메뉴 건너뛰기




Volumn 191, Issue 11, 2009, Pages 3526-3533

In Escherichia coli, MreB and FtsZ direct the synthesis of lateral cell wall via independent pathways that require PBP 2

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYPEPTIDASE; FTSZ PROTEIN; MREB PROTEIN; PENICILLIN BINDING PROTEIN 2; PENTAPEPTIDE; PEPTIDOGLYCAN; UNCLASSIFIED DRUG; 2,6 DICHLOROBENZYLTHIOPSEUDOUREA; 2,6-DICHLOROBENZYLTHIOPSEUDOUREA; ARABINOSE; AZTREONAM; BACTERIAL PROTEIN; CYTOSKELETON PROTEIN; DRUG DERIVATIVE; ESCHERICHIA COLI PROTEIN; FTSZ PROTEIN, BACTERIA; MREB PROTEIN, E COLI; PENICILLIN BINDING PROTEIN; SULA PROTEIN, E COLI; THIOUREA;

EID: 66149136478     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01812-08     Document Type: Article
Times cited : (66)

References (38)
  • 1
    • 34248364322 scopus 로고    scopus 로고
    • The tubulin homologue FtsZ contributes to cell elongation by guiding cell wall precursor synthesis in Caulobacter crescentus
    • DOI 10.1111/j.1365-2958.2007.05720.x
    • Aaron, M., G. Charbon, H. Lam, H. Schwarz, W. Vollmer, and C. Jacobs- Wagner. 2007. The tubulin homologue FtsZ contributes to cell elongation by guiding cell wall precursor synthesis in Caulobacter crescentus. Mol. Microbiol. 64:938-952. (Pubitemid 46743973)
    • (2007) Molecular Microbiology , vol.64 , Issue.4 , pp. 938-952
    • Aaron, M.1    Charbon, G.2    Lam, H.3    Schwarz, H.4    Vollmer, W.5    Jacobs-Wagner, C.6
  • 2
    • 0036900016 scopus 로고    scopus 로고
    • Assembly of cell division proteins at the E. coli cell center
    • Buddelmeijer, N., and J. Beckwith. 2002. Assembly of cell division proteins at the E. coli cell center. Curr. Opin. Microbiol. 5:553-557.
    • (2002) Curr. Opin. Microbiol. , vol.5 , pp. 553-557
    • Buddelmeijer, N.1    Beckwith, J.2
  • 3
    • 0030742717 scopus 로고    scopus 로고
    • Cell elongation and septation are two mutually exclusive processes in Escherichia coli
    • DOI 10.1007/s002030050481
    • Canepari, P., C. Signoretto, M. Boaretti, and M. M. Lleo. 1997. Cell elongation and septation are two mutually exclusive processes in Escherichia coli. Arch. Microbiol. 168:152-159. (Pubitemid 27359845)
    • (1997) Archives of Microbiology , vol.168 , Issue.2 , pp. 152-159
    • Canepari, P.1    Signoretto, C.2    Boaretti, M.3    Lleo, M.D.M.4
  • 5
    • 33646420904 scopus 로고    scopus 로고
    • Orchestrating bacterial cell morphogenesis
    • Carballido-Lopez, R. 2006. Orchestrating bacterial cell morphogenesis. Mol. Microbiol. 60:815-819.
    • (2006) Mol. Microbiol. , vol.60 , pp. 815-819
    • Carballido-Lopez, R.1
  • 7
    • 0037494988 scopus 로고    scopus 로고
    • Control of cell morphogenesis in bacteria. Two distinct ways to make a rod-shaped cell
    • Daniel, R. A., and J. Errington. 2003. Control of cell morphogenesis in bacteria. Two distinct ways to make a rod-shaped cell. Cell 113:767-776.
    • (2003) Cell , vol.113 , pp. 767-776
    • Daniel, R.A.1    Errington, J.2
  • 8
    • 0032985224 scopus 로고    scopus 로고
    • Escherichia coli mutants lacking all possible combinations of eight penicillin binding proteins: Viability, characteristics, and implications for peptidoglycan synthesis
    • Denome, S. A., P. K. Elf, T. A. Henderson, D. E. Nelson, and K. D. Young. 1999. Escherichia coli mutants lacking all possible combinations of eight penicillin binding proteins: viability, characteristics, and implications for peptidoglycan synthesis. J. Bacteriol. 181:3981-3993.
