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Volumn 86, Issue 5, 2012, Pages 1036-1051

Three redundant murein endopeptidases catalyse an essential cleavage step in peptidoglycan synthesis of Escherichia coli K12

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDOGLYCAN; PROTEINASE; SPR PROTEIN; UNCLASSIFIED DRUG; YDHO PROTEIN; YEBA PROTEIN;

EID: 84870185885     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12058     Document Type: Article
Times cited : (163)

References (58)
  • 1
    • 18244415313 scopus 로고    scopus 로고
    • Evolutionary history, structural features and biochemical diversity of the NlpC/P60 superfamily of enzymes
    • Anantharaman, V., and Aravind, L. (2003) Evolutionary history, structural features and biochemical diversity of the NlpC/P60 superfamily of enzymes. Genome Biol 4: R11.
    • (2003) Genome Biol , vol.4
    • Anantharaman, V.1    Aravind, L.2
  • 2
    • 51849165615 scopus 로고    scopus 로고
    • Solution NMR structure of the NlpC/P60 domain of lipoprotein Spr from Escherichia coli: structural evidence for a novel cysteine peptidase catalytic triad
    • Aramini, J.M., Rossi, P., Huang, Y.J., Zhao, L., Jiang, M., Maglaqui, M., etal. (2008) Solution NMR structure of the NlpC/P60 domain of lipoprotein Spr from Escherichia coli: structural evidence for a novel cysteine peptidase catalytic triad. Biochemistry 47: 9715-9717.
    • (2008) Biochemistry , vol.47 , pp. 9715-9717
    • Aramini, J.M.1    Rossi, P.2    Huang, Y.J.3    Zhao, L.4    Jiang, M.5    Maglaqui, M.6
  • 3
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, single-gene knock-out mutants: the Keio collection
    • Baba, T., Ara, T., Hasegawa, M., Takai, Y., Okumura, Y., Baba, M., etal. (2006) Construction of Escherichia coli K-12 in-frame, single-gene knock-out mutants: the Keio collection. Mol Syst Biol 2: 2006.0008.
    • (2006) Mol Syst Biol , vol.2 , pp. 20060008
    • Baba, T.1    Ara, T.2    Hasegawa, M.3    Takai, Y.4    Okumura, Y.5    Baba, M.6
  • 4
    • 81755177857 scopus 로고    scopus 로고
    • Genetic interaction maps in Escherichia coli reveal functional crosstalk among cell envelope biogenesis pathways
    • Babu, M., Diaz-Mejia, J.J., Vlasblom, J., Gagarinova, A., Phanse, S., Graham, C., etal. (2011) Genetic interaction maps in Escherichia coli reveal functional crosstalk among cell envelope biogenesis pathways. PLoS Genet 7: e1002377.
    • (2011) PLoS Genet , vol.7
    • Babu, M.1    Diaz-Mejia, J.J.2    Vlasblom, J.3    Gagarinova, A.4    Phanse, S.5    Graham, C.6
  • 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. (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.4
  • 6
    • 2942538589 scopus 로고    scopus 로고
    • Screening for synthetic lethal mutants in Escherichia coli and identification of EnvC (YibP) as a periplasmic septal ring factor with murein hydrolase activity
    • Bernhardt, T.G., and de Boer, P.A. (2004) Screening for synthetic lethal mutants in Escherichia coli and identification of EnvC (YibP) as a periplasmic septal ring factor with murein hydrolase activity. Mol Microbiol 52: 1255-1269.
