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Volumn 87, Issue 5, 2013, Pages 1074-1087

Colocalization and interaction between elongasome and divisome during a preparative cell division phase in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; PENICILLIN BINDING PROTEIN 2; PENICILLIN BINDING PROTEIN 3; UNCLASSIFIED DRUG;

EID: 84874214695     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12150     Document Type: Article
Times cited : (87)

References (65)
  • 1
    • 34248364322 scopus 로고    scopus 로고
    • The tubulin homologue FtsZ contributes to cell elongation by guiding cell wall precursor synthesis in Caulobacter crescentus
    • Aaron, M., Charbon, G., Lam, H., Schwarz, H., Vollmer, W., and Jacobs-Wagner, C. (2007) The tubulin homologue FtsZ contributes to cell elongation by guiding cell wall precursor synthesis in Caulobacter crescentus. Mol Microbiol 64: 938-952.
    • (2007) Mol Microbiol , vol.64 , pp. 938-952
    • Aaron, M.1    Charbon, G.2    Lam, H.3    Schwarz, H.4    Vollmer, W.5    Jacobs-Wagner, C.6
  • 3
    • 77954376358 scopus 로고    scopus 로고
    • Direct interactions of early and late assembling division proteins in Escherichia coli cells resolved by FRET
    • Alexeeva, S., Gadella, T.W., Jr, Verheul, J., Verhoeven, G.S., and den Blaauwen, T. (2010) Direct interactions of early and late assembling division proteins in Escherichia coli cells resolved by FRET. Mol Microbiol 77: 384-398.
    • (2010) Mol Microbiol , vol.77 , pp. 384-398
    • Alexeeva, S.1    Gadella Jr., T.W.2    Verheul, J.3    den Verhoeven, G.S.4    Blaauwen, T.5
  • 5
    • 59649113418 scopus 로고    scopus 로고
    • RodZ (YfgA) is required for proper assembly of the MreB actin cytoskeleton and cell shape in E. coli
    • Bendezu, F.O., Hale, C.A., Bernhardt, T.G., and de Boer, P.A. (2009) RodZ (YfgA) is required for proper assembly of the MreB actin cytoskeleton and cell shape in E. coli. EMBO J 28: 193-204.
    • (2009) EMBO J , vol.28 , pp. 193-204
    • Bendezu, F.O.1    Hale, C.A.2    de Bernhardt, T.G.3    Boer, P.A.4
  • 6
    • 33748333182 scopus 로고    scopus 로고
    • Interaction between two murein (peptidoglycan) synthases, PBP3 and PBP1B, in Escherichia coli
    • Bertsche, U., Kast, T., Wolf, B., Fraipont, C., Aarsman, M.E., Kannenberg, K., etal. (2006) Interaction between two murein (peptidoglycan) synthases, PBP3 and PBP1B, in Escherichia coli. Mol Microbiol 61: 675-690.
    • (2006) Mol Microbiol , vol.61 , pp. 675-690
    • Bertsche, U.1    Kast, T.2    Wolf, B.3    Fraipont, C.4    Aarsman, M.E.5    Kannenberg, K.6
  • 7
    • 0026059127 scopus 로고
    • FtsZ ring structure associated with division in Escherichia coli
    • Bi, E.F., and Lutkenhaus, J. (1991) FtsZ ring structure associated with division in Escherichia coli. Nature 354: 161-164.
    • (1991) Nature , vol.354 , pp. 161-164
    • Bi, E.F.1    Lutkenhaus, J.2
  • 9
    • 0037244586 scopus 로고    scopus 로고
    • Penicillin-binding protein PBP2 of Escherichia coli localizes preferentially in the lateral wall and at mid-cell in comparison with the old cell pole
    • den Blaauwen, T., Aarsman, M.E., Vischer, N.O., and Nanninga, N. (2003) Penicillin-binding protein PBP2 of Escherichia coli localizes preferentially in the lateral wall and at mid-cell in comparison with the old cell pole. Mol Microbiol 47: 539-547.
