메뉴 건너뛰기




Volumn 61, Issue 3, 2006, Pages 675-690

Interaction between two murein (peptidoglycan) synthases, PBP3 and PBP1B, in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; GAMMA GLUTAMYLTRANSFERASE; GLYCOSYLTRANSFERASE; HISTIDINE; PBP1B ENZYME; PBP3 ENZYME; PEPTIDOGLYCAN SYNTHASE ENZYME; SEPHAROSE; UNCLASSIFIED DRUG;

EID: 33748333182     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2006.05280.x     Document Type: Article
Times cited : (151)

References (69)
  • 2
    • 0344603819 scopus 로고    scopus 로고
    • Identification of two penicillin-binding multienzyme complexes in Haemophilus influenzae
    • Alaedini, A., and Day, R.A. (1999) Identification of two penicillin-binding multienzyme complexes in Haemophilus influenzae. Biochem Biophys Res Commun 264: 191-195.
    • (1999) Biochem Biophys Res Commun , vol.264 , pp. 191-195
    • Alaedini, A.1    Day, R.A.2
  • 3
    • 1342325471 scopus 로고    scopus 로고
    • Role of class A penicillin-binding proteins in PBP5-mediated beta-lactam resistance in Enterococcus faecalis
    • Arbeloa, A., Segal, H., Hugonnet, J.E., Josseaume, N., Dubost, L., Brouard, J.P., et al. (2004) Role of class A penicillin-binding proteins in PBP5-mediated beta-lactam resistance in Enterococcus faecalis. J Bacteriol 186: 1221-1228.
    • (2004) J Bacteriol , vol.186 , pp. 1221-1228
    • Arbeloa, A.1    Segal, H.2    Hugonnet, J.E.3    Josseaume, N.4    Dubost, L.5    Brouard, J.P.6
  • 4
    • 27844575191 scopus 로고    scopus 로고
    • In vitro murein (peptidoglycan) synthesis by dimers of the bifunctional transglycosylase-transpeptidase PBP1B from Escherichia coli
    • Bertsche, U., Breukink, E., Kast, T., and Vollmer, W. (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
  • 5
    • 0024542299 scopus 로고
    • Preparation and characterization of monoclonal antibodies against native membrane-bound penicillin-binding protein 1B of Escherichia coli
    • den Blaauwen, T., Wientjes, F.B., Kolk, A.H., Spratt, B.G., and Nanninga, N. (1989) Preparation and characterization of monoclonal antibodies against native membrane-bound penicillin-binding protein 1B of Escherichia coli. J Bacteriol 171: 1394-1401.
    • (1989) J Bacteriol , vol.171 , pp. 1394-1401
    • Den Blaauwen, T.1    Wientjes, F.B.2    Kolk, A.H.3    Spratt, B.G.4    Nanninga, N.5
  • 6
    • 0025602827 scopus 로고
    • Mapping of conformational epitopes of monoclonal antibodies against Escherichia coli penicillin-binding protein 1B (PBP 1B) by means of hybrid protein analysis: Implications for the tertiary structure of PBP 1B
    • den Blaauwen, T., Pas, E., Edelman, A., Spratt, B.G., and Nanninga, N. (1990a) Mapping of conformational epitopes of monoclonal antibodies against Escherichia coli penicillin-binding protein 1B (PBP 1B) by means of hybrid protein analysis: implications for the tertiary structure of PBP 1B. J Bacteriol 172: 7284-7288.
    • (1990) J Bacteriol , vol.172 , pp. 7284-7288
    • Den Blaauwen, T.1    Pas, E.2    Edelman, A.3    Spratt, B.G.4    Nanninga, N.5
  • 7
    • 0025020741 scopus 로고
    • Interaction of monoclonal antibodies with the enzymatic domains of penicillin-binding protein 1b of Escherichia coli
    • den Blaauwen, T., Aarsman, M., and Nanninga, N. (1990b) Interaction of monoclonal antibodies with the enzymatic domains of penicillin-binding protein 1b of Escherichia coli. J Bacteriol 172: 63-70.
    • (1990) J Bacteriol , vol.172 , pp. 63-70
    • Den Blaauwen, T.1    Aarsman, M.2    Nanninga, N.3
  • 8
    • 0035724314 scopus 로고    scopus 로고
    • Distribution of the Escherichia coli structural maintenance of chromosomes (SMC)-like protein MukB in the cell
    • den Blaauwen, T., Lindqvist, A., Löwe, J., and Nanninga, N. (2001) Distribution of the Escherichia coli structural maintenance of chromosomes (SMC)-like protein MukB in the cell. Mol Microbiol 42: 1179-1188.
    • (2001) Mol Microbiol , vol.42 , pp. 1179-1188
    • Den Blaauwen, T.1    Lindqvist, A.2    Löwe, J.3    Nanninga, N.4
  • 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
  • 10
    • 0021906412 scopus 로고
    • Production of thiol-penicillin-binding protein 3 of Escherichia coli using a two primer method of site-directed mutagenesis
    • Broome-Smith, J.K., Hedge, P.J., and Spratt, B.G. (1985) Production of thiol-penicillin-binding protein 3 of Escherichia coli using a two primer method of site-directed mutagenesis. EMBO J 4: 231-235.
    • (1985) EMBO J , vol.4 , pp. 231-235
    • Broome-Smith, J.K.1    Hedge, P.J.2    Spratt, B.G.3
  • 11
    • 2942570076 scopus 로고    scopus 로고
    • A complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal region
    • Buddelmeijer, N., and Beckwith, J. (2004) A complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal region. Mol Microbiol 52: 1315-1327.
    • (2004) Mol Microbiol , vol.52 , pp. 1315-1327
    • Buddelmeijer, N.1    Beckwith, J.2
  • 12
    • 0018956590 scopus 로고
    • Analysis of gene control signals by DNA fusion and cloning in Escherichia coli
    • Casabadan, M.J., and Cohen, S.N. (1980) Analysis of gene control signals by DNA fusion and cloning in Escherichia coli. J Mol Biol 138: 179-207.
    • (1980) J Mol Biol , vol.138 , pp. 179-207
    • Casabadan, M.J.1    Cohen, S.N.2
  • 13
    • 0036280067 scopus 로고    scopus 로고
    • Penicillin-binding proteins 1a and 1b form independent dimers in Escherichia coli
    • Charpentier, X., Chalut, C., Remy, M.H., and Masson, J.M. (2002) Penicillin-binding proteins 1a and 1b form independent dimers in Escherichia coli. