메뉴 건너뛰기




Volumn 190, Issue 11, 2008, Pages 3914-3922

Growth of Escherichia coli: Significance of peptidoglycan degradation during elongation and septation

Author keywords

[No Author keywords available]

Indexed keywords

AMIDASE; BACTERIAL PROTEIN; GLYCAN; GLYCOSYLTRANSFERASE; MECILLINAM; MREB PROTEIN; PENICILLIN BINDING PROTEIN; PENICILLIN BINDING PROTEIN 2; PEPTIDOGLYCAN; PROFADOL; PROTEIN AMPD; PROTEIN RODA;

EID: 44349107842     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00207-08     Document Type: Article
Times cited : (80)

References (70)
  • 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., 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.
    • (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
  • 2
    • 31544450286 scopus 로고    scopus 로고
    • Baba, T., T. Ara, M. Hasegawa, Y. Takai, Y. Okumura, M. Baba, K. A. Datsenko, M. Tomita, B. L. Wanner, and H. Mori. 2006. Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol. Syst. Biol. doi:10.1038/msb4100050.
    • Baba, T., T. Ara, M. Hasegawa, Y. Takai, Y. Okumura, M. Baba, K. A. Datsenko, M. Tomita, B. L. Wanner, and H. Mori. 2006. Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol. Syst. Biol. doi:10.1038/msb4100050.
  • 3
    • 0019452243 scopus 로고
    • Exoenzymatic activity of transglycosylase isolated from Escherichia coli
    • Beachey, E. H., W. Keck, M. A. de Pedro, and U. Schwarz. 1981. Exoenzymatic activity of transglycosylase isolated from Escherichia coli. Eur. J. Biochem. 116:355-358.
    • (1981) Eur. J. Biochem , vol.116 , pp. 355-358
    • Beachey, E.H.1    Keck, W.2    de Pedro, M.A.3    Schwarz, U.4
  • 4
    • 0015502091 scopus 로고
    • A binding protein involved in the transport of cystine and diaminopimelic acid in Escherichia coli
    • Berger, E. A., and L. A. Heppel. 1972. A binding protein involved in the transport of cystine and diaminopimelic acid in Escherichia coli. J. Biol. Chem. 247:7684-7694.
    • (1972) J. Biol. Chem , vol.247 , pp. 7684-7694
    • Berger, E.A.1    Heppel, L.A.2
  • 5
    • 27844575191 scopus 로고    scopus 로고
    • In vitro murein peptidoglycan synthesis by dimers of the bifunctional transglycosylase-transpeptidase PBP1B from Escherichia coli
    • Bertsche, U., E. Breukink, T. Kast, and W. Vollmer. 2005. In vitro murein peptidoglycan synthesis by dimers of the bifunctional transglycosylase-transpeptidase PBP1B from Escherichia coli. J. Biol. Chem. 280:38096-38101.
    • (2005) J. Biol. Chem , vol.280 , pp. 38096-38101
    • Bertsche, U.1    Breukink, E.2    Kast, T.3    Vollmer, W.4
  • 6
    • 33748333182 scopus 로고    scopus 로고
    • Bertsche, U., T. Kast, B. Wolf, C. Fraipont, M. E. Aarsman, K. Kannenberg, M. von Rechenberg, M. Nguyen-Distèche, T. den Blaauwen, J. V. Höltje, and W. Vollmer. 2006. Interaction between two murein (peptidoglycan) synthases, PBP3 and PBP1B, in Escherichia coli. Mol. Microbiol. 61:675-690.
    • Bertsche, U., T. Kast, B. Wolf, C. Fraipont, M. E. Aarsman, K. Kannenberg, M. von Rechenberg, M. Nguyen-Distèche, T. den Blaauwen, J. V. Höltje, and W. Vollmer. 2006. Interaction between two murein (peptidoglycan) synthases, PBP3 and PBP1B, in Escherichia coli. Mol. Microbiol. 61:675-690.
  • 7
    • 0027513320 scopus 로고
    • Cell division inhibitors SulA and MinCD prevent formation of the FtsZ ring
    • Bi, E., and J. Lutkenhaus. 1993. Cell division inhibitors SulA and MinCD prevent formation of the FtsZ ring. J. Bacteriol. 175:1118-1125.
    • (1993) J. Bacteriol , vol.175 , pp. 1118-1125
    • Bi, E.1    Lutkenhaus, J.2
  • 8
    • 0016265366 scopus 로고
    • Electron microscope study of septum formation in Escherichia coli strains B and B-r during synchronous growth
    • Burdett, I. D., and R. G. Murray. 1974. Electron microscope study of septum formation in Escherichia coli strains B and B-r during synchronous growth. J. Bacteriol. 119:1039-1056.
    • (1974) J. Bacteriol , vol.119 , pp. 1039-1056
    • Burdett, I.D.1    Murray, R.G.2
  • 9
    • 0016193630 scopus 로고
    • Septum formation in Escherichia coli: Characterization of septal structure and the effects of antibiotics on cell division
    • Burdett, I. D., and R. G. Murray. 1974. Septum formation in Escherichia coli: characterization of septal structure and the effects of antibiotics on cell division. J. Bacteriol. 119:303-324.
    • (1974) J. Bacteriol , vol.119 , pp. 303-324
    • Burdett, I.D.1    Murray, R.G.2
  • 10
    • 0020554044 scopus 로고
    • Evidence for diffuse growth of the cylindrical portion of the Escherichia coli murein sacculus
    • Burman, L. G., J. Raichler, and J. T. Park. 1983. Evidence for diffuse growth of the cylindrical portion of the Escherichia coli murein sacculus. J. Bacteriol. 155:983-988.
    • (1983) J. Bacteriol , vol.155 , pp. 983-988
    • Burman, L.G.1    Raichler, J.2    Park, J.T.3
  • 11
    • 0033897724 scopus 로고    scopus 로고
    • Molecular characterization of the β-N-acetylglucosaminidase of Escherichia coli and its role in cell wall recycling
    • Cheng, Q., H. Li, K. Merdek, and J. T. Park. 2000. Molecular characterization of the β-N-acetylglucosaminidase of Escherichia coli and its role in cell wall recycling. J. Bacteriol. 182:4836- 4840.
    • (2000) J. Bacteriol , vol.182 , pp. 4836-4840
    • Cheng, Q.1    Li, H.2    Merdek, K.3    Park, J.T.4
  • 12
    • 0036889483 scopus 로고    scopus 로고
    • Substrate specificity of the AmpG permease required for recycling of cell wall anhydro-muropeptides
    • Cheng, Q., and J. T. Park. 2002. Substrate specificity of the AmpG permease required for recycling of cell wall anhydro-muropeptides. J. Bacteriol. 184:6434-6436.
    • (2002) J. Bacteriol , vol.184 , pp. 6434-6436
    • Cheng, Q.1    Park, J.T.2
  • 13
    • 0023782390 scopus 로고
    • Mode of peptidoglycan synthesis in Salmonella typhimurium: Single-strand insertion
    • Cooper, S., M. L. Hsieh, and B. Guenther. 1988. Mode of peptidoglycan synthesis in Salmonella typhimurium: single-strand insertion. J. Bacteriol. 170:3509-3512.
    • (1988) J. Bacteriol , vol.170 , pp. 3509-3512
    • Cooper, S.1    Hsieh, M.L.2    Guenther, B.3
  • 14
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and B. L. Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 15
    • 0024458975 scopus 로고
    • Peptidoglycan synthesis during the cell cycle of Escherichia coli: Composition and mode of insertion
    • de Jonge, B. L., F. B. Wientjes, I. Jurida, F. Driehuis, J. T. Wouters, and N. Nanninga. 1989. Peptidoglycan synthesis during the cell cycle of Escherichia coli: composition and mode of insertion. J. Bacteriol. 171:5783-5794.
    • (1989) J. Bacteriol , vol.171 , pp. 5783-5794
    • de Jonge, B.L.1    Wientjes, F.B.2    Jurida, I.3    Driehuis, F.4    Wouters, J.T.5    Nanninga, N.6
  • 16
    • 0034976746 scopus 로고    scopus 로고
    • Constitutive septal murein synthesis in Escherichia coli with impaired activity of the morphogenetic proteins RodA and penicillin-binding protein 2
    • de Pedro, M. A., W. D. Donachie, J. V. Höltje, and H. Schwarz. 2001. Constitutive septal murein synthesis in Escherichia coli with impaired activity of the morphogenetic proteins RodA and penicillin-binding protein 2. J. Bacteriol. 183:4115-4126.
