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Volumn 7, Issue 4, 2018, Pages 953-961

De Novo Synthesis of Basal Bacterial Cell Division Proteins FtsZ, FtsA, and ZipA Inside Giant Vesicles

Author keywords

cell division; Cell free translation; FtsZ; giant vesicles; PURE system; synthetic cell

Indexed keywords

BACTERIAL PROTEIN; FTSA PROTEIN; FTSZ PROTEIN; UNCLASSIFIED DRUG; ZIPA PROTEIN; 1-PALMITOYL-2-OLEOYLGLYCERO-3-PHOSPHOGLYCEROL; 1-PALMITOYL-2-OLEOYLPHOSPHATIDYLCHOLINE; CARRIER PROTEIN; CELL CYCLE PROTEIN; CYTOSKELETON PROTEIN; ESCHERICHIA COLI PROTEIN; FTSA PROTEIN, E COLI; FTSZ PROTEIN, BACTERIA; GREEN FLUORESCENT PROTEIN; GUANOSINE TRIPHOSPHATE; LIPOSOME; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLGLYCEROL; ZIPA PROTEIN, E COLI;

EID: 85045854321     PISSN: None     EISSN: 21615063     Source Type: Journal    
DOI: 10.1021/acssynbio.7b00350     Document Type: Article
Times cited : (61)

References (43)
  • 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, 642-53, 10.1038/nrmicro2198
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 642-653
    • Adams, D.W.1    Errington, J.2
  • 2
    • 84962069677 scopus 로고    scopus 로고
    • Splitsville: Structural and functional insights into the dynamic bacterial Z ring
    • Haeusser, D. and Margolin, W. (2016) Splitsville: structural and functional insights into the dynamic bacterial Z ring. Nat. Rev. Microbiol. 14, 305-319, 10.1038/nrmicro.2016.26
    • (2016) Nat. Rev. Microbiol. , vol.14 , pp. 305-319
    • Haeusser, D.1    Margolin, W.2
  • 3
    • 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, 1722-34, 10.1111/j.1365-2958.2005.04522.x
    • (2005) Mol. Microbiol. , vol.55 , pp. 1722-1734
    • Pichoff, S.1    Lutkenhaus, J.2
  • 4
    • 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. J. (1997) Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. coli. Cell 88, 175-85, 10.1016/S0092-8674(00)81838-3
    • (1997) Cell , vol.88 , pp. 175-185
    • Hale, C.A.1    De Boer, P.A.J.2
  • 5
    • 84862988236 scopus 로고    scopus 로고
    • Isolation, Characterization and Lipid-Binding 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 Lipid-Binding Properties of the Recalcitrant FtsA Division Protein from Escherichia coli. PLoS One 7, e39829, 10.1371/journal.pone.0039829
    • (2012) PLoS One , vol.7 , pp. e39829
    • Martos, A.1    Monterroso, B.2    Zorrilla, S.3    Reija, B.4    Alfonso, C.5    Mingorance, J.6    Rivas, G.7    Jiménez, M.8
  • 6
    • 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., and Boer, P. A. de. (2000) ZipA-induced bundling of FtsZ polymers mediated by an interaction between C-terminal domains. J. Bacteriol. 182, 5153-66, 10.1128/JB.182.18.5153-5166.2000
    • (2000) J. Bacteriol. , vol.182 , pp. 5153-5166
    • Hale, C.A.1    Rhee, A.C.2    De Boer, P.A.3
  • 7
    • 84857375148 scopus 로고    scopus 로고
    • The Escherichia coli cell division protein ZipA forms homodimers prior to association with FtsZ
    • Skoog, K. and Daley, D. O. (2012) The Escherichia coli cell division protein ZipA forms homodimers prior to association with FtsZ. Biochemistry 51, 1407-15, 10.1021/bi2015647
    • (2012) Biochemistry , vol.51 , pp. 1407-1415
    • Skoog, K.1    Daley, D.O.2
  • 8
    • 84891344282 scopus 로고    scopus 로고
    • The bacterial cell division proteins FtsA and FtsZ self-organize into dynamic cytoskeletal patterns
    • Loose, M. and Mitchison, T. (2014) The bacterial cell division proteins FtsA and FtsZ self-organize into dynamic cytoskeletal patterns. Nat. Cell Biol. 16, 38-46, 10.1038/ncb2885
    • (2014) Nat. Cell Biol. , vol.16 , pp. 38-46
    • Loose, M.1    Mitchison, T.2
  • 10
    • 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, 2372-83, 10.1093/emboj/18.9.2372
    • (1999) EMBO J. , vol.18 , pp. 2372-2383
    • Raychaudhuri, D.1
  • 11
    • 84929660640 scopus 로고    scopus 로고
    • FtsZ Polymers Tethered to the Membrane by ZipA Are Susceptible to Spatial Regulation by Min Waves
    • Martos, A., Raso, A., Jiménez, M., Petrášek, Z., Rivas, G., and Schwille, P. (2015) FtsZ Polymers Tethered to the Membrane by ZipA Are Susceptible to Spatial Regulation by Min Waves. Biophys. J. 108, 2371-2383, 10.1016/j.bpj.2015.03.031
    • (2015) Biophys. J. , vol.108 , pp. 2371-2383
    • Martos, A.1    Raso, A.2    Jiménez, M.3    Petrášek, Z.4    Rivas, G.5    Schwille, P.6
  • 12
    • 84879700551 scopus 로고    scopus 로고
    • Liposome division by a simple bacterial division machinery
    • Osawa, M. and Erickson, H. P. (2013) Liposome division by a simple bacterial division machinery. Proc. Natl. Acad. Sci. U. S. A. 110, 11000-4, 10.1073/pnas.1222254110
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 11000-11004
    • Osawa, M.1    Erickson, H.P.2
  • 13
    • 84990997649 scopus 로고    scopus 로고
    • Architecture of the ring formed by the tubulin homologue FtsZ in bacterial cell division
    • Szwedziak, P., Wang, Q., Bharat, T., Tsim, M., and Löwe, J. (2014) Architecture of the ring formed by the tubulin homologue FtsZ in bacterial cell division. eLife 3, e04601, 10.7554/eLife.04601
    • (2014) ELife , vol.3 , pp. e04601
    • Szwedziak, P.1    Wang, Q.2    Bharat, T.3    Tsim, M.4    Löwe, J.5
  • 14
    • 84920896637 scopus 로고    scopus 로고
    • Role of the FtsA C terminus as a switch for polymerization and membrane association
    • Krupka, M., Cabré, E. J., Jiménez, M., Rivas, G., Rico, A. I., and Vicente, M. (2014) Role of the FtsA C terminus as a switch for polymerization and membrane association. mBio 5, e02221, 10.1128/mBio.02221-14
    • (2014) MBio , vol.5 , pp. e02221
    • Krupka, M.1    Cabré, E.J.2    Jiménez, M.3    Rivas, G.4    Rico, A.I.5    Vicente, M.6
  • 15
    • 77955246394 scopus 로고    scopus 로고
    • Direct integration of cell-free-synthesized connexin-43 into liposomes and hemichannel formation
    • Moritani, Y., Nomura, S. M., Morita, I., and Akiyoshi, K. (2010) Direct integration of cell-free-synthesized connexin-43 into liposomes and hemichannel formation. FEBS J. 277, 3343-52, 10.1111/j.1742-4658.2010.07736.x
    • (2010) FEBS J. , vol.277 , pp. 3343-3352
    • Moritani, Y.1    Nomura, S.M.2    Morita, I.3    Akiyoshi, K.4
  • 16
    • 84904470988 scopus 로고    scopus 로고
    • In vitro synthesis of the E. coli Sec translocon from DNA
    • Matsubayashi, H., Kuruma, Y., and Ueda, T. (2014) In vitro synthesis of the E. coli Sec translocon from DNA. Angew. Chem., Int. Ed. 53, 7535-8, 10.1002/anie.201403929
    • (2014) Angew. Chem., Int. Ed. , vol.53 , pp. 7535-7538
    • Matsubayashi, H.1    Kuruma, Y.2    Ueda, T.3
  • 17
    • 11144220854 scopus 로고    scopus 로고
    • A vesicle bioreactor as a step toward an artificial cell assembly
    • Noireaux, V. and Libchaber, A. (2004) A vesicle bioreactor as a step toward an artificial cell assembly. Proc. Natl. Acad. Sci. U. S. A. 101, 17669-74, 10.1073/pnas.0408236101