    • (2003) Mol Microbiol , vol.47 , pp. 539-547
    • den Blaauwen, T.1    Aarsman, M.E.2    Vischer, N.O.3    Nanninga, N.4
  • 11
    • 84861204197 scopus 로고    scopus 로고
    • The early divisome protein FtsA interacts directly through its 1c subdomain with the cytoplasmic domain of the late divisome protein FtsN
    • Busiek, K.K., Eraso, J.M., Wang, Y., and Margolin, W. (2012) The early divisome protein FtsA interacts directly through its 1c subdomain with the cytoplasmic domain of the late divisome protein FtsN. J Bacteriol 194: 1989-2000.
    • (2012) J Bacteriol , vol.194 , pp. 1989-2000
    • Busiek, K.K.1    Eraso, J.M.2    Wang, Y.3    Margolin, W.4
  • 12
    • 0026687952 scopus 로고
    • Fluorescence resonance energy transfer and nucleic acids
    • Clegg, R.M. (1992) Fluorescence resonance energy transfer and nucleic acids. Methods Enzymol 211: 353-388.
    • (1992) Methods Enzymol , vol.211 , pp. 353-388
    • Clegg, R.M.1
  • 13
    • 0026639433 scopus 로고
    • Fluorescence resonance energy transfer analysis of the structure of the four-way DNA junction
    • Clegg, R.M., Murchie, A.I., Zechel, A., Carlberg, C., Diekmann, S., and Lilley, D.M. (1992) Fluorescence resonance energy transfer analysis of the structure of the four-way DNA junction. Biochemistry 31: 4846-4856.
    • (1992) Biochemistry , vol.31 , pp. 4846-4856
    • Clegg, R.M.1    Murchie, A.I.2    Zechel, A.3    Carlberg, C.4    Diekmann, S.5    Lilley, D.M.6
  • 14
    • 0346252349 scopus 로고    scopus 로고
    • Use of a two-hybrid assay to study the assembly of a complex multicomponent protein machinery: bacterial septosome differentiation
    • Di Lallo, G., Fagioli, M., Barionovi, D., Ghelardini, P., and Paolozzi, L. (2003) Use of a two-hybrid assay to study the assembly of a complex multicomponent protein machinery: bacterial septosome differentiation. Microbiology 149: 3353-3359.
    • (2003) Microbiology , vol.149 , pp. 3353-3359
    • Di Lallo, G.1    Fagioli, M.2    Barionovi, D.3    Ghelardini, P.4    Paolozzi, L.5
  • 16
    • 0029956443 scopus 로고    scopus 로고
    • Direct quantitation of the number of individual penicillin-binding proteins per cell in Escherichia coli
    • Dougherty, T.J., Kennedy, K., Kessler, R.E., and Pucci, M.J. (1996) Direct quantitation of the number of individual penicillin-binding proteins per cell in Escherichia coli. J Bacteriol 178: 6110-6115.
    • (1996) J Bacteriol , vol.178 , pp. 6110-6115
    • Dougherty, T.J.1    Kennedy, K.2    Kessler, R.E.3    Pucci, M.J.4
  • 18
    • 77958525927 scopus 로고    scopus 로고
    • In vivo structure of the E. coli FtsZ-ring revealed by photoactivated localization microscopy (PALM)
    • Fu, G., Huang, T., Buss, J., Coltharp, C., Hensel, Z., and Xiao, J. (2010) In vivo structure of the E. coli FtsZ-ring revealed by photoactivated localization microscopy (PALM). PLoS ONE 5: e12682.
    • (2010) PLoS ONE , vol.5
    • Fu, G.1    Huang, T.2    Buss, J.3    Coltharp, C.4    Hensel, Z.5    Xiao, J.6
  • 19
    • 70349358349 scopus 로고    scopus 로고
    • Gadella, T.W.J. (ed.) Pillai, S., and van der Vliet, P.C. (eds). Amsterdam: Elsevier Science & Technology.
    • Gadella, T.W.J. (ed.) (2008) FRET and FLIM Techniques. Pillai, S., and van der Vliet, P.C. (eds). Amsterdam: Elsevier Science & Technology.
    • (2008) FRET and FLIM Techniques
  • 20
    • 79960075043 scopus 로고    scopus 로고
    • Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B. subtilis
    • Garner, E.C., Bernard, R., Wang, W., Zhuang, X., Rudner, D.Z., and Mitchison, T. (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    Bernard, R.2    Wang, W.3    Zhuang, X.4    Rudner, D.Z.5    Mitchison, T.6
  • 21
    • 21844441637 scopus 로고    scopus 로고
    • Diverse paths to midcell: assembly of the bacterial cell division machinery
    • Goehring, N.W., and Beckwith, J. (2005) Diverse paths to midcell: assembly of the bacterial cell division machinery. Curr Biol 15: R514-R526.