    • (2001) J. Bacteriol , vol.183 , pp. 4115-4126
    • de Pedro, M.A.1    Donachie, W.D.2    Höltje, J.V.3    Schwarz, H.4
  • 18
    • 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
  • 19
    • 29344476196 scopus 로고    scopus 로고
    • The cell-shape protein MreC interacts with extracytoplasmic proteins including cell wall assembly complexes in Caulobacter crescentus
    • Divakaruni, A. V., R. R. Loo, Y. Xie, J. A. Loo, and J. W. Gober. 2005. The cell-shape protein MreC interacts with extracytoplasmic proteins including cell wall assembly complexes in Caulobacter crescentus. Proc. Natl. Acad. Sci. USA 102:18602-18607.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 18602-18607
    • Divakaruni, A.V.1    Loo, R.R.2    Xie, Y.3    Loo, J.A.4    Gober, J.W.5
  • 20
    • 1542616355 scopus 로고    scopus 로고
    • MreB, the cell shape-determining bacterial actin homologue, co-ordinates cell wall morphogenesis in Caulobacter crescentus
    • Figge, R. M., A. V. Divakaruni, and J. W. Gober. 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
  • 21
    • 13544274210 scopus 로고    scopus 로고
    • MreB actin-mediated segregation of a specific region of a bacterial chromosome
    • 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.
    • (2005) Cell , vol.120 , pp. 329-341
    • Gitai, Z.1    Dye, N.A.2    Reisenauer, A.3    Wachi, M.4    Shapiro, L.5
  • 22
    • 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-R526.
    • (2005) Curr. Biol , vol.15
    • Goehring, N.W.1    Beckwith, J.2
  • 23
    • 0021881891 scopus 로고
    • Recycling of murein by Escherichia coli
    • Goodell, E. W. 1985. Recycling of murein by Escherichia coli. J. Bacteriol. 163:305-310.
    • (1985) J. Bacteriol , vol.163 , pp. 305-310
    • Goodell, E.W.1
  • 24
    • 0021981840 scopus 로고
    • Release of cell wall peptides into culture medium by exponentially growing Escherichia coli
    • Goodell, E. W., and U. Schwarz. 1985. Release of cell wall peptides into culture medium by exponentially growing Escherichia coli. J. Bacteriol. 162:391-397.
    • (1985) J. Bacteriol , vol.162 , pp. 391-397
    • Goodell, E.W.1    Schwarz, U.2
  • 25
  • 26
    • 0036843026 scopus 로고    scopus 로고
    • Effects of multiple deletions of murein hydrolases on viability, septum cleavage, and sensitivity to large toxic molecules in Escherichia coli
    • Heidrich, C., A. Ursinus, J. Berger, H. Schwarz, and J. V. Höltje. 2002. Effects of multiple deletions of murein hydrolases on viability, septum cleavage, and sensitivity to large toxic molecules in Escherichia coli. J. Bacteriol. 184:6093-6099.
    • (2002) J. Bacteriol , vol.184 , pp. 6093-6099
    • Heidrich, C.1    Ursinus, A.2    Berger, J.3    Schwarz, H.4    Höltje, J.V.5
  • 27
    • 0031944802 scopus 로고    scopus 로고
    • Henriques, A. O., P. Glaser, P. J. Piggot, and C. P. Moran, Jr. 1998. Control of cell shape and elongation by the rodA gene in Bacillus subtilis. Mol. Microbiol. 28:235-247.
    • Henriques, A. O., P. Glaser, P. J. Piggot, and C. P. Moran, Jr. 1998. Control of cell shape and elongation by the rodA gene in Bacillus subtilis. Mol. Microbiol. 28:235-247.
  • 28
    • 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.
    • (1998) Microbiol. Mol. Biol. Rev , vol.62 , pp. 181-203
    • Höltje, J.V.1
  • 30
    • 0020352441 scopus 로고
    • A mecillinam-sensitive peptidoglycan crosslinking reaction in Escherichia coli
    • Ishino, F., S. Tamaki, B. G. Spratt, and M. Matsuhashi. 1982. A mecillinam-sensitive peptidoglycan crosslinking reaction in Escherichia coli. Biochem. Biophys. Res. Commun. 109:689-696.