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 17669-17674
    • Noireaux, V.1    Libchaber, A.2
  • 18
    • 70349778973 scopus 로고    scopus 로고
    • Microfluidic Formation of Monodisperse, Cell-Sized, and Unilamellar Vesicles
    • Ota, S., Yoshizawa, S., and Takeuchi, S. (2009) Microfluidic Formation of Monodisperse, Cell-Sized, and Unilamellar Vesicles. Angew. Chem., Int. Ed. 48, 6533-6537, 10.1002/anie.200902182
    • (2009) Angew. Chem., Int. Ed. , vol.48 , pp. 6533-6537
    • Ota, S.1    Yoshizawa, S.2    Takeuchi, S.3
  • 19
    • 84902130440 scopus 로고    scopus 로고
    • Liposome display for in vitro selection and evolution of membrane proteins
    • Fujii, S., Matsuura, T., Sunami, T., Nishikawa, T., Kazuta, Y., and Yomo, T. (2014) Liposome display for in vitro selection and evolution of membrane proteins. Nat. Protoc. 9, 1578-91, 10.1038/nprot.2014.107
    • (2014) Nat. Protoc. , vol.9 , pp. 1578-1591
    • Fujii, S.1    Matsuura, T.2    Sunami, T.3    Nishikawa, T.4    Kazuta, Y.5    Yomo, T.6
  • 20
    • 84964555320 scopus 로고    scopus 로고
    • Cell-free compartmentalized protein synthesis inside double emulsion templated liposomes with in vitro synthesized and assembled ribosomes
    • Caschera, F., Lee, J., Ho, K., Liu, A., and Jewett, M. (2016) Cell-free compartmentalized protein synthesis inside double emulsion templated liposomes with in vitro synthesized and assembled ribosomes. Chem. Commun. 52, 5467-9, 10.1039/C6CC00223D
    • (2016) Chem. Commun. , vol.52 , pp. 5467-5469
    • Caschera, F.1    Lee, J.2    Ho, K.3    Liu, A.4    Jewett, M.5
  • 22
    • 20444457941 scopus 로고    scopus 로고
    • Rapid in vitro assembly dynamics and subunit turnover of FtsZ demonstrated by fluorescence resonance energy transfer
    • 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, 22549-54, 10.1074/jbc.M500895200
    • (2005) J. Biol. Chem. , vol.280 , pp. 22549-22554
    • Chen, Y.1    Erickson, H.P.2
  • 23
    • 63149130741 scopus 로고    scopus 로고
    • Bimodal protein solubility distribution revealed by an aggregation analysis of the entire ensemble of Escherichia coli proteins
    • Niwa, T., Ying, B. -W. W., Saito, K., Jin, W., Takada, S., Ueda, T., and Taguchi, H. (2009) Bimodal protein solubility distribution revealed by an aggregation analysis of the entire ensemble of Escherichia coli proteins. Proc. Natl. Acad. Sci. U. S. A. 106, 4201-6, 10.1073/pnas.0811922106
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 4201-4206
    • Niwa, T.1    Ying, B.-W.W.2    Saito, K.3    Jin, W.4    Takada, S.5    Ueda, T.6    Taguchi, H.7
  • 24
    • 0028008820 scopus 로고
    • Mutations in ftsZ that confer resistance to SulA affect the interaction of FtsZ with GTP
    • Dai, K., Mukherjee, A., Xu, Y., and Lutkenhaus (1994) Mutations in ftsZ that confer resistance to SulA affect the interaction of FtsZ with GTP. J. Bacteriol. 176, 130-136, 10.1128/jb.176.1.130-136.1994
    • (1994) J. Bacteriol. , vol.176 , pp. 130-136
    • Dai, K.1    Mukherjee, A.2    Xu, Y.3    Lutkenhaus4
  • 25
    • 0029851154 scopus 로고    scopus 로고
    • Colocalization of cell division proteins FtsZ and FtsA to cytoskeletal structures in living Escherichia coli cells by using green fluorescent protein