    • (1999) J. Bacteriol. , vol.181 , pp. 3981-3993
    • Denome, S.A.1    Elf, P.K.2    Henderson, T.A.3    Nelson, D.E.4    Young, K.D.5
  • 10
    • 34548677525 scopus 로고    scopus 로고
    • The cell shape proteins MreB and MreC control cell morphogenesis by positioning cell wall synthetic complexes
    • Divakaruni, A. V., C. Baida, C. L. White, and J. W. Gober. 2007. The cell shape proteins MreB and MreC control cell morphogenesis by positioning cell wall synthetic complexes. Mol. Microbiol. 66:174-188.
    • (2007) Mol. Microbiol. , vol.66 , pp. 174-188
    • Divakaruni, A.V.1    Baida, C.2    White, C.L.3    Gober, J.W.4
  • 12
    • 15944399775 scopus 로고    scopus 로고
    • A magnesium-dependent mreB null mutant: Implications for the role of mreB in Bacillus subtilis
    • DOI 10.1111/j.1365-2958.2005.04506.x
    • Formstone, A., and J. Errington. 2005. A magnesium-dependent mreB null mutant: implications for the role of mreB in Bacillus subtilis. Mol. Microbiol. 55:1646-1657. (Pubitemid 40445203)
    • (2005) Molecular Microbiology , vol.55 , Issue.6 , pp. 1646-1657
    • Formstone, A.1    Errington, J.2
  • 13
    • 0025123204 scopus 로고
    • Differential effect of mutational impairment of penicillin-binding proteins 1A and 1B on Escherichia coli strains harboring thermosensitive mutations in the cell division genes ftsA, ftsQ, ftsZ, and pbpB
    • Garcia del Portillo, F., and M. A. de Pedro. 1990. Differential effect of mutational impairment of penicillin-binding proteins 1A and 1B on Escherichia coli strains harboring thermosensitive mutations in the cell division genes ftsA, ftsQ, ftsZ, and pbpB. J. Bacteriol. 172:5863-5870. (Pubitemid 20317125)
    • (1990) Journal of Bacteriology , vol.172 , Issue.10 , pp. 5863-5870
    • Garcia Del Portillo, F.1    De Pedro, M.A.2
  • 14
    • 13544274210 scopus 로고    scopus 로고
    • MreB actin-mediated segregation of a specific region of a bacterial chromosome
    • DOI 10.1016/j.cell.2005.01.007
    • Gitai, Z., N. A. Dye, A. Reisenauer, M. Wachi, and L. Shapiro. 2005. MreB actin-mediated segregation of a specific region of a bacterial chromosome. Cell 120:329-341. (Pubitemid 40222428)
    • (2005) Cell , vol.120 , Issue.3 , pp. 329-341
    • Gitai, Z.1    Dye, N.A.2    Reisenauer, A.3    Wachi, M.4    Shapiro, L.5
  • 15
    • 21844441637 scopus 로고    scopus 로고
    • Diverse paths to midcell: Assembly of the bacterial cell division machinery
    • Goehring, N. W., and J. Beckwith. 2005. Diverse paths to midcell: assembly of the bacterial cell division machinery. Curr. Biol. 15:R514-R26.
    • (2005) Curr. Biol. , vol.15
    • Goehring, N.W.1    Beckwith, J.2
  • 16
    • 0015061858 scopus 로고
    • Procaryotic cell division with respect to wall and membranes
    • Higgins, M. L., and G. D. Shockman. 1971. Procaryotic cell division with respect to wall and membranes. CRC Crit. Rev. Microbiol. 1:29-72.