    • (2004) Mol Microbiol , vol.52 , pp. 1255-1269
    • Bernhardt, T.G.1    de Boer, P.A.2
  • 8
    • 0021337819 scopus 로고
    • Molecular model for elongation of the murein sacculus of Escherichia coli
    • Burman, L.G., and Park, J.T. (1984) Molecular model for elongation of the murein sacculus of Escherichia coli. Proc Natl Acad Sci USA 81: 1844-1848.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 1844-1848
    • Burman, L.G.1    Park, J.T.2
  • 9
    • 0020602206 scopus 로고
    • Evidence for multisite growth of Escherichia coli murein involving concomitant endopeptidase and transpeptidase activities
    • Burman, L.G., Reichler, J., and Park, J.T. (1983) Evidence for multisite growth of Escherichia coli murein involving concomitant endopeptidase and transpeptidase activities. J Bacteriol 156: 386-392.
    • (1983) J Bacteriol , vol.156 , pp. 386-392
    • Burman, L.G.1    Reichler, J.2    Park, J.T.3
  • 10
    • 33747837700 scopus 로고    scopus 로고
    • Actin homolog MreBH governs cell morphogenesis by localization of the cell wall hydrolase LytE
    • Carballido-Lopez, R., Formstone, A., Li, Y., Ehrlich, S.D., Noirot, P., and Errington, J. (2006) Actin homolog MreBH governs cell morphogenesis by localization of the cell wall hydrolase LytE. Dev Cell 11: 399-409.
    • (2006) Dev Cell , vol.11 , pp. 399-409
    • Carballido-Lopez, R.1    Formstone, A.2    Li, Y.3    Ehrlich, S.D.4    Noirot, P.5    Errington, J.6
  • 11
    • 76049128976 scopus 로고    scopus 로고
    • Rapid β-lactam-induced lysis requires successful assembly of the cell division machinery
    • Chung, H.S., Yao, Z., Goehring, N.W., Kishnoy, R., Beckwith, J., and Kahne, D. (2009) Rapid β-lactam-induced lysis requires successful assembly of the cell division machinery. Proc Natl Acad Sci USA 106: 21872-21877.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 21872-21877
    • Chung, H.S.1    Yao, Z.2    Goehring, N.W.3    Kishnoy, R.4    Beckwith, J.5    Kahne, D.6
  • 12
    • 0023782390 scopus 로고
    • Mode of peptidoglycan synthesis in Salmonella typhimurium: single-strand insertion
    • Cooper, S., Hsieh, M.L., and Guenther, B. (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
  • 13
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K.A., and Wanner, B.L. (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
  • 14
    • 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., Elf, P.K., Henderson, T.A., Nelson, D.E., and Young, K.D. (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
  • 15
    • 27744484159 scopus 로고    scopus 로고
    • Crystal structures of active LytM
    • Firczuk, M., Mucha, A., and Bochtler, M. (2005) Crystal structures of active LytM. J Mol Biol 354: 578-590.
    • (2005) J Mol Biol , vol.354 , pp. 578-590
    • Firczuk, M.1    Mucha, A.2    Bochtler, M.3
  • 16
    • 59649121975 scopus 로고    scopus 로고
    • RodZ, a new player in bacterial cell morphogenesis
    • Gerdes, K. (2009) RodZ, a new player in bacterial cell morphogenesis. EMBO J 28: 171-172.
    • (2009) EMBO J , vol.28 , pp. 171-172
    • Gerdes, K.1
  • 17
    • 0023765918 scopus 로고
    • Separation and quantification of muropeptides with high-performance liquid chromatography
    • Glauner, B. (1988) Separation and quantification of muropeptides with high-performance liquid chromatography. Anal Biochem 172: 451-464.
    • (1988) Anal Biochem , vol.172 , pp. 451-464
    • Glauner, B.1
  • 18
    • 0023677844 scopus 로고
    • The composition of the murein of Escherichia coli
    • Glauner, B., Holtje, J.V., and Schwarz, U. (1988) The composition of the murein of Escherichia coli. J Biol Chem 263: 10088-10095.