    • Ma, X., Ehrhardt, D., and Margolin, W. (1996) Colocalization of cell division proteins FtsZ and FtsA to cytoskeletal structures in living Escherichia coli cells by using green fluorescent protein. Proc. Natl. Acad. Sci. U. S. A. 93, 12998-13003, 10.1073/pnas.93.23.12998
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 12998-13003
    • Ma, X.1    Ehrhardt, D.2    Margolin, W.3
  • 27
    • 0141925615 scopus 로고    scopus 로고
    • The MinD membrane targeting sequence is a transplantable lipid-binding helix
    • Szeto, T., Rowland, S., Habrukowich, C., and King, G. (2003) The MinD membrane targeting sequence is a transplantable lipid-binding helix. J. Biol. Chem. 278, 40050-6, 10.1074/jbc.M306876200
    • (2003) J. Biol. Chem. , vol.278 , pp. 40050-40056
    • Szeto, T.1    Rowland, S.2    Habrukowich, C.3    King, G.4
  • 28
    • 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, 3476-84, 10.1038/emboj.2009.277
    • (2009) EMBO J. , vol.28 , pp. 3476-3484
    • Osawa, M.1    Anderson, D.E.2    Erickson, H.P.3
  • 29
    • 84903137672 scopus 로고    scopus 로고
    • In Vitro Membrane Protein Synthesis Inside Cell-Sized Vesicles Reveals the Dependence of Membrane Protein Integration on Vesicle Volume
    • Soga, H., Fujii, S., Yomo, T., Kato, Y., Watanabe, H., and Matsuura, T. (2014) In Vitro Membrane Protein Synthesis Inside Cell-Sized Vesicles Reveals the Dependence of Membrane Protein Integration on Vesicle Volume. ACS Synth. Biol. 3, 372-379, 10.1021/sb400094c
    • (2014) ACS Synth. Biol. , vol.3 , pp. 372-379
    • Soga, H.1    Fujii, S.2    Yomo, T.3    Kato, Y.4    Watanabe, H.5    Matsuura, T.6
  • 30
    • 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., Velez, M., 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, 10.1074/jbc.M305230200
    • (2003) J. Biol. Chem. , vol.278 , pp. 37664-37671
    • Gonzalez, J.1    Velez, M.2    Andreu, J.M.3    Vicente, M.4    Rivas, G.5
  • 31
  • 32
    • 0033031388 scopus 로고    scopus 로고
    • Visualization of membrane domains in Escherichia coli
    • Fishov and Woldringh (1999) Visualization of membrane domains in Escherichia coli. Mol. Microbiol. 32, 1166-72, 10.1046/j.1365-2958.1999.01425.x
    • (1999) Mol. Microbiol. , vol.32 , pp. 1166-1172
    • Fishov1    Woldringh2
  • 33
    • 84907015800 scopus 로고    scopus 로고
    • Localization of anionic phospholipids in Escherichia coli cells
    • Oliver, P. M., Crooks, J. A., Leidl, M., and Yoon, E. J. (2014) Localization of anionic phospholipids in Escherichia coli cells. J. Bacteriol. 196, 3386-98, 10.1128/JB.01877-14
    • (2014) J. Bacteriol. , vol.196 , pp. 3386-3398
    • Oliver, P.M.1    Crooks, J.A.2    Leidl, M.3    Yoon, E.J.4
  • 35
    • 84984620247 scopus 로고    scopus 로고
    • Cell-sized asymmetric lipid vesicles facilitate the investigation of asymmetric membranes
    • Kamiya, K., Kawano, R., Osaki, T., Akiyoshi, K., and Takeuchi, S. (2016) Cell-sized asymmetric lipid vesicles facilitate the investigation of asymmetric membranes. Nat. Chem. 8, 881-889, 10.1038/nchem.2537
    • (2016) Nat. Chem. , vol.8 , pp. 881-889
    • Kamiya, K.1    Kawano, R.2    Osaki, T.3    Akiyoshi, K.4    Takeuchi, S.5
  • 36
    • 77955489876 scopus 로고    scopus 로고
    • Cytoskeletal Cross-linking and Bundling in Motor-Independent Contraction
    • Sun, S., Walcott, S., and Wolgemuth, C. (2010) Cytoskeletal Cross-linking and Bundling in Motor-Independent Contraction. Curr. Biol. 20, R649-R654, 10.1016/j.cub.2010.07.004
    • (2010) Curr. Biol. , vol.20 , pp. R649-R654