    • (1982) Biochem. Biophys. Res. Commun , vol.109 , pp. 689-696
    • Ishino, F.1    Tamaki, S.2    Spratt, B.G.3    Matsuhashi, M.4
  • 31
    • 0041701451 scopus 로고    scopus 로고
    • Novel S-benzylisothiourea compound that induces spherical cells in Escherichia coli probably by acting on a rod-shape-determining protein(s) other than penicillin-binding protein 2
    • Iwai, N., K. Nagai, and M. Wachi. 2002. Novel S-benzylisothiourea compound that induces spherical cells in Escherichia coli probably by acting on a rod-shape-determining protein(s) other than penicillin-binding protein 2. Biosci. Biotechnol. Biochem. 66:2658-2662.
    • (2002) Biosci. Biotechnol. Biochem , vol.66 , pp. 2658-2662
    • Iwai, N.1    Nagai, K.2    Wachi, M.3
  • 32
    • 0028147092 scopus 로고
    • Bacterial cell wall recycling provides cytosolic muropeptides as effectors for β-lactamase induction
    • Jacobs, C., L. J. Huang, E. Bartowsky, S. Normark, and J. T. Park. 1994. Bacterial cell wall recycling provides cytosolic muropeptides as effectors for β-lactamase induction. EMBO J. 13:4684-4694.
    • (1994) EMBO J , vol.13 , pp. 4684-4694
    • Jacobs, C.1    Huang, L.J.2    Bartowsky, E.3    Normark, S.4    Park, J.T.5
  • 34
    • 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., R. M.-A. Baselga, S. Alexeeva, F. G. Hansen, M. Vicente, N. Nanninga, and T. den Blaauwen. 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    Baselga, R.M.-A.2    Alexeeva, S.3    Hansen, F.G.4    Vicente, M.5    Nanninga, N.6    den Blaauwen, T.7
  • 35
    • 0031748682 scopus 로고    scopus 로고
    • Membrane-bound lytic endotransglycosylase in Escherichia coli
    • Kraft, A. R., M. F. Templin, and J. V. Höltje. 1998. Membrane-bound lytic endotransglycosylase in Escherichia coli. J. Bacteriol. 180:3441-3447.
    • (1998) J. Bacteriol , vol.180 , pp. 3441-3447
    • Kraft, A.R.1    Templin, M.F.2    Höltje, J.V.3
  • 36
    • 12344306119 scopus 로고    scopus 로고
    • The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex
    • Kruse, T., J. Bork-Jensen, and K. Gerdes. 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
  • 37
    • 0025966272 scopus 로고
    • Direct proof of a "more-than-single-layered" peptidoglycan architecture of Escherichia coli W7: A neutron small-angle scattering study
    • Labischinski, H., E. W. Goodell, A. Goodell, and M. L. Hochberg. 1991. Direct proof of a "more-than-single-layered" peptidoglycan architecture of Escherichia coli W7: a neutron small-angle scattering study. J. Bacteriol. 173:751-756.
    • (1991) J. Bacteriol , vol.173 , pp. 751-756
    • Labischinski, H.1    Goodell, E.W.2    Goodell, A.3    Hochberg, M.L.4
  • 38
    • 0020458828 scopus 로고
    • Cytoplasmic steps of peptidoglycan synthesis in Escherichia coli
    • Mengin-Lecreulx, D., B. Flouret, and J. van Heijenoort. 1982. Cytoplasmic steps of peptidoglycan synthesis in Escherichia coli. J. Bacteriol. 151:1109-1117.
    • (1982) J. Bacteriol , vol.151 , pp. 1109-1117
    • Mengin-Lecreulx, D.1    Flouret, B.2    van Heijenoort, J.3
  • 39
    • 0029787789 scopus 로고    scopus 로고
    • Identification of the mpl gene encoding UDP-N-acetylmuramate: L-alanyl-γ-D-glutamyl-meso-diaminopimelate ligase in Escherichia coli and its role in recycling of cell wall peptidoglycan
    • Mengin-Lecreulx, D., J. van Heijenoort, and J. T. Park. 1996. Identification of the mpl gene encoding UDP-N-acetylmuramate: L-alanyl-γ-D-glutamyl-meso-diaminopimelate ligase in Escherichia coli and its role in recycling of cell wall peptidoglycan. J. Bacteriol. 178:5347-5352.