    • (1988) J Biol Chem , vol.263 , pp. 10088-10095
    • Glauner, B.1    Holtje, J.V.2    Schwarz, U.3
  • 19
    • 84455161264 scopus 로고    scopus 로고
    • AmpH, a bifunctional dd-endopeptidase and dd-carboxypeptidase of Escherichia coli
    • Gonzalez-Leiza, S.M., de Pedro, M.A., and Ayala, J.A. (2011) AmpH, a bifunctional dd-endopeptidase and dd-carboxypeptidase of Escherichia coli. J Bacteriol 193: 6887-6894.
    • (2011) J Bacteriol , vol.193 , pp. 6887-6894
    • Gonzalez-Leiza, S.M.1    de Pedro, M.A.2    Ayala, J.A.3
  • 20
    • 0021038807 scopus 로고
    • Cleavage and resynthesis of peptide cross-bridges in Escherichia coli murein
    • Goodell, E.W., and Schwarz, U. (1983) Cleavage and resynthesis of peptide cross-bridges in Escherichia coli murein. J Bacteriol 156: 136-140.
    • (1983) J Bacteriol , vol.156 , pp. 136-140
    • Goodell, E.W.1    Schwarz, U.2
  • 21
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose pBAD promoter
    • Guzman, L.M., BelD., Carson, M.J., and Beckwith, J. (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose pBAD promoter. J Bacteriol 177: 4121-4130.
    • (1995) J Bacteriol , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 22
    • 0029776767 scopus 로고    scopus 로고
    • Overproduction of penicillin-binding protein 7 suppresses thermosensitive growth defect at low osmolarity due to an spr mutation of Escherichia coli
    • Hara, H., Abe, N., Nakakouji, M., Nishimura, Y., and Horiuchi, K. (1996) Overproduction of penicillin-binding protein 7 suppresses thermosensitive growth defect at low osmolarity due to an spr mutation of Escherichia coli. Microb Drug Resist 2: 63-72.
    • (1996) Microb Drug Resist , vol.2 , pp. 63-72
    • Hara, H.1    Abe, N.2    Nakakouji, M.3    Nishimura, Y.4    Horiuchi, K.5
  • 23
    • 0016537405 scopus 로고
    • A rapid determination of sodium dodecyl sulfate with methylene blue
    • Hayashi, K. (1975) A rapid determination of sodium dodecyl sulfate with methylene blue. Anal Biochem 67: 503-506.
    • (1975) Anal Biochem , vol.67 , pp. 503-506
    • Hayashi, K.1
  • 24
    • 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., Ursinus, A., Berger, J., Schwarz, H., and Holtje, J.V. (2002) Effects of multiple deletions of murein hydrolases on viability, septum cleavage, and sensitivity to large toxic molecules in Escherichia coli. J Bacteriol 184: 2595-2602.
    • (2002) J Bacteriol , vol.184 , pp. 2595-2602
    • Heidrich, C.1    Ursinus, A.2    Berger, J.3    Schwarz, H.4    Holtje, J.V.5
  • 25
    • 84455162073 scopus 로고    scopus 로고
    • Peptidoglycan hydrolases of Escherichia coli
    • van Heijenoort, J. (2011) Peptidoglycan hydrolases of Escherichia coli. Microbiol Mol Biol Rev 75: 636-663.
    • (2011) Microbiol Mol Biol Rev , vol.75 , pp. 636-663
    • van Heijenoort, J.1
  • 26
    • 0002426524 scopus 로고
    • 'Three for one' - a simple growth mechanism that guarantees a precise copy of the throd-shaped sacculus of Escherichia coli
    • de Pedro, M.A., Holtje, J.V., and Loffelhardt, W. (eds). New York: Plenum Press
    • Holtje, J.V. (1993) 'Three for one' - a simple growth mechanism that guarantees a precise copy of the throd-shaped sacculus of Escherichia coli. In Bacterial Growth and Lysis. de Pedro, M.A., Holtje, J.V., and Loffelhardt, W. (eds). New York: Plenum Press, pp. 419-426.
