J.4    Walz, T.5
  • 32
    • 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. ZipA is a MAP-Tau homolog and is essential for structural integrity of the cytokinetic FtsZ ring during bacterial cell division. EMBO J. 1999, 18:2372-2383.
    • (1999) EMBO J. , vol.18 , pp. 2372-2383
    • RayChaudhuri, D.1
  • 34
    • 0040735625 scopus 로고    scopus 로고
    • Magnesium-induced linear self-association of the FtsZ bacterial cell division protein monomer. The primary steps for FtsZ assembly
    • Rivas G., López A., Mingorance J., Ferrándiz M.J., Zorrilla S., Minton A.P., et al. Magnesium-induced linear self-association of the FtsZ bacterial cell division protein monomer. The primary steps for FtsZ assembly. J. Biol. Chem. 2000, 275:11740-11749.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11740-11749
    • Rivas, G.1    López, A.2    Mingorance, J.3    Ferrándiz, M.J.4    Zorrilla, S.5    Minton, A.P.6
  • 35
    • 84863338243 scopus 로고    scopus 로고
    • SNARE proteins: one to fuse and three to keep the nascent fusion pore open
    • Shi L., Shen Q.T., Kiel A., Wang J., Wang H.W., et al. SNARE proteins: one to fuse and three to keep the nascent fusion pore open. Science 2012, 335:1355-1359.
    • (2012) Science , vol.335 , pp. 1355-1359
    • Shi, L.1    Shen, Q.T.2    Kiel, A.3    Wang, J.4    Wang, H.W.5
  • 36
    • 0037022642 scopus 로고    scopus 로고
    • Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching
    • Stricker J., Maddox P., Salmon E.D., Erickson H.P. Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching. Proc. Natl. Acad. Sci. USA 2002, 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
  • 37
    • 0020509332 scopus 로고
    • A rapid procedure for preparing fluorescein-labeled specific antibodies from whole antiserum: its use in analyzing cytoskeletal architecture
    • Talian J.C., Olmsted J.B., Goldman R.D. A rapid procedure for preparing fluorescein-labeled specific antibodies from whole antiserum: its use in analyzing cytoskeletal architecture. J. Cell Biol. 1983, 97:1277-1282.
    • (1983) J. Cell Biol. , vol.97 , pp. 1277-1282
    • Talian, J.C.1    Olmsted, J.B.2    Goldman, R.D.3
  • 38
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: an extensible image processing suite for electron microscopy
    • Tang G., Peng L., Baldwin P.R., Mann D.S., Jiang W., et al. EMAN2: an extensible image processing suite for electron microscopy. J. Struct. Biol. 2007, 157:38-46.
    • (2007) J. Struct. Biol. , vol.157 , pp. 38-46
    • Tang, G.1    Peng, L.2    Baldwin, P.R.3    Mann, D.S.4    Jiang, W.5
  • 39
    • 33745209434 scopus 로고    scopus 로고
    • The order of the ring: assembly of Escherichia coli cell division components
    • Vicente M., Rico A.I. The order of the ring: assembly of Escherichia coli cell division components. Mol. Microbiol. 2006, 61:5-8.
    • (2006) Mol. Microbiol. , vol.61 , pp. 5-8
    • Vicente, M.1    Rico, A.I.2
  • 40
    • 75749154495 scopus 로고    scopus 로고
    • Recreation of the terminal events in physiological integrin activation
    • Ye F., Hu G., Taylor D., Ratnikov B., Bobkov A.A., et al. Recreation of the terminal events in physiological integrin activation. J. Cell Biol. 2010, 188:157-173.
    • (2010) J. Cell Biol. , vol.188 , pp. 157-173
    • Ye, F.1    Hu, G.2    Taylor, D.3    Ratnikov, B.4    Bobkov, A.A.5
  • 41
    • 78650876748 scopus 로고    scopus 로고
    • Morphology and structure of lipoproteins revealed by an optimized negative-staining protocol of electron microscopy
    • Zhang L., Song J., Cavigiolio G., Ishida B.Y., Zhang S., et al. Morphology and structure of lipoproteins revealed by an optimized negative-staining protocol of electron microscopy. J. Lipid Res. 2011, 52:175-184.
    • (2011) J. Lipid Res. , vol.52 , pp. 175-184
    • Zhang, L.1    Song, J.2    Cavigiolio, G.3    Ishida, B.Y.4    Zhang, S.5


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