    • Sun, S.1    Walcott, S.2    Wolgemuth, C.3
  • 37
    • 84959206512 scopus 로고    scopus 로고
    • Defining the rate-limiting processes of bacterial cytokinesis
    • Coltharp, C., Buss, J., Plumer, T., and Xiao, J. (2016) Defining the rate-limiting processes of bacterial cytokinesis. Proc. Natl. Acad. Sci. U. S. A. 113, E1044-E1053, 10.1073/pnas.1514296113
    • (2016) Proc. Natl. Acad. Sci. U. S. A. , vol.113 , pp. E1044-E1053
    • Coltharp, C.1    Buss, J.2    Plumer, T.3    Xiao, J.4
  • 38
    • 84897109056 scopus 로고    scopus 로고
    • Disassembly of the divisome in Escherichia coli: Evidence that FtsZ dissociates before compartmentalization
    • Söderström, B., Skoog, K., Blom, H., Weiss, D. S., von Heijne, G., and Daley, D. O. (2014) Disassembly of the divisome in Escherichia coli: evidence that FtsZ dissociates before compartmentalization. Mol. Microbiol. 92, 1-9, 10.1111/mmi.12534
    • (2014) Mol. Microbiol. , vol.92 , pp. 1-9
    • Söderström, B.1    Skoog, K.2    Blom, H.3    Weiss, D.S.4    Von Heijne, G.5    Daley, D.O.6
  • 39
    • 31344455122 scopus 로고    scopus 로고
    • Approaches to semi-synthetic minimal cells: A review
    • Luisi, P., Ferri, F., and Stano, P. (2006) Approaches to semi-synthetic minimal cells: a review. Naturwissenschaften 93, 113, 10.1007/s00114-005-0056-z
    • (2006) Naturwissenschaften , vol.93 , pp. 113
    • Luisi, P.1    Ferri, F.2    Stano, P.3
  • 40
    • 59249084001 scopus 로고    scopus 로고
    • A synthetic biology approach to the construction of membrane proteins in semi-synthetic minimal cells
    • Kuruma, Y., Stano, P., Ueda, T., and Luisi, P. L. (2009) A synthetic biology approach to the construction of membrane proteins in semi-synthetic minimal cells. Biochim. Biophys. Acta, Biomembr. 1788, 567-74, 10.1016/j.bbamem.2008.10.017
    • (2009) Biochim. Biophys. Acta, Biomembr. , vol.1788 , pp. 567-574
    • Kuruma, Y.1    Stano, P.2    Ueda, T.3    Luisi, P.L.4
  • 41
    • 84990963875 scopus 로고    scopus 로고
    • Cell-Free Phospholipid Biosynthesis by Gene-Encoded Enzymes Reconstituted in Liposomes
    • Scott, A., Noga, M., Graaf, P., de Westerlaken, I., Yildirim, E., and Danelon, C. (2016) Cell-Free Phospholipid Biosynthesis by Gene-Encoded Enzymes Reconstituted in Liposomes. PLoS One 11, e0163058, 10.1371/journal.pone.0163058
    • (2016) PLoS One , vol.11 , pp. e0163058
    • Scott, A.1    Noga, M.2    Graaf, P.3    De Westerlaken, I.4    Yildirim, E.5    Danelon, C.6
  • 42
    • 84940489518 scopus 로고    scopus 로고
    • The PURE system for the cell-free synthesis of membrane proteins
    • Kuruma, Y. and Ueda, T. (2015) The PURE system for the cell-free synthesis of membrane proteins. Nat. Protoc. 10, 1328-44, 10.1038/nprot.2015.082
    • (2015) Nat. Protoc. , vol.10 , pp. 1328-1344
    • Kuruma, Y.1    Ueda, T.2
  • 43
    • 84881490273 scopus 로고    scopus 로고
    • Cooperative working of bacterial chromosome replication proteins generated by a reconstituted protein expression system
    • Fujiwara, K., Katayama, T., and Nomura, S. M. (2013) Cooperative working of bacterial chromosome replication proteins generated by a reconstituted protein expression system. Nucleic Acids Res. 41, 7176-83, 10.1093/nar/gkt489
    • (2013) Nucleic Acids Res. , vol.41 , pp. 7176-7183
    • Fujiwara, K.1    Katayama, T.2    Nomura, S.M.3


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