    • (1993) Bacterial Growth and Lysis , pp. 419-426
    • Holtje, J.V.1
  • 27
    • 0029820401 scopus 로고    scopus 로고
    • A hypothetical holoenzyme involved in the replication of the murein sacculus of Escherichia coli
    • Holtje, J.V. (1996) A hypothetical holoenzyme involved in the replication of the murein sacculus of Escherichia coli. Microbiology 142: 1911-1918.
    • (1996) Microbiology , vol.142 , pp. 1911-1918
    • Holtje, J.V.1
  • 28
    • 0037858060 scopus 로고    scopus 로고
    • Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli
    • Holtje, 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
    • Holtje, J.V.1
  • 29
    • 0024458975 scopus 로고
    • Peptidoglycan synthesis during the cell cycle of Escherichia coli: composition and mode of insertion
    • de Jonge, B.L.M., Wientjes, F.B., Jurida, I., Driehuis, F., Wouters, J.T.M., and Nanninga, N. (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.M.1    Wientjes, F.B.2    Jurida, I.3    Driehuis, F.4    Wouters, J.T.M.5    Nanninga, N.6
  • 30
    • 0018677604 scopus 로고
    • Escherichia coli murein-DD-endopeptidase insensitive to β-lactam antibiotics
    • Keck, W., and Schwarz, U. (1979) Escherichia coli murein-DD-endopeptidase insensitive to β-lactam antibiotics. J Bacteriol 139: 770-774.
    • (1979) J Bacteriol , vol.139 , pp. 770-774
    • Keck, W.1    Schwarz, U.2
  • 31
    • 0035216867 scopus 로고    scopus 로고
    • Homogeneous expression of the pBAD promoter in Escherichia coli by constitutive expression of the low-affinity high-capacity AraE transporter
    • Khlebnikov, A., Datsenko, K.A., Skaug, T., Wanner, B.L., and Keasling, J.D. (2001) Homogeneous expression of the pBAD promoter in Escherichia coli by constitutive expression of the low-affinity high-capacity AraE transporter. Microbiology 147: 3241-3247.
    • (2001) Microbiology , vol.147 , pp. 3241-3247
    • Khlebnikov, A.1    Datsenko, K.A.2    Skaug, T.3    Wanner, B.L.4    Keasling, J.D.5
  • 32
    • 0025346080 scopus 로고
    • Additional arguments for the key role of 'smart' autolysins in the enlargement of the wall of Gram-negative bacteria
    • Koch, A.L. (1990) Additional arguments for the key role of 'smart' autolysins in the enlargement of the wall of Gram-negative bacteria. Res Microbiol 141: 529-541.
    • (1990) Res Microbiol , vol.141 , pp. 529-541
    • Koch, A.L.1
  • 33
    • 0032080539 scopus 로고    scopus 로고
    • The three-for-one model for Gram-negative wall growth: a problem and a possible solution
    • Koch, A.L. (1998) The three-for-one model for Gram-negative wall growth: a problem and a possible solution. FEMS Microbiol Lett 162: 127-134.
    • (1998) FEMS Microbiol Lett , vol.162 , pp. 127-134
    • Koch, A.L.1
  • 34
    • 0025817577 scopus 로고
    • Analysis of murein and murein precursors during antibiotic-induced lysis of Escherichia coli
    • Kohlrausch, U., and Holtje, J.V. (1991) Analysis of murein and murein precursors during antibiotic-induced lysis of Escherichia coli. J Bacteriol 173: 3425-3431.
    • (1991) J Bacteriol , vol.173 , pp. 3425-3431
    • Kohlrausch, U.1    Holtje, J.V.2
  • 35
    • 0026084885 scopus 로고
    • Penicillin-binding protein 4 of Escherichia coli: molecular cloning of the dacB gene, controlled overexpression, and alterations in murein composition
    • Korat, B., Mottl, H., and Keck, W. (1991) Penicillin-binding protein 4 of Escherichia coli: molecular cloning of the dacB gene, controlled overexpression, and alterations in murein composition. Mol Microbiol 5: 675-684.