    • (1971) CRC Crit. Rev. Microbiol. , vol.1 , pp. 29-72
    • Higgins, M.L.1    Shockman, G.D.2
  • 17
    • 0037858060 scopus 로고    scopus 로고
    • Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli
    • Höltje, J.-V. 1998. Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli. Microbiol. Mol. Biol. Rev. 62:181-203. (Pubitemid 28130800)
    • (1998) Microbiology and Molecular Biology Reviews , vol.62 , Issue.1 , pp. 181-203
    • Holtje, J.-V.1
  • 18
    • 0035937396 scopus 로고    scopus 로고
    • Control of cell shape in bacteria: Helical, actin-like filaments in Bacillus subtilis
    • Jones, L. J., R. Carballido-Lopez, and J. Errington. 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
  • 19
    • 12344306119 scopus 로고    scopus 로고
    • The morphogenetic Mre- BCD proteins of Escherichia coli form an essential membrane-bound complex
    • Kruse, T., J. Bork-Jensen, and K. Gerdes. 2005. The morphogenetic Mre- BCD 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
  • 20
    • 23844444807 scopus 로고    scopus 로고
    • Roles for MreC and MreD proteins in helical growth of the cylindrical cell wall in Bacillus subtilis
    • DOI 10.1111/j.1365-2958.2005.04736.x
    • Leaver, M., and J. Errington. 2005. Roles for MreC and MreD proteins in helical growth of the cylindrical cell wall in Bacillus subtilis. Mol. Microbiol. 57:1196-1209. (Pubitemid 41176518)
    • (2005) Molecular Microbiology , vol.57 , Issue.5 , pp. 1196-1209
    • Leaver, M.1    Errington, J.2
  • 21
    • 0030956145 scopus 로고    scopus 로고
    • Bacterial cell division and the Z ring
    • Lutkenhaus, J., and S. G. Addinall. 1997. Bacterial cell division and the Z ring. Annu. Rev. Biochem. 66:93-116.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 93-116
    • Lutkenhaus, J.1    Addinall, S.G.2
  • 22
    • 0033823009 scopus 로고    scopus 로고
    • Themes and variations in prokaryotic cell division
    • Margolin, W. 2000. Themes and variations in prokaryotic cell division. FEMS Microbiol. Rev. 24:531-548.
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 531-548
    • Margolin, W.1
  • 23
    • 33644778043 scopus 로고    scopus 로고
    • Trapping of a spiral-like intermediate of the bacterial cytokinetic protein FtsZ
    • DOI 10.1128/JB.188.5.1680-1690.2006
    • Michie, K. A., L. G. Monahan, P. L. Beech, and E. J. Harry. 2006. Trapping of a spiral-like intermediate of the bacterial cytokinetic protein FtsZ. J. Bacteriol. 188:1680-1690. (Pubitemid 43346847)
    • (2006) Journal of Bacteriology , vol.188 , Issue.5 , pp. 1680-1690
    • Michie, K.A.1    Monahan, L.G.2    Beech, P.L.3    Harry, E.J.4
  • 24
    • 0031912354 scopus 로고    scopus 로고
    • Morphogenesis of Escherichia coli
    • Nanninga, N. 1998. Morphogenesis of Escherichia coli. Microbiol. Mol. Biol. Rev. 62:110-129.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 110-129
    • Nanninga, N.1
  • 25
    • 0001985244 scopus 로고    scopus 로고
    • The murein sacculus
    • F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), ASM Press, Washington, DC
    • Park, J. T. 1996. The murein sacculus, p. 48-57. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella typhimurium: cellular and molecular biology, 2nd ed., vol.1. ASM Press, Washington, DC.
    • (1996) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology, 2nd Ed. , vol.1 , pp. 48-57
    • Park, J.T.1
  • 26
    • 34247349124 scopus 로고    scopus 로고
    • A new assembly pathway for the cytokinetic Z ring from a dynamic helical structure in vegetatively growing cells of Bacillus subtilis
    • DOI 10.1111/j.1365-2958.2007.05673.x
    • Peters, P. C., M. D. Migocki, C. Thoni, and E. J. Harry. 2007. A new assembly pathway for the cytokinetic Z ring from a dynamic helical structure in vegetatively growing cells of Bacillus subtilis. Mol. Microbiol. 64:487-499. (Pubitemid 46632632)
    • (2007) Molecular Microbiology , vol.64 , Issue.2 , pp. 487-499
    • Peters, P.C.1    Migocki, M.D.2    Thoni, C.3    Harry, E.J.4
  • 27
    • 15744385269 scopus 로고    scopus 로고
    • Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA
    • Pichoff, S., and J. Lutkenhaus. 2005. Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA. Mol. Microbiol. 55:1722-1734.
    • (2005) Mol. Microbiol. , vol.55 , pp. 1722-1734
    • Pichoff, S.1    Lutkenhaus, J.2
  • 28
    • 0242606152 scopus 로고    scopus 로고
    • Dispersed mode of Staphylococcus aureus cell wall synthesis in the absence of the division machinery
    • Pinho, M. G., and J. Errington. 2003. Dispersed mode of Staphylococcus aureus cell wall synthesis in the absence of the division machinery. Mol. Microbiol. 50:871-881.
    • (2003) Mol. Microbiol. , vol.50 , pp. 871-881
    • Pinho, M.G.1    Errington, J.2
  • 29
    • 0347364718 scopus 로고    scopus 로고
    • Role of penicillin-binding proteins in bacterial cell morphogenesis
    • Popham, D. L., and K. D. Young. 2003. Role of penicillin-binding proteins in bacterial cell morphogenesis. Curr. Opin. Microbiol. 6:594-599.
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 594-599
    • Popham, D.L.1    Young, K.D.2
  • 30
    • 0028324126 scopus 로고
    • The two-competing site (TCS) model for cell shape regulation in bacteria: The envelope as an integration point for the regulatory circuits of essential physiological events
    • Satta, G., R. Fontana, and P. Canepari. 1994. The two-competing site (TCS) model for cell shape regulation in bacteria: the envelope as an integration point for the regulatory circuits of essential physiological events. Adv. Microb. Physiol. 36:181-245.
    • (1994) Adv. Microb. Physiol. , vol.36 , pp. 181-245
    • Satta, G.1    Fontana, R.2    Canepari, P.3
  • 32
    • 0018148856 scopus 로고
    • Escherichia coli resistance to beta-lactam antibiotics through a decrease in the affinity of a target for lethality
    • Spratt, B. G. 1978. Escherichia coli resistance to beta-lactam antibiotics through a decrease in the affinity of a target for lethality. Nature 274:713-715.
    • (1978) Nature , vol.274 , pp. 713-715
    • Spratt, B.G.1
  • 33
    • 3142602980 scopus 로고    scopus 로고
    • FtsZ exhibits rapid movement and oscillation waves in Helix-like patterns in Escherichia coli
    • DOI 10.1016/j.cub.2004.06.048, PII S0960982204004336
    • Thanedar, S., and W. Margolin. 2004. FtsZ exhibits rapid movement and oscillation waves in helix-like patterns in Escherichia coli. Curr. Biol. 14:1167-1173. (Pubitemid 38893979)
    • (2004) Current Biology , vol.14 , Issue.13 , pp. 1167-1173
    • Thanedar, S.1    Margolin, W.2
  • 34
    • 44349107842 scopus 로고    scopus 로고
    • Growth of Escherichia coli: Significance of peptidoglycan degradation during elongation and septation
    • Uehara, T., and J. T. Park. 2008. Growth of Escherichia coli: significance of peptidoglycan degradation during elongation and septation. J. Bacteriol. 190:3914-3922.
    • (2008) J. Bacteriol. , vol.190 , pp. 3914-3922
    • Uehara, T.1    Park, J.T.2
  • 35
    • 34547618469 scopus 로고    scopus 로고
    • FtsZ directs a second mode of peptidoglycan synthesis in Escherichia coli
    • Varma, A., M. A. de Pedro, and K. D. Young. 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
  • 36
    • 4944246437 scopus 로고    scopus 로고
    • FtsZ collaborates with penicillin binding proteins to generate bacterial cell shape in Escherichia coli
    • DOI 10.1128/JB.186.20.6768-6774.2004
    • Varma, A., and K. D. Young. 2004. FtsZ collaborates with penicillin binding proteins to generate bacterial cell shape in Escherichia coli. J. Bacteriol. 186:6768-6774. (Pubitemid 39332114)
    • (2004) Journal of Bacteriology , vol.186 , Issue.20 , pp. 6768-6774
    • Varma, A.1    Young, K.D.2
  • 37
    • 0024332035 scopus 로고
    • New mre genes mreC and mreD, responsible for formation of the rod shape of Escherichia coli cells
    • Wachi, M., M. Doi, Y. Okada, and M. Matsuhashi. 1989. New mre genes mreC and mreD, responsible for formation of the rod shape of Escherichia coli cells. J. Bacteriol. 171:6511-6516.
    • (1989) J. Bacteriol. , vol.171 , pp. 6511-6516
    • Wachi, M.1    Doi, M.2    Okada, Y.3    Matsuhashi, M.4
  • 38
    • 0024381715 scopus 로고
    • Rate and topography of peptidoglycan synthesis during cell division in Escherichia coli: Concept of a leading edge
    • Wientjes, F. B., and N. Nanninga. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.