    • (2005) Curr Biol , vol.15
    • Goehring, N.W.1    Beckwith, J.2
  • 22
    • 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
  • 23
    • 84864010982 scopus 로고    scopus 로고
    • Osmolality-dependent relocation of penicillin-binding protein PBP2 to the division site in Caulobacter crescentus
    • Hocking, J., Priyadarshini, R., Takacs, C.N., Costa, T., Dye, N.A., Shapiro, L., etal. (2012) Osmolality-dependent relocation of penicillin-binding protein PBP2 to the division site in Caulobacter crescentus. J Bacteriol 194: 3116-3127.
    • (2012) J Bacteriol , vol.194 , pp. 3116-3127
    • Hocking, J.1    Priyadarshini, R.2    Takacs, C.N.3    Costa, T.4    Dye, N.A.5    Shapiro, L.6
  • 24
    • 80052479510 scopus 로고    scopus 로고
    • Mechanical control of bacterial cell shape
    • Jiang, H., Si, F., Margolin, W., and Sun, S.X. (2011) Mechanical control of bacterial cell shape. Biophys J 101: 327-335.
    • (2011) Biophys J , vol.101 , pp. 327-335
    • Jiang, H.1    Si, F.2    Margolin, W.3    Sun, S.X.4
  • 25
    • 0035937396 scopus 로고    scopus 로고
    • Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis
    • Jones, L.J., Carballido-Lopez, R., and Errington, J. (2001) Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis. Cell 104: 913-922.
    • (2001) Cell , vol.104 , pp. 913-922
    • Jones, L.J.1    Carballido-Lopez, R.2    Errington, J.3
  • 26
    • 3142736368 scopus 로고    scopus 로고
    • Cyan-emitting and orange-emitting fluorescent proteins as a donor/acceptor pair for fluorescence resonance energy transfer
    • Karasawa, S., Araki, T., Nagai, T., Mizuno, H., and Miyawaki, A. (2004) Cyan-emitting and orange-emitting fluorescent proteins as a donor/acceptor pair for fluorescence resonance energy transfer. Biochem J 381: 307-312.
    • (2004) Biochem J , vol.381 , pp. 307-312
    • Karasawa, S.1    Araki, T.2    Nagai, T.3    Mizuno, H.4    Miyawaki, A.5
  • 27
    • 34250627500 scopus 로고    scopus 로고
    • DNA and origin region segregation are not affected by the transition from rod to sphere after inhibition of Escherichia coli MreB by A22
    • Karczmarek, A., Martinez-Arteaga, R., Alexeeva, S., Hansen, F.G., Vicente, M., Nanninga, N., and den Blaauwen, T. (2007) DNA and origin region segregation are not affected by the transition from rod to sphere after inhibition of Escherichia coli MreB by A22. Mol Microbiol 65: 51-63.
    • (2007) Mol Microbiol , vol.65 , pp. 51-63
    • Karczmarek, A.1    Martinez-Arteaga, R.2    Alexeeva, S.3    Hansen, F.G.4    Vicente, M.5    den Nanninga, N.6    Blaauwen, T.7
  • 28
    • 1242275409 scopus 로고    scopus 로고
    • R174 of Escherichia coli FtsZ is involved in membrane interaction and protofilament bundling, and is essential for cell division
    • Koppelman, C.M., Aarsman, M.E., Postmus, J., Pas, E., Muijsers, A.O., Scheffers, D.J., etal. (2004) R174 of Escherichia coli FtsZ is involved in membrane interaction and protofilament bundling, and is essential for cell division. Mol Microbiol 51: 645-657.
    • (2004) Mol Microbiol , vol.51 , pp. 645-657
    • Koppelman, C.M.1    Aarsman, M.E.2    Postmus, J.3    Pas, E.4    Muijsers, A.O.5    Scheffers, D.J.6
  • 29
    • 12344306119 scopus 로고    scopus 로고
    • The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex
    • 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.