    • (1991) Mol Microbiol , vol.5 , pp. 675-684
    • Korat, B.1    Mottl, H.2    Keck, W.3
  • 36
    • 34447538362 scopus 로고    scopus 로고
    • Overproduction of Penicillin-binding protein 2 and its inactive variants causes morphological changes and lysis in Escherichia coli
    • Legaree, B.A., Adams, C.B., and Clarke, A.J. (2007) Overproduction of Penicillin-binding protein 2 and its inactive variants causes morphological changes and lysis in Escherichia coli. J Bacteriol 189: 4975-4983.
    • (2007) J Bacteriol , vol.189 , pp. 4975-4983
    • Legaree, B.A.1    Adams, C.B.2    Clarke, A.J.3
  • 37
    • 10044294976 scopus 로고    scopus 로고
    • Endopeptidase penicillin-binding proteins 4 and 7 play an auxiliary role in determining uniform morphology of Escherichia coli
    • Meberg, B.M., Paulson, A.L., Priyadarshini, R., and Young, K.D. (2004) Endopeptidase penicillin-binding proteins 4 and 7 play an auxiliary role in determining uniform morphology of Escherichia coli. J Bacteriol 186: 8326-8336.
    • (2004) J Bacteriol , vol.186 , pp. 8326-8336
    • Meberg, B.M.1    Paulson, A.L.2    Priyadarshini, R.3    Young, K.D.4
  • 39
    • 0001985244 scopus 로고    scopus 로고
    • The murein sacculus
    • 2nd edn. Neidhardt, F.C., Curtiss, R., III, Ingraham, J.L., LE.C.C., Low, K.B., Magasanik, B., eds). Washington, DC: ASM press
    • Park, J.T. (1996) The murein sacculus. In Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd edn. Neidhardt, F.C., Curtiss, R., III, Ingraham, J.L., LE.C.C., Low, K.B., Magasanik, B., etal. (eds). Washington, DC: ASM press, pp. 48-57.
    • (1996) Escherichia coli and Salmonella: Cellular and Molecular Biology , pp. 48-57
    • Park, J.T.1
  • 41
    • 33746649568 scopus 로고    scopus 로고
    • Daughter cell separation by penicillin-binding proteins and peptidoglycan amidases in Escherichia coli
    • Priyadarshini, R., Popham, D.L., and Young, K.D. (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
  • 42
    • 0027991987 scopus 로고
    • Penicillin-binding protein 7/8 of Escherichia coli is a DD-endopeptidase
    • Romeis, T., and Holtje, J.V. (1994a) Penicillin-binding protein 7/8 of Escherichia coli is a DD-endopeptidase. Eur J Biochem 224: 597-604.
    • (1994) Eur J Biochem , vol.224 , pp. 597-604
    • Romeis, T.1    Holtje, J.V.2
  • 43
    • 0028016512 scopus 로고
    • Specific interaction of penicillin-binding proteins 3 and 7/8 with the soluble lytic transglycosylase in Escherichia coli
    • Romeis, T., and Holtje, J.V. (1994b) Specific interaction of penicillin-binding proteins 3 and 7/8 with the soluble lytic transglycosylase in Escherichia coli. J Biol Chem 269: 21603-21607.
    • (1994) J Biol Chem , vol.269 , pp. 21603-21607
    • Romeis, T.1    Holtje, J.V.2
  • 44
    • 84861126596 scopus 로고    scopus 로고
    • A widespread bacterial type VI secretion effector superfamily identified using a heuristic approach
    • Russel, A.B., Singh, P., Brittnacher, M., Bui, N.K., Hood, R.D., Carl, M.A., etal. (2012) A widespread bacterial type VI secretion effector superfamily identified using a heuristic approach. Cell Host Microbe 11: 538-549.