    • (1996) J. Bacteriol , vol.178 , pp. 5347-5352
    • Mengin-Lecreulx, D.1    van Heijenoort, J.2    Park, J.T.3
  • 40
  • 41
    • 0032539813 scopus 로고    scopus 로고
    • Inhibition of FtsZ polymerization by SulA, an inhibitor of septation in Escherichia coli
    • Mukherjee, A., C. Cao, and J. Lutkenhaus. 1998. Inhibition of FtsZ polymerization by SulA, an inhibitor of septation in Escherichia coli. Proc. Natl. Acad. Sci. USA 95:2885-2890.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2885-2890
    • Mukherjee, A.1    Cao, C.2    Lutkenhaus, J.3
  • 42
    • 0025775118 scopus 로고
    • Cell division and peptidoglycan assembly in Escherichia coli
    • Nanninga, N. 1991. Cell division and peptidoglycan assembly in Escherichia coli. Mol. Microbiol. 5:791-795.
    • (1991) Mol. Microbiol , vol.5 , pp. 791-795
    • Nanninga, N.1
  • 43
    • 4243272858 scopus 로고
    • An overview of the assembly, turnover, and recycling of the murein sacculus
    • M. A. de Pedro et al, ed, Plenum Press, New York, NY
    • Park, J. T. 1993. An overview of the assembly, turnover, and recycling of the murein sacculus. p. 119-126. In M. A. de Pedro et al. (ed.), Bacterial growth and lysis. Plenum Press, New York, NY.
    • (1993) Bacterial growth and lysis , pp. 119-126
    • Park, J.T.1
  • 44
    • 0001985244 scopus 로고    scopus 로고
    • The murein sacculus
    • F. C. Neidhardt et al, ed, American Society for Microbiology, Washington, DC
    • Park, J. T. 1996. The murein sacculus, p. 48-57. In F. C. Neidhardt et al. (ed.), Escherichia coli and Salmonella typhimurium: cellular and molecular biology, vol. 2. American Society for Microbiology, Washington, DC.
    • (1996) Escherichia coli and Salmonella typhimurium: Cellular and molecular biology , vol.2 , pp. 48-57
    • Park, J.T.1
  • 45
    • 0027514558 scopus 로고
    • Turnover and recycling of the murein sacculus in oligopeptide permease-negative strains of Escherichia coli: Indirect evidence for an alternative permease system and for a monolayered sacculus
    • Park, J. T. 1993. Turnover and recycling of the murein sacculus in oligopeptide permease-negative strains of Escherichia coli: indirect evidence for an alternative permease system and for a monolayered sacculus. J. Bacteriol. 175:7-11.
    • (1993) J. Bacteriol , vol.175 , pp. 7-11
    • Park, J.T.1
  • 46
    • 0015927252 scopus 로고
    • FL-1060: A new penicillin with a unique mode of action
    • Park, J. T., and L. Burman. 1973. FL-1060: a new penicillin with a unique mode of action. Biochem. Biophys. Res. Commun. 51:863-868.
    • (1973) Biochem. Biophys. Res. Commun , vol.51 , pp. 863-868
    • Park, J.T.1    Burman, L.2
  • 47
    • 44949258242 scopus 로고    scopus 로고
    • How bacteria consume their own exoskeleton (turnover and recycling of the cell wall peptidoglycan)
    • in press
    • Park, J. T., and T. Uehara. How bacteria consume their own exoskeleton (turnover and recycling of the cell wall peptidoglycan). Microbiol. Mol. Biol. Rev., in press.
    • Microbiol. Mol. Biol. Rev
    • Park, J.T.1    Uehara, T.2
  • 48
    • 35548940362 scopus 로고    scopus 로고
    • The direction of glycan chain elongation by peptidoglycan glycosyltransferases
    • Perlstein, D. L., Y. Zhang, T. S. Wang, D. E. Kahne, and S. Walker. 2007. The direction of glycan chain elongation by peptidoglycan glycosyltransferases. J. Am. Chem. Soc. 129:12674-12675.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 12674-12675
    • Perlstein, D.L.1    Zhang, Y.2    Wang, T.S.3    Kahne, D.E.4    Walker, S.5
  • 49
    • 34447515813 scopus 로고    scopus 로고
    • Role of peptidoglycan amidases in the development and morphology of the division septum in Escherichia coli
    • Priyadarshini, R., M. A. de Pedro, and K. D. Young. 2007. Role of peptidoglycan amidases in the development and morphology of the division septum in Escherichia coli. J. Bacteriol. 189:5334-5347.