    • (2005) Mol Microbiol , vol.55 , pp. 78-89
    • Kruse, T.1    Bork-Jensen, J.2    Gerdes, K.3
  • 30
    • 25144451503 scopus 로고    scopus 로고
    • The rcs phosphorelay: a complex signal transduction system
    • Majdalani, N., and Gottesman, S. (2005) The rcs phosphorelay: a complex signal transduction system. Annu Rev Microbiol 59: 379-405.
    • (2005) Annu Rev Microbiol , vol.59 , pp. 379-405
    • Majdalani, N.1    Gottesman, S.2
  • 31
    • 0036155122 scopus 로고    scopus 로고
    • The Escherichia coli cell division protein FtsW is required to recruit its cognate transpeptidase, FtsI (PBP3), to the division site
    • Mercer, K.L., and Weiss, D.S. (2002) The Escherichia coli cell division protein FtsW is required to recruit its cognate transpeptidase, FtsI (PBP3), to the division site. J Bacteriol 184: 904-912.
    • (2002) J Bacteriol , vol.184 , pp. 904-912
    • Mercer, K.L.1    Weiss, D.S.2
  • 32
    • 34547651288 scopus 로고    scopus 로고
    • The essential peptidoglycan glycosyltransferase MurG forms a complex with proteins involved in lateral envelope growth as well as with proteins involved in cell division in Escherichia coli
    • Mohammadi, T., Karczmarek, A., Crouvoisier, M., Bouhss, A., Mengin-Lecreulx, D., and den Blaauwen, T. (2007) The essential peptidoglycan glycosyltransferase MurG forms a complex with proteins involved in lateral envelope growth as well as with proteins involved in cell division in Escherichia coli. Mol Microbiol 65: 1106-1121.
    • (2007) Mol Microbiol , vol.65 , pp. 1106-1121
    • Mohammadi, T.1    Karczmarek, A.2    Crouvoisier, M.3    Bouhss, A.4    den Mengin-Lecreulx, D.5    Blaauwen, T.6
  • 33
    • 79955007775 scopus 로고    scopus 로고
    • Identification of FtsW as a transporter of lipid-linked cell wall precursors across the membrane
    • Mohammadi, T., van Dam, V., Sijbrandi, R., Vernet, T., Zapun, A., Bouhss, A., etal. (2011) Identification of FtsW as a transporter of lipid-linked cell wall precursors across the membrane. EMBO J 30: 1425-1432.
    • (2011) EMBO J , vol.30 , pp. 1425-1432
    • Mohammadi, T.1    van Dam, V.2    Sijbrandi, R.3    Vernet, T.4    Zapun, A.5    Bouhss, A.6
  • 34
    • 79955031537 scopus 로고    scopus 로고
    • A novel in vivo cell-wall labeling approach sheds new light on peptidoglycan synthesis in Escherichia coli
    • Olrichs, N.K., Aarsman, M.E., Verheul, J., Arnusch, C.J., Martin, N.I., Herve, M., etal. (2011) A novel in vivo cell-wall labeling approach sheds new light on peptidoglycan synthesis in Escherichia coli. Chembiochem 12: 1124-1133.
    • (2011) Chembiochem , vol.12 , pp. 1124-1133
    • Olrichs, N.K.1    Aarsman, M.E.2    Verheul, J.3    Arnusch, C.J.4    Martin, N.I.5    Herve, M.6
  • 36
    • 78650497005 scopus 로고    scopus 로고
    • Lipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases
    • Paradis-Bleau, C., Markovski, M., Uehara, T., Lupoli, T.J., Walker, S., Kahne, D.E., and Bernhardt, T.G. (2010) Lipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases. Cell 143: 1110-1120.
    • (2010) Cell , vol.143 , pp. 1110-1120
    • Paradis-Bleau, C.1    Markovski, M.2    Uehara, T.3    Lupoli, T.J.4    Walker, S.5    Kahne, D.E.6    Bernhardt, T.G.7
  • 38
    • 0020178780 scopus 로고
    • Consensus values and weighting factors
    • Paule, R., and Mandel, J. (1982) Consensus values and weighting factors. J Res Natl Bur Stand 87: 377-385.
    • (1982) J Res Natl Bur Stand , vol.87 , pp. 377-385
    • Paule, R.1    Mandel, J.2
  • 40
    • 4444297890 scopus 로고    scopus 로고
    • Structural determinants required to target penicillin-binding protein 3 to the septum of Escherichia coli
    • Piette, A., Fraipont, C., den Blaauwen, T., Aarsman, M.E., Pastoret, S., and Nguyen-Disteche, M. (2004) Structural determinants required to target penicillin-binding protein 3 to the septum of Escherichia coli. J Bacteriol 186: 6110-6117.
    • (2004) J Bacteriol , vol.186 , pp. 6110-6117
    • Piette, A.1    den Fraipont, C.2    Blaauwen, T.3    Aarsman, M.E.4    Pastoret, S.5    Nguyen-Disteche, M.6
  • 41
    • 77954375639 scopus 로고    scopus 로고
    • Septal and lateral wall localization of PBP5, the major d,d-carboxypeptidase of Escherichia coli, requires substrate recognition and membrane attachment
    • Potluri, L., Karczmarek, A., Verheul, J., Piette, A., Wilkin, J.M., Werth, N., etal. (2010) Septal and lateral wall localization of PBP5, the major d, d-carboxypeptidase of Escherichia coli, requires substrate recognition and membrane attachment. Mol Microbiol 77: 300-323.
    • (2010) Mol Microbiol , vol.77 , pp. 300-323
    • Potluri, L.1    Karczmarek, A.2    Verheul, J.3    Piette, A.4    Wilkin, J.M.5    Werth, N.6
  • 42
    • 84868326175 scopus 로고    scopus 로고
    • ZipA is required for FtsZ-dependent preseptal peptidoglycan synthesis prior to invagination during cell division
    • Potluri, L., Kannan, S., and Young, K.D. (2012) ZipA is required for FtsZ-dependent preseptal peptidoglycan synthesis prior to invagination during cell division. J Bacteriol 194: 5334-5342.
    • (2012) J Bacteriol , vol.194 , pp. 5334-5342
    • Potluri, L.1    Kannan, S.2    Young, K.D.3
  • 43
    • 58149234369 scopus 로고    scopus 로고
    • Timing the start of division in E. coli: a single-cell study
    • Reshes, G., Vanounou, S., Fishov, I., and Feingold, M. (2008) Timing the start of division in E. coli: a single-cell study. Phys Biol 5: 046001-046009.
    • (2008) Phys Biol , vol.5 , pp. 046001-046009
    • Reshes, G.1    Vanounou, S.2    Fishov, I.3    Feingold, M.4
  • 44
    • 79960913936 scopus 로고    scopus 로고
    • Direct membrane binding by bacterial actin MreB
    • Salje, J., van den Ent, F., de Boer, P., and Lowe, J. (2011) Direct membrane binding by bacterial actin MreB. Mol Cell 43: 478-487.
    • (2011) Mol Cell , vol.43 , pp. 478-487
    • Salje, J.1    van den Ent, F.2    de Boer, P.3    Lowe, J.4
  • 45
    • 39149088656 scopus 로고    scopus 로고
    • The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis
    • Sauvage, E., Kerff, F., Terrak, M., Ayala, J.A., and Charlier, P. (2008) The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis. FEMS Microbiol Rev 32: 234-258.
    • (2008) FEMS Microbiol Rev , vol.32 , pp. 234-258
    • Sauvage, E.1    Kerff, F.2    Terrak, M.3    Ayala, J.A.4    Charlier, P.5
  • 46
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from discosoma sp. red fluorescent protein
    • Shaner, N.C., Campbell, R.E., Steinbach, P.A., Giepmans, B.N., Palmer, A.E., and Tsien, R.Y. (2004) Improved monomeric red, orange and yellow fluorescent proteins derived from discosoma sp. red fluorescent protein. Nat Biotechnol 22: 1567-1572.
    • (2004) Nat Biotechnol , vol.22 , pp. 1567-1572
    • Shaner, N.C.1    Campbell, R.E.2    Steinbach, P.A.3    Giepmans, B.N.4    Palmer, A.E.5    Tsien, R.Y.6
  • 47
    • 0013096299 scopus 로고
    • Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12
    • Spratt, B.G. (1975) Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12. Proc Natl Acad Sci USA 72: 2999-3003.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 2999-3003
    • Spratt, B.G.1
  • 48
    • 84871055385 scopus 로고    scopus 로고
    • The helical MreB cytoskeleton in E. coli MC1000/ pLE7 is an artifact of the N-terminal YFP tag
    • doi:10.1128/JB.00505-12.
    • Swulius, M.T., and Jensen, G.J. (2012) The helical MreB cytoskeleton in E. coli MC1000/ pLE7 is an artifact of the N-terminal YFP tag. J Bacteriol 194: 6382-6386 doi:10.1128/JB.00505-12.
    • (2012) J Bacteriol , vol.194 , pp. 6382-6386
    • Swulius, M.T.1    Jensen, G.J.2
  • 51
    • 84855889658 scopus 로고    scopus 로고
    • From the regulation of peptidoglycan synthesis to bacterial growth and morphology
    • Typas, A., Banzhaf, M., Gross, C.A., and Vollmer, W. (2011) From the regulation of peptidoglycan synthesis to bacterial growth and morphology. Nat Rev Microbiol 10: 123-136.
    • (2011) Nat Rev Microbiol , vol.10 , pp. 123-136
    • Typas, A.1    Banzhaf, M.2    Gross, C.A.3    Vollmer, W.4
  • 52
    • 66149136478 scopus 로고    scopus 로고
    • In Escherichia coli, MreB and FtsZ direct the synthesis of lateral cell wall via independent pathways that require PBP 2
    • Varma, A., and Young, K.D. (2009) In Escherichia coli, MreB and FtsZ direct the synthesis of lateral cell wall via independent pathways that require PBP 2. J Bacteriol 191: 3526-3533.
    • (2009) J Bacteriol , vol.191 , pp. 3526-3533
    • Varma, A.1    Young, K.D.2
  • 53
    • 34547618469 scopus 로고    scopus 로고
    • FtsZ directs a second mode of peptidoglycan synthesis in Escherichia coli
    • Varma, A., de Pedro, M.A., and Young, K.D. (2007) FtsZ directs a second mode of peptidoglycan synthesis in Escherichia coli. J Bacteriol 189: 5692-5704.
    • (2007) J Bacteriol , vol.189 , pp. 5692-5704
    • Varma, A.1    de Pedro, M.A.2    Young, K.D.3
  • 54
    • 36749016781 scopus 로고    scopus 로고
    • Duplication and segregation of the actin (MreB) cytoskeleton during the prokaryotic cell cycle
    • Vats, P., and Rothfield, L. (2007) Duplication and segregation of the actin (MreB) cytoskeleton during the prokaryotic cell cycle. Proc Natl Acad Sci USA 104: 17795-17800.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 17795-17800
    • Vats, P.1    Rothfield, L.2
  • 55
    • 62949149564 scopus 로고    scopus 로고
    • Assembly of the MreB-associated cytoskeletal ring of Escherichia coli
    • Vats, P., Shih, Y.L., and Rothfield, L. (2009) Assembly of the MreB-associated cytoskeletal ring of Escherichia coli. Mol Microbiol 72: 170-182.
    • (2009) Mol Microbiol , vol.72 , pp. 170-182
    • Vats, P.1    Shih, Y.L.2    Rothfield, L.3
  • 56
    • 0027363663 scopus 로고
    • Penicillin-binding protein 2 inactivation in Escherichia coli results in cell division inhibition, which is relieved by FtsZ overexpression
    • Vinella, D., Joseleau-Petit, D., Thévenet, D., Bouloc, P., and D'Ari, R. (1993) Penicillin-binding protein 2 inactivation in Escherichia coli results in cell division inhibition, which is relieved by FtsZ overexpression. J Bacteriol 175: 6704-6710.
    • (1993) J Bacteriol , vol.175 , pp. 6704-6710
    • Vinella, D.1    Joseleau-Petit, D.2    Thévenet, D.3    Bouloc, P.4    D'Ari, R.5
  • 57
    • 50049104157 scopus 로고    scopus 로고
    • Murein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli
    • Vollmer, W., and Bertsche, U. (2008) Murein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli. Biochim Biophys Acta 1778: 1714-1734.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 1714-1734
    • Vollmer, W.1    Bertsche, U.2
  • 58
    • 0023638691 scopus 로고
    • Mutant isolation and molecular cloning of mre genes, which determine cell shape, sensitivity to mecillinam, and amount of penicillin-binding proteins in Escherichia coli
    • Wachi, M., Doi, M., Tamaki, S., Park, W., Nakajima-Iijima, S., and Matsuhashi, M. (1987) Mutant isolation and molecular cloning of mre genes, which determine cell shape, sensitivity to mecillinam, and amount of penicillin-binding proteins in Escherichia coli. J Bacteriol 169: 4935-4940.
    • (1987) J Bacteriol , vol.169 , pp. 4935-4940
    • Wachi, M.1    Doi, M.2    Tamaki, S.3    Park, W.4    Nakajima-Iijima, S.5    Matsuhashi, M.6
  • 59
    • 84863229704 scopus 로고    scopus 로고
    • Helical insertion of peptidoglycan produces chiral ordering of the bacterial cell wall
    • Wang, S., Furchtgott, L., Huang, K.C., and Shaevitz, J.W. (2012) Helical insertion of peptidoglycan produces chiral ordering of the bacterial cell wall. Proc Natl Acad Sci USA 109: E595-E604.
    • (2012) Proc Natl Acad Sci USA , vol.109
    • Wang, S.1    Furchtgott, L.2    Huang, K.C.3    Shaevitz, J.W.4
  • 60
    • 0030931117 scopus 로고    scopus 로고
    • Analysis of the interaction of FtsZ with itself, GTP, and FtsA
    • Wang, X., Huang, J., Mukherjee, A., Cao, C., and Lutkenhaus, J. (1997) Analysis of the interaction of FtsZ with itself, GTP, and FtsA. J Bacteriol 179: 5551-5559.
    • (1997) J Bacteriol , vol.179 , pp. 5551-5559
    • Wang, X.1    Huang, J.2    Mukherjee, A.3    Cao, C.4    Lutkenhaus, J.5
  • 61
    • 0032932435 scopus 로고    scopus 로고
    • Localization of FtsI (PBP3) to the septal ring requires its membrane anchor, the Z ring, FtsA, FtsQ, and FtsL
    • Weiss, D.S., Chen, J.C., Ghigo, J.M., Boyd, D., and Beckwith, J. (1999) Localization of FtsI (PBP3) to the septal ring requires its membrane anchor, the Z ring, FtsA, FtsQ, and FtsL. J Bacteriol 181: 508-520.
    • (1999) J Bacteriol , vol.181 , pp. 508-520
    • Weiss, D.S.1    Chen, J.C.2    Ghigo, J.M.3    Boyd, D.4    Beckwith, J.5
  • 62
    • 84870267223 scopus 로고
    • The generalisation of student's problems when several different population variances are involved
    • Welch, B.L. (1947) The generalisation of student's problems when several different population variances are involved. Biometrika 34: 28-35.
    • (1947) Biometrika , vol.34 , pp. 28-35
    • Welch, B.L.1
  • 63
    • 77951608842 scopus 로고    scopus 로고
    • Positioning cell wall synthetic complexes by the bacterial morphogenetic proteins MreB and MreD
    • White, C.L., Kitich, A., and Gober, J.W. (2010) Positioning cell wall synthetic complexes by the bacterial morphogenetic proteins MreB and MreD. Mol Microbiol 76: 616-633.
    • (2010) Mol Microbiol , vol.76 , pp. 616-633
    • White, C.L.1    Kitich, A.2    Gober, J.W.3
  • 64
    • 0024381715 scopus 로고
    • Rate and topography of peptidoglycan synthesis during cell division in Escherichia coli: concept of a leading edge
    • Wientjes, F.B., and Nanninga, N. (1989) Rate and topography of peptidoglycan synthesis during cell division in Escherichia coli: concept of a leading edge. J Bacteriol 171: 3412-3419.
    • (1989) J Bacteriol , vol.171 , pp. 3412-3419
    • Wientjes, F.B.1    Nanninga, N.2
  • 65
    • 11144318755 scopus 로고    scopus 로고
    • The transmembrane helix of the Escherichia coli division protein FtsI localizes to the septal ring
    • Wissel, M.C., Wendt, J.L., Mitchell, C.J., and Weiss, D.S. (2005) The transmembrane helix of the Escherichia coli division protein FtsI localizes to the septal ring. J Bacteriol 187: 320-328.
    • (2005) J Bacteriol , vol.187 , pp. 320-328
    • Wissel, M.C.1    Wendt, J.L.2    Mitchell, C.J.3    Weiss, D.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.