    • (2012) Cell Host Microbe , vol.11 , pp. 538-549
    • Russel, A.B.1    Singh, P.2    Brittnacher, M.3    Bui, N.K.4    Hood, R.D.5    Carl, M.A.6
  • 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
    • 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
  • 47
    • 0018338932 scopus 로고
    • The mechanism of the irreversible antimicrobial effects of penicillins: how the beta-lactam antibiotics kill and lyse bacteria
    • Tomasz, A. (1979) The mechanism of the irreversible antimicrobial effects of penicillins: how the beta-lactam antibiotics kill and lyse bacteria. Annu Rev Microbiol 33: 113-137.
    • (1979) Annu Rev Microbiol , vol.33 , pp. 113-137
    • Tomasz, A.1
  • 48
    • 0002249336 scopus 로고
    • Building and breaking of bonds in the cell wall of bacteria - the role for autolysins
    • Nombela, C. (ed.). Amsterdam: Elsevier Science Publishers
    • Tomasz, A. (1984) Building and breaking of bonds in the cell wall of bacteria - the role for autolysins. In Microbial Cell Wall Synthesis and Autolysis. Nombela, C. (ed.). Amsterdam: Elsevier Science Publishers, pp. 3-12.
    • (1984) Microbial Cell Wall Synthesis and Autolysis , pp. 3-12
    • Tomasz, A.1
  • 49
    • 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. (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
  • 50
    • 67749117916 scopus 로고    scopus 로고
    • LytM-domain factors are required for daughter cell separation and rapid ampicillin-induced lysis in Escherichia coli
    • Uehara, T., Dinh, T., and Bernhardt, T.G. (2009) LytM-domain factors are required for daughter cell separation and rapid ampicillin-induced lysis in Escherichia coli. J Bacteriol 191: 5094-5107.
    • (2009) J Bacteriol , vol.191 , pp. 5094-5107
    • Uehara, T.1    Dinh, T.2    Bernhardt, T.G.3
  • 51
    • 77951470447 scopus 로고    scopus 로고
    • Daughter cell-separation is controlled by cytokinetic ring-activated cell wall hydrolysis
    • Uehara, T., Parzych, K.R., Dinh, T., and Bernhardt, T.G. (2010) Daughter cell-separation is controlled by cytokinetic ring-activated cell wall hydrolysis. EMBO J 29: 1412-1422.
    • (2010) EMBO J , vol.29 , pp. 1412-1422
    • Uehara, T.1    Parzych, K.R.2    Dinh, T.3    Bernhardt, T.G.4
  • 52
    • 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
    • 84873775015 scopus 로고
    • Bagshaped macromolecules - a new outlook on bacterial cell walls
    • Weidel, W., and Pelzer, H. (1964) Bagshaped macromolecules - a new outlook on bacterial cell walls. Adv Enzymol 26: 193-232.
    • (1964) Adv Enzymol , vol.26 , pp. 193-232
    • Weidel, W.1    Pelzer, H.2
  • 57
    • 0022341427 scopus 로고
    • Kinetics of uptake and incorporation of meso-diaminopimelic acid in different Escherichia coli strains
    • Wientjes, F.B., Evelien, P., Taschner, P.E.M., and Woldringh, C.L. (1985) Kinetics of uptake and incorporation of meso-diaminopimelic acid in different Escherichia coli strains. J Bacteriol 164: 331-337.
    • (1985) J Bacteriol , vol.164 , pp. 331-337
    • Wientjes, F.B.1    Evelien, P.2    Taschner, P.E.M.3    Woldringh, C.L.4
  • 58
    • 84864816426 scopus 로고    scopus 로고
    • A conformational switch controls cell wall remodeling enzymes required for bacterial cell division
    • Yang, D.C., Tan, K., Joachimiak, A., and Bernhardt, T.G. (2012) A conformational switch controls cell wall remodeling enzymes required for bacterial cell division. Mol Microbiol 85: 768-781.
    • (2012) Mol Microbiol , vol.85 , pp. 768-781
    • Yang, D.C.1    Tan, K.2    Joachimiak, A.3    Bernhardt, T.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.