    • (2007) J. Bacteriol , vol.189 , pp. 5334-5347
    • Priyadarshini, R.1    de Pedro, M.A.2    Young, K.D.3
  • 50
    • 33746649568 scopus 로고    scopus 로고
    • Daughter cell separation by penicillin-binding proteins and peptidoglycan amidases in Escherichia coli
    • Priyadarshini, R., D. L. Popham, and K. D. Young. 2006. Daughter cell separation by penicillin-binding proteins and peptidoglycan amidases in Escherichia coli. J. Bacteriol. 188:5345-5355.
    • (2006) J. Bacteriol , vol.188 , pp. 5345-5355
    • Priyadarshini, R.1    Popham, D.L.2    Young, K.D.3
  • 51
    • 0037699937 scopus 로고    scopus 로고
    • Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles
    • Shih, Y. L., T. Le, and L. Rothfield. 2003. Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles. Proc. Natl. Acad. Sci. USA 100:7865-7870.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 7865-7870
    • Shih, Y.L.1    Le, T.2    Rothfield, L.3
  • 52
    • 0018930187 scopus 로고
    • Defective and plaque-forming lambda transducing bacteriophage carrying penicillin-binding protein-cell shape genes: Genetic and physical mapping and identification of gene products from the lip-dacA-rodA-pbpA-leuS region of the Escherichia coli chromosome
    • Spratt, B. G., A. Boyd, and N. Stoker. 1980. Defective and plaque-forming lambda transducing bacteriophage carrying penicillin-binding protein-cell shape genes: genetic and physical mapping and identification of gene products from the lip-dacA-rodA-pbpA-leuS region of the Escherichia coli chromosome. J. Bacteriol. 143:569-581.
    • (1980) J. Bacteriol , vol.143 , pp. 569-581
    • Spratt, B.G.1    Boyd, A.2    Stoker, N.3
  • 53
    • 0016837552 scopus 로고
    • Penicillin-binding proteins and cell shape in E. coli
    • Spratt, B. G., and A. B. Pardee. 1975. Penicillin-binding proteins and cell shape in E. coli. Nature 254:516-517.
    • (1975) Nature , vol.254 , pp. 516-517
    • Spratt, B.G.1    Pardee, A.B.2
  • 54
    • 0033517146 scopus 로고    scopus 로고
    • A defect in cell wall recycling triggers autolysis during the stationary growth phase of Escherichia coli
    • Templin, M. F., A. Ursinus, and J. V. Höltje. 1999. A defect in cell wall recycling triggers autolysis during the stationary growth phase of Escherichia coli. EMBO J. 18:4108-4117.
    • (1999) EMBO J , vol.18 , pp. 4108-4117
    • Templin, M.F.1    Ursinus, A.2    Höltje, J.V.3
  • 55
    • 34547613915 scopus 로고    scopus 로고
    • An anhydro-N-acetylmuramyl-L-alanine amidase with broad specificity tethered to the outer membrane of Escherichia coli
    • Uehara, T., and J. T. Park. 2007. An anhydro-N-acetylmuramyl-L-alanine amidase with broad specificity tethered to the outer membrane of Escherichia coli. J. Bacteriol. 189:5634-5641.
    • (2007) J. Bacteriol , vol.189 , pp. 5634-5641
    • Uehara, T.1    Park, J.T.2
  • 56
    • 0036062233 scopus 로고    scopus 로고
    • Role of the murein precursor UDP-N-acetylmuramyl-L-Ala-γ-D-Glu-meso- diaminopimelic acid-D-Ala-D-Ala in repression of β-lactamase induction in cell division mutants
    • Uehara, T., and J. T. Park. 2002. Role of the murein precursor UDP-N-acetylmuramyl-L-Ala-γ-D-Glu-meso- diaminopimelic acid-D-Ala-D-Ala in repression of β-lactamase induction in cell division mutants. J. Bacteriol. 184:4233-4239.
    • (2002) J. Bacteriol , vol.184 , pp. 4233-4239
    • Uehara, T.1    Park, J.T.2
  • 57
    • 0027979985 scopus 로고
    • Purification and properties of a membrane-bound lytic transglycosylase from Escherichia coli
    • Ursinus, A., and J. V. Höltje. 1994. Purification and properties of a membrane-bound lytic transglycosylase from Escherichia coli. J. Bacteriol. 176: 338-343.
    • (1994) J. Bacteriol , vol.176 , pp. 338-343
    • Ursinus, A.1    Höltje, J.V.2
  • 58
    • 34248341732 scopus 로고    scopus 로고
    • Transmembrane transport of peptidoglycan precursors across model and bacterial membranes
    • van Dam, V., R. Sijbrandi, M. Kol, E. Swiezewska, B. de Kruijff, and E. Breukink. 2007. Transmembrane transport of peptidoglycan precursors across model and bacterial membranes. Mol. Microbiol. 64:1105-1114.
    • (2007) Mol. Microbiol , vol.64 , pp. 1105-1114
    • van Dam, V.1    Sijbrandi, R.2    Kol, M.3    Swiezewska, E.4    de Kruijff, B.5    Breukink, E.6
  • 59
    • 0035817819 scopus 로고    scopus 로고
    • Prokaryotic origin of the actin cytoskeleton
    • van den Ent, F., L. A. Amos, and J. Lowe. 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
  • 60
  • 61
    • 37349041697 scopus 로고    scopus 로고
    • Lipid intermediates in the biosynthesis of bacterial peptidoglycan
    • van Heijenoort, J. 2007. Lipid intermediates in the biosynthesis of bacterial peptidoglycan. Microbiol. Mol. Biol. Rev. 71:620-635.
    • (2007) Microbiol. Mol. Biol. Rev , vol.71 , pp. 620-635
    • van Heijenoort, J.1
  • 62
    • 0026623124 scopus 로고
    • Membrane intermediates in the peptidoglycan metabolism of Escherichia coli: Possible roles of PBP 1b and PBP 3
    • van Heijenoort, Y., M. Gómez, M. Derrien, J. Ayala, and J. van Heijenoort. 1992. Membrane intermediates in the peptidoglycan metabolism of Escherichia coli: possible roles of PBP 1b and PBP 3. J. Bacteriol. 174:3549-3557.
    • (1992) J. Bacteriol , vol.174 , pp. 3549-3557
    • van Heijenoort, Y.1    Gómez, M.2    Derrien, M.3    Ayala, J.4    van Heijenoort, J.5
  • 63
    • 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
  • 64
    • 4944246437 scopus 로고    scopus 로고
    • FtsZ collaborates with penicillin binding proteins to generate bacterial cell shape in Escherichia coli
    • 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.
    • (2004) J. Bacteriol , vol.186 , pp. 6768-6774
    • Varma, A.1    Young, K.D.2
  • 65
    • 50049104157 scopus 로고    scopus 로고
    • Vollmer, W., and U. Bertsche. 2007. Murein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli. Biochim. Biophys. Acta doi:10.1016/j.bbamem.2007.06.007.
    • Vollmer, W., and U. Bertsche. 2007. Murein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli. Biochim. Biophys. Acta doi:10.1016/j.bbamem.2007.06.007.
  • 66
    • 0034671524 scopus 로고    scopus 로고
    • Characterization of a β-N-acetylglucosaminidase of Escherichia coli and elucidation of its role in muropeptide recycling and β-lactamase induction
    • Vötsch, W., and M. F. Templin. 2000. Characterization of a β-N-acetylglucosaminidase of Escherichia coli and elucidation of its role in muropeptide recycling and β-lactamase induction. J. Biol. Chem. 275:39032-39038.
    • (2000) J. Biol. Chem , vol.275 , pp. 39032-39038
    • Vötsch, W.1    Templin, M.F.2
  • 67
    • 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
  • 68
    • 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., M. Doi, S. Tamaki, W. Park, S. Nakajima-Iijima, and M. Matsuhashi. 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
  • 69
    • 0015737203 scopus 로고
    • The direction of glycan synthesis in a bacterial peptidoglycan
    • Ward, J. B., and H. R. Perkins. 1973. The direction of glycan synthesis in a bacterial peptidoglycan. Biochem. J. 135:721-728.
    • (1973) Biochem. J , vol.135 , pp. 721-728
    • Ward, J.B.1    Perkins, H.R.2
  • 70
    • 0025873897 scopus 로고
    • On the role of the high molecular weight penicillin-binding proteins in the cell cycle of Escherichia coli
    • Wientjes, F. B., and N. Nanninga. 1991. On the role of the high molecular weight penicillin-binding proteins in the cell cycle of Escherichia coli. Res. Microbiol. 142:333-344.
    • (1991) Res. Microbiol , vol.142 , pp. 333-344
    • Wientjes, F.B.1    Nanninga, N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.