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Volumn 32, Issue 13, 2013, Pages 1953-1965

Direct interaction of FtsZ and MreB is required for septum synthesis and cell division in Escherichia coli

Author keywords

Cell division; Cell elongation; Ftsz; Mreb; septum

Indexed keywords

FTSZ PROTEIN; MREB PROTEIN; PEPTIDOGLYCAN;

EID: 84880238403     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2013.129     Document Type: Article
Times cited : (111)

References (64)
  • 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, 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
    • 0030856502 scopus 로고    scopus 로고
    • FtsN, a late recruit to the septum in Escherichia coli
    • Addinall SG, Cao C, Lutkenhaus J (1997) FtsN, a late recruit to the septum in Escherichia coli. Mol Microbiol 25: 303-309
    • (1997) Mol Microbiol , vol.25 , pp. 303-309
    • Addinall, S.G.1    Cao, C.2    Lutkenhaus, J.3
  • 5
    • 33846286901 scopus 로고    scopus 로고
    • Shaping the actin cytoskeleton using microtubule tips
    • Basu R, Chang F (2007) Shaping the actin cytoskeleton using microtubule tips. Curr Opin Cell Biol 19: 88-94
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 88-94
    • Basu, R.1    Chang, F.2
  • 6
    • 39749142159 scopus 로고    scopus 로고
    • Conditional lethality, division defects, membrane involution, and endocytosis in mre and mrd shape mutants of Escherichia coli
    • Bendezu FO, De Boer PAJ (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
    • Bendezu, F.O.1    De Boer Paj2
  • 7
    • 59649113418 scopus 로고    scopus 로고
    • RodZ (YfgA) is required for proper assembly of the MreB actin cytoskeleton and cell shape in E. coli
    • Bendezu FO, Hale CA, Bernhardt TG, De Boer PAJ (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    Bernhardt, T.G.3    De Boer, P.A.J.4
  • 9
    • 0026059127 scopus 로고
    • FtsZ ring structure associated with division in Escherichia coli
    • Bi E, 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.1    Lutkenhaus, J.2
  • 10
    • 16544365268 scopus 로고    scopus 로고
    • Low-fidelity Pyrococcus furiosus DNA polymerase mutants useful in error-prone PCR
    • Biles BD, Connolly BA (2004) Low-fidelity Pyrococcus furiosus DNA polymerase mutants useful in error-prone PCR. Nucleic Acids Res 32: e176
    • (2004) Nucleic Acids Res , vol.32
    • Biles, B.D.1    Connolly, B.A.2
  • 11
    • 0026687729 scopus 로고
    • An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins
    • Bork P, Sander C, Valencia A (1992) An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins. PNAS 89: 7290-7294
    • (1992) PNAS , vol.89 , pp. 7290-7294
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 13
    • 7744230898 scopus 로고    scopus 로고
    • Z-Ring-independent interaction between a subdomain of FtsA and late septation proteins as revealed by a polar recruitment assay
    • Corbin BD, Geissler B, Sadasivam M, Margolin W (2004) Z-Ring-independent interaction between a subdomain of FtsA and late septation proteins as revealed by a polar recruitment assay. J Bacteriol 186: 7736-7744
    • (2004) J Bacteriol , vol.186 , pp. 7736-7744
    • Corbin, B.D.1    Geissler, B.2    Sadasivam, M.3    Margolin, W.4
  • 14
    • 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 MEG, Vischer NOE, 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    Meg, A.2    Noe, V.3    Nanninga, N.4
  • 15
    • 78649646536 scopus 로고    scopus 로고
    • Advances in understanding E. coli cell fission
    • De Boer PAJ (2010) Advances in understanding E. coli cell fission. Curr Opin Microbiol 13: 730-737
    • (2010) Curr Opin Microbiol , vol.13 , pp. 730-737
    • De Boer, P.A.J.1
  • 16
    • 0026705484 scopus 로고
    • The essential bacterial cell-division protein FtsZ is a GTPase
    • De Boer P, Crossley R, Rothfield L (1992) The essential bacterial cell-division protein FtsZ is a GTPase. Nature 359: 254-256
    • (1992) Nature , vol.359 , pp. 254-256
    • De Boer, P.1    Crossley, R.2    Rothfield, L.3
  • 18
    • 29344476196 scopus 로고    scopus 로고
    • The cell-shape protein MreC interacts with extracytoplasmic proteins including cell wall assembly complexes in Caulobacter crescentus
    • Divakaruni AV, Ogorzalek Loo RR, Xie Y, Loo JA, Gober JW (2005) The cell-shape protein MreC interacts with extracytoplasmic proteins including cell wall assembly complexes in Caulobacter crescentus. PNAS 102: 18602-18607
    • (2005) PNAS , vol.102 , pp. 18602-18607
    • Divakaruni, A.V.1    Ogorzalek Loo, R.R.2    Xie, Y.3    Loo, J.A.4    Gober, J.W.5
  • 20
    • 34447318642 scopus 로고    scopus 로고
    • Evolution of the cytoskeleton
    • Erickson HP (2007) Evolution of the cytoskeleton. BioEssays 29: 668-677
    • (2007) BioEssays , vol.29 , pp. 668-677
    • Erickson, H.P.1
  • 21
    • 77749288955 scopus 로고    scopus 로고
    • Manipulating each MreB of Bdellovibrio bacteriovorus gives diverse morphological and predatory phenotypes
    • Fenton AK, Lambert C,Wagstaff PC, Sockett RE (2010) Manipulating each MreB of Bdellovibrio bacteriovorus gives diverse morphological and predatory phenotypes. J Bacteriol 192: 1299-1311
    • (2010) J Bacteriol , vol.192 , pp. 1299-1311
    • Fenton, A.K.1    Lambert, C.2    Wagstaff, P.C.3    Sockett, R.E.4
  • 22
    • 1542616355 scopus 로고    scopus 로고
    • MreB, the cell shape-determining bacterial actin homologue, co-ordinates cell wall morphogenesis in Caulobacter crescentus
    • Figge RM, Divakaruni AV, Gober JW (2004) MreB, the cell shape-determining bacterial actin homologue, co-ordinates cell wall morphogenesis in Caulobacter crescentus. Mol Microbiol 51: 1321-1332
    • (2004) Mol Microbiol , vol.51 , pp. 1321-1332
    • Figge, R.M.1    Divakaruni, A.V.2    Gober, J.W.3
  • 23
    • 75749107907 scopus 로고    scopus 로고
    • Cell mechanics and the cytoskeleton
    • Fletcher DA, Mullins RD (2010) Cell mechanics and the cytoskeleton. Nature 463: 485-492
    • (2010) Nature , vol.463 , pp. 485-492
    • Fletcher, D.A.1    Mullins, R.D.2
  • 24
    • 84855881444 scopus 로고    scopus 로고
    • FtsZ-ZapA-ZapB interactome of Escherichia coli
    • Galli E, Gerdes K (2012) FtsZ-ZapA-ZapB interactome of Escherichia coli. J Bacteriol 194: 292-302
    • (2012) J Bacteriol , vol.194 , pp. 292-302
    • Galli, E.1    Gerdes, K.2
  • 25
    • 79960075043 scopus 로고    scopus 로고
    • Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B. subtilis
    • Garner EC, Bernard R, Wang W, Zhuang X, Rudner DZ, 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
  • 26
    • 0027176669 scopus 로고
    • Transcription of ftsZ oscillates during the cell cycle of Esherichia coli
    • Garrido T, Scnchez M, Palacios P, Aldea M, Vicente M (1993) Transcription of ftsZ oscillates during the cell cycle of Esherichia coli. EMBO J 12: 3957-3965
    • (1993) EMBO J , vol.12 , pp. 3957-3965
    • Garrido, T.1    Scnchez, M.2    Palacios, P.3    Aldea, M.4    Vicente, M.5
  • 27
    • 72449160318 scopus 로고    scopus 로고
    • Self-enhanced accumulation of FtsN at division sites and roles for other proteins with a SPOR domain (DamX, DedD, and RlpA) in Escherichia coli cell constriction
    • Gerding Ma, Liu B, Bendezu FO, Hale CA, Bernhardt TG, De Boer PAJ (2009) Self-enhanced accumulation of FtsN at division sites and roles for other proteins with a SPOR domain (DamX, DedD, and RlpA) in Escherichia coli cell constriction. J Bacteriol 191: 7383-7401
    • (2009) J Bacteriol , vol.191 , pp. 7383-7401
    • Gerding, M.1    Liu, B.2    Bendezu, F.O.3    Hale, C.A.4    Bernhardt, T.G.5    De Boer Paj6
  • 29
    • 33744479995 scopus 로고    scopus 로고
    • A new FtsZ-interacting protein, YlmF, complements the activity of FtsA during progression of cell division in Bacillus subtilis
    • Ishikawa S, Kawai Y, Hiramatsu K, Kuwano M, Ogasawara N (2006) A new FtsZ-interacting protein, YlmF, complements the activity of FtsA during progression of cell division in Bacillus subtilis. Mol Microbiol 60: 1364-1380
    • (2006) Mol Microbiol , vol.60 , pp. 1364-1380
    • Ishikawa, S.1    Kawai, Y.2    Hiramatsu, K.3    Kuwano, M.4    Ogasawara, N.5
  • 30
    • 0035937396 scopus 로고    scopus 로고
    • Control of cell shape in bacteria: Helical, actin-like filaments in Bacillus subtilis
    • Jones LJ, Carballido-Lopez R, 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
  • 32
    • 15244361175 scopus 로고    scopus 로고
    • Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis
    • Karimova G, Dautin N, Ladant D (2005) Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis. J Bacteriol 187: 2233-2243
    • (2005) J Bacteriol , vol.187 , pp. 2233-2243
    • Karimova, G.1    Dautin, N.2    Ladant, D.3
  • 33
    • 12344306119 scopus 로고    scopus 로고
    • The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex
    • Kruse T, Bork-Jensen J, 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
  • 34
    • 0141864658 scopus 로고    scopus 로고
    • Dysfunctional MreB inhibits chromosome segregation in Escherichia coli
    • Kruse T, Mller-Jensen J, Lbner-Olesen A, Gerdes K (2003) Dysfunctional MreB inhibits chromosome segregation in Escherichia coli. EMBO J 22: 5283-5292
    • (2003) EMBO J , vol.22 , pp. 5283-5292
    • Kruse, T.1    Mller-Jensen, J.2    Lbner-Olesen, A.3    Gerdes, K.4
  • 36
    • 72449131554 scopus 로고    scopus 로고
    • FtsN-trigger for septation
    • Lutkenhaus J (2009) FtsN-trigger for septation. J Bacteriol 191: 7381-7382
    • (2009) J Bacteriol , vol.191 , pp. 7381-7382
    • Lutkenhaus, J.1
  • 37
    • 0018972825 scopus 로고
    • FtsA-envA region of the and identification of a new fts organization of genes in the ftsA-envA region of the Escherichia coli genetic map and identification of a new fts locus (ftsZ)
    • Lutkenhaus JF,Wolf-Watz H, Donachie WD (1980) ftsA-envA region of the and identification of a new fts organization of genes in the ftsA-envA region of the Escherichia coli genetic map and identification of a new fts locus (ftsZ). J Bacteriol 142: 615-620
    • (1980) J Bacteriol , vol.142 , pp. 615-620
    • Lutkenhaus, J.F.1    Wolf-Watz, H.2    Donachie, W.D.3
  • 38
    • 0032786248 scopus 로고    scopus 로고
    • Genetic and functional analyses of the conserved C-Terminal core domain of Escherichia coli FtsZ
    • Ma X, Margolin W (1999) Genetic and functional analyses of the conserved C-Terminal core domain of Escherichia coli FtsZ. J Bacteriol 181: 7531-7544
    • (1999) J Bacteriol , vol.181 , pp. 7531-7544
    • Ma, X.1    Margolin, W.2
  • 40
    • 33746358181 scopus 로고    scopus 로고
    • Dynamic filaments of the bacterial cytoskeleton
    • Michie KA, Lowe J (2006) Dynamic filaments of the bacterial cytoskeleton. Ann Rev Biochem 75: 467-492
    • (2006) Ann Rev Biochem , vol.75 , pp. 467-492
    • Michie, K.A.1    Lowe, J.2
  • 42
    • 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, 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    Mengin-Lecreulx, D.5    Den Blaauwen, T.6
  • 44
    • 13444274140 scopus 로고    scopus 로고
    • Structural insights into FtsZ protofilament formation
    • Oliva MA, Cordell SC, Lowe J (2004) Structural insights into FtsZ protofilament formation. Nat Struct Mol Biol 11: 1243-1250
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 1243-1250
    • Oliva, M.A.1    Cordell, S.C.2    Lowe, J.3
  • 45
    • 84868326175 scopus 로고    scopus 로고
    • ZipA is required for FtsZ-dependent preseptal peptidoglycan synthesis prior to invagination during cell division
    • Potluri L-P, Kannan S, Young KD (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.-P.1    Kannan, S.2    Young, K.D.3
  • 46
    • 79960913936 scopus 로고    scopus 로고
    • Direct membrane binding by bacterial actin MreB
    • Salje J, Van den Ent F, De Boer P, 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
  • 47
    • 57149120088 scopus 로고    scopus 로고
    • Determination of bacterial rod shape by a novel cytoskeletal membrane protein
    • Shiomi D, Sakai M, Niki H (2008) Determination of bacterial rod shape by a novel cytoskeletal membrane protein. EMBO J 27: 3081-3091
    • (2008) EMBO J , vol.27 , pp. 3081-3091
    • Shiomi, D.1    Sakai, M.2    Niki, H.3
  • 48
    • 79955024764 scopus 로고    scopus 로고
    • Highthroughput, subpixel-precision analysis of bacterial morphogenesis and intracellular spatiooral dynamics
    • Sliusarenko O, Heinritz J, Emonet T, Jacobs-Wagner C (2012) Highthroughput, subpixel-precision analysis of bacterial morphogenesis and intracellular spatiooral dynamics. Mol Microbiol 80: 612-627
    • (2012) Mol Microbiol , vol.80 , pp. 612-627
    • Sliusarenko, O.1    Heinritz, J.2    Emonet, T.3    Jacobs-Wagner, C.4
  • 49
    • 84871055385 scopus 로고    scopus 로고
    • The helical MreB cytoskeleton in E. coli MC1000/pLE7 is an artifact of the N-terminal YFP tag
    • Swulius MT, Jensen GJ (2012) The helical MreB cytoskeleton in E. coli MC1000/pLE7 is an artifact of the N-terminal YFP tag. J Bacteriol 194: 6382-6386
    • (2012) J Bacteriol , vol.194 , pp. 6382-6386
    • Swulius, M.T.1    Jensen, G.J.2
  • 50
    • 79953808579 scopus 로고    scopus 로고
    • YeeV is an Escherichia coli toxin that inhibits cell division by targeting the cytoskeleton proteins
    • Tan Q, Awano N, Inouye M (2011) YeeV is an Escherichia coli toxin that inhibits cell division by targeting the cytoskeleton proteins, FtsZ and MreB. Mol Microbiol 79: 109-118
    • (2011) FtsZ and MreB. Mol Microbiol , vol.79 , pp. 109-118
    • Tan, Q.1    Awano, N.2    Inouye, M.3
  • 51
    • 84855889658 scopus 로고    scopus 로고
    • From the regulation of peptidoglycan synthesis to bacterial growth and morphology
    • Typas A, Banzhaf M, Gross CA, Vollmer W (2012) From the regulation of peptidoglycan synthesis to bacterial growth and morphology. Nat Rev Microbiol 10: 123-136
    • (2012) Nat Rev Microbiol , vol.10 , pp. 123-136
    • Typas, A.1    Banzhaf, M.2    Gross, C.A.3    Vollmer, W.4
  • 52
    • 0035817819 scopus 로고    scopus 로고
    • Prokaryotic origin of the actin cytoskeleton
    • Van den Ent F, Amos LA, Lowe J (2001) Prokaryotic origin of the actin cytoskeleton. Nature 413: 39-44
    • (2001) Nature , vol.413 , pp. 39-44
    • Van Den Ent, F.1    Amos, L.A.2    Lowe, J.3
  • 53
    • 77949567575 scopus 로고    scopus 로고
    • Bacterial actin MreB assembles in complex with cell shape protein RodZ
    • Van den Ent F, Johnson CM, Persons L, De Boer P, Lowe J (2010) Bacterial actin MreB assembles in complex with cell shape protein RodZ. EMBO J 29: 1081-1090
    • (2010) EMBO J , vol.29 , pp. 1081-1090
    • Van Den Ent, F.1    Johnson, C.M.2    Persons, L.3    De Boer, P.4    Lowe, J.5
  • 56
    • 34547618469 scopus 로고    scopus 로고
    • FtsZ directs a second mode of peptidoglycan synthesis in Escherichia coli
    • Varma A, De Pedro MA, Young KD (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
  • 57
    • 66149136478 scopus 로고    scopus 로고
    • Escherichia coli, MreB and FtsZ direct the synthesis of lateral cell wall via independent pathways that require PBP 2
    • Varma A, Young KD (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
  • 58
    • 36749016781 scopus 로고    scopus 로고
    • Duplication and segregation of the actin (MreB) cytoskeleton during the prokaryotic cell cycle
    • Vats P, Rothfield L (2007) Duplication and segregation of the actin (MreB) cytoskeleton during the prokaryotic cell cycle. PNAS 104: 17795-17800
    • (2007) PNAS , vol.104 , pp. 17795-17800
    • Vats, P.1    Rothfield, L.2
  • 59
    • 62949149564 scopus 로고    scopus 로고
    • Assembly of the MreBassociated cytoskeletal ring of Escherichia coli
    • Vats P, Shih Y-L, Rothfield L (2009) Assembly of the MreBassociated 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
  • 60
    • 50049104157 scopus 로고    scopus 로고
    • Murein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli
    • Vollmer W, 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
  • 61
    • 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, 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
  • 62
    • 0024401930 scopus 로고
    • Negative control of cell division by mreB, a gene that functions in determining the rod shape of Escherichia coli cells
    • Wachi M, Matsuhashi M (1989) Negative control of cell division by mreB, a gene that functions in determining the rod shape of Escherichia coli cells. J Bacteriol 171: 3123-3127
    • (1989) J Bacteriol , vol.171 , pp. 3123-3127
    • Wachi, M.1    Matsuhashi, M.2
  • 63
    • 77951608842 scopus 로고    scopus 로고
    • Positioning cell wall synthetic complexes by the bacterial morphogenetic proteins MreB and MreD
    • White CL, Kitich A, Gober JW (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 FB, 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


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