메뉴 건너뛰기




Volumn 1, Issue 2, 2012, Pages 53-59

Assembly of MreB filaments on liposome membranes: A synthetic biology approach

Author keywords

Artificial cells; Bacterial cytoskeleton MreB; Cell free gene expression; Vesicle bioreactor

Indexed keywords

BACTERIAL PROTEIN; LIPOSOME; MREB PROTEIN; PROTEIN MREC; UNCLASSIFIED DRUG;

EID: 84859579073     PISSN: None     EISSN: 21615063     Source Type: Journal    
DOI: 10.1021/sb200003v     Document Type: Article
Times cited : (94)

References (32)
  • 2
    • 69249235852 scopus 로고    scopus 로고
    • Biology under construction: In vitro reconstitution of cellular function
    • Liu, A. P., and Fletcher, D. A. (2009) Biology under construction: In vitro reconstitution of cellular function. Nat. Rev. Mol. Cell Biol. 2009 (10), 644-650.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.2009 , Issue.10 , pp. 644-650
    • Liu, A.P.1    Fletcher, D.A.2
  • 3
    • 33845965687 scopus 로고    scopus 로고
    • Synthetic biology projects in vitro
    • DOI 10.1101/gr.5776007
    • Forster, A. C., and Church, G. M. (2007) Synthetic biology projects in vitro. Genome Res. 17, 1-6. (Pubitemid 46041659)
    • (2007) Genome Research , vol.17 , Issue.1 , pp. 1-6
    • Forster, A.C.1    Church, G.M.2
  • 4
    • 63049085934 scopus 로고    scopus 로고
    • Self-assembly approaches for the construction of cell architecture mimics
    • Brizard, A. M., and van Esch, J. H. (2009) Self-assembly approaches for the construction of cell architecture mimics. Soft Matter 5, 1320-1327.
    • (2009) Soft Matter , vol.5 , pp. 1320-1327
    • Brizard, A.M.1    Van Esch, J.H.2
  • 6
    • 77956537388 scopus 로고    scopus 로고
    • Self-assembly of filopodia-like structures on supported lipid bilayers
    • Lee, K., Gallop, J. L., Rambani, K., and Kirschner, M. W. (2010) Self-assembly of filopodia-like structures on supported lipid bilayers. Science 329, 1341-1345.
    • (2010) Science , vol.329 , pp. 1341-1345
    • Lee, K.1    Gallop, J.L.2    Rambani, K.3    Kirschner, M.W.4
  • 8
    • 0026482154 scopus 로고
    • Morphological changes in liposomes caused by polymerization of encapsulated actin and spontaneous formation of actin bundles
    • Miyata, H., and Hotani, H. (1992) Morphological changes in liposomes caused by polymerization of encapsulated actin and spontaneous formation of actin bundles. Proc. Natl. Acad. Sci. U.S.A. 89, 11547-11551.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 11547-11551
    • Miyata, H.1    Hotani, H.2
  • 10
    • 55549106113 scopus 로고    scopus 로고
    • Entrapping desired amounts of actin filaments and molecular motor proteins in giant liposomes
    • Takiguchi, K., Yamada, A., Negishi, M., Tanaka-Takiguchi, Y., and Yoshikawa, K. (2008) Entrapping desired amounts of actin filaments and molecular motor proteins in giant liposomes. Langmuir 24, 11323-11326.
    • (2008) Langmuir , vol.24 , pp. 11323-11326
    • Takiguchi, K.1    Yamada, A.2    Negishi, M.3    Tanaka-Takiguchi, Y.4    Yoshikawa, K.5
  • 12
    • 0031372605 scopus 로고    scopus 로고
    • Mechanics of microtubule-based membrane extension
    • Fygenson, D. K., Marko, J. F., and Libchaber, A. (1997) Mechanics of microtubule-based membrane extension. Phys. Rev. Lett. 79, 4497.
    • (1997) Phys. Rev. Lett. , vol.79 , pp. 4497
    • Fygenson, D.K.1    Marko, J.F.2    Libchaber, A.3
  • 13
    • 67349200275 scopus 로고    scopus 로고
    • Effects of confinement on the self-organization of microtubules and motors
    • Pinot, M., Chesnel, F., Kubiak, J. Z., Arnal, I., Nedelec, F. J., and Gueroui, Z. (2009) Effects of confinement on the self-organization of microtubules and motors. Curr. Biol. 19, 954-960.
    • (2009) Curr. Biol. , vol.19 , pp. 954-960
    • Pinot, M.1    Chesnel, F.2    Kubiak, J.Z.3    Arnal, I.4    Nedelec, F.J.5    Gueroui, Z.6
  • 16
    • 44049091371 scopus 로고    scopus 로고
    • Reconstitution of contractile FtsZ rings in liposomes
    • DOI 10.1126/science.1154520
    • Osawa, M., Anderson, D. E., and Erickson, H. P. (2008) Reconstitution of contractile FtsZ rings in liposomes. Science 320, 792-794. (Pubitemid 351929627)
    • (2008) Science , vol.320 , Issue.5877 , pp. 792-794
    • Osawa, M.1    Anderson, D.E.2    Erickson, H.P.3
  • 17
    • 58649111971 scopus 로고    scopus 로고
    • Actin homolog MreB affects chromosome segregation by regulating topoisomerase 4 in Escherichia coli
    • Madabhushi, R., and Marians, K. J. (2009) Actin homolog MreB affects chromosome segregation by regulating topoisomerase 4 in Escherichia coli. Mol. Cell 33, 171-180.
    • (2009) Mol. Cell , vol.33 , pp. 171-180
    • Madabhushi, R.1    Marians, K.J.2
  • 18
    • 12344306119 scopus 로고    scopus 로고
    • The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex
    • DOI 10.1111/j.1365-2958.2004.04367.x
    • Kruse, T., Bork-Jensen, J., and Gerdes, K. (2005) The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane bound complex. Mol. Microbiol. 55, 78-89. (Pubitemid 40127886)
    • (2005) Molecular Microbiology , vol.55 , Issue.1 , pp. 78-89
    • Kruse, T.1    Bork-Jensen, J.2    Gerdes, K.3
  • 19
    • 33751363915 scopus 로고    scopus 로고
    • Dimeric structure of the cell shape protein MreC and its functional implications
    • DOI 10.1111/j.1365-2958.2006.05485.x
    • van den Ent, F., Leaver, M., Bendezu, F., Errington, J., Boer, P. D., and Lowe, J. (2006) Dimeric structure of the cell shape protein MreC and its functional implications. Mol. Microbiol. 62, 1631-1642. (Pubitemid 44813809)
    • (2006) Molecular Microbiology , vol.62 , Issue.6 , pp. 1631-1642
    • Van Den Ent, F.1    Leaver, M.2    Bendezu, F.3    Errington, J.4    De Boer, P.5    Lowe, J.6
  • 23
    • 79952775158 scopus 로고    scopus 로고
    • Development of an artificial cell, from self-organization to computation and self-reproduction
    • Noireaux, V., Maeda, Y. T., and Libchaber, A. (2011) Development of an artificial cell, from self-organization to computation and self-reproduction. Proc. Natl. Acad. Sci. U.S.A. 108, 3473-3480.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 3473-3480
    • Noireaux, V.1    Maeda, Y.T.2    Libchaber, A.3
  • 24
    • 78649779373 scopus 로고    scopus 로고
    • α-hemolysin pore formation into a supported phospholipid bilayer using cell free expression
    • Chalmeau, J., Monina, N., Shin, J., Vieu, C., and Noireaux, V. (2011) α-Hemolysin pore formation into a supported phospholipid bilayer using cell free expression. Biochim. Biophys. Acta 1808, 271-278.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 271-278
    • Chalmeau, J.1    Monina, N.2    Shin, J.3    Vieu, C.4    Noireaux, V.5
  • 25
    • 78649788244 scopus 로고    scopus 로고
    • Efficient cell-free expression with the endogenous E. coli RNA polymerase and sigma factor 70
    • Shin, J., and Noireaux, V. (2010) Efficient cell-free expression with the endogenous E. coli RNA polymerase and sigma factor 70. J. Biol. Eng. 4, 8.
    • (2010) J. Biol. Eng. , vol.4 , pp. 8
    • Shin, J.1    Noireaux, V.2
  • 26
    • 0030857501 scopus 로고    scopus 로고
    • Role of lipids in the permeabilization of membranes by class L amphipathic helical peptides
    • DOI 10.1021/bi970045l
    • Polozov, I. V., Polozova, A. I., Tytler, E. M., Anantharamaiah, G. M., Segrest, J. P., Woolley, G. A., and Epand, R. M. (1997) Role of lipids in the permeabilization of membranes by class L amphipathic helical peptides. Biochemistry 36, 9237-9245. (Pubitemid 27329509)
    • (1997) Biochemistry , vol.36 , Issue.30 , pp. 9237-9245
    • Polozov, I.V.1    Polozova, A.I.2    Tytler, E.M.3    Anantharamaiah, G.M.4    Segrest, J.P.5    Woolley, G.A.6    Epand, R.M.7
  • 27
    • 67649352970 scopus 로고    scopus 로고
    • Membrane fluidity and lipid order in ternary giant unilamellar vesicles using a new Bodipy-cholesterol derivative
    • Ariola, F. S., Li, Z., Cornejo, C., Bittman, R., and Heikal, A. A. (2009) Membrane fluidity and lipid order in ternary giant unilamellar vesicles using a new Bodipy-cholesterol derivative. Biophys. J. 96, 2696-2708.
    • (2009) Biophys. J. , vol.96 , pp. 2696-2708
    • Ariola, F.S.1    Li, Z.2    Cornejo, C.3    Bittman, R.4    Heikal, A.A.5
  • 28
    • 41049090929 scopus 로고    scopus 로고
    • Macromolecular crowding and confinement: Biochemical, biophysical, and potential physiological consequences
    • Zhou, H.-X., Rivas, G., and Minton, A. P. (2008) Macromolecular crowding and confinement: Biochemical, biophysical, and potential physiological consequences. Annu. Rev. Biophys. 37, 375-397.
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 375-397
    • Zhou, H.-X.1    Rivas, G.2    Minton, A.P.3
  • 29
    • 79960075043 scopus 로고    scopus 로고
    • Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B. subtilis
    • Garner, E. C., et al. (2011) Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B. subtilis. Science 333, 222-225.
    • (2011) Science , vol.333 , pp. 222-225
    • Garner, E.C.1
  • 30
    • 79960083390 scopus 로고    scopus 로고
    • Processive movement of MreB-associated cell wall biosynthetic complexes in bacteria
    • Domínguez-Escobar, J., et al. (2011) Processive movement of MreB-associated cell wall biosynthetic complexes in bacteria. Science 333, 225-228.
    • (2011) Science , vol.333 , pp. 225-228
    • Domínguez-Escobar, J.1
  • 32
    • 0024244368 scopus 로고
    • The T7 phage gene 10 leader RNA, a ribosome-binding site that dramatically enhances the expression of foreign genes in Escherichia coli
    • DOI 10.1016/0378-1119(88)90329-0
    • Olins, P. O., Devine, C. S., Rangwala, S. H., and Kavka, K. S. (1988) The T7 phage gene 10 leader RNA, a ribosome-binding site that dramatically enhances the expression of foreign genes in Escherichia coli. Gene 73, 227-235. (Pubitemid 19033799)
    • (1988) Gene , vol.73 , Issue.1 , pp. 227-235
    • Olins, P.O.1    Devine, C.S.2    Rangwala, S.H.3    Kavka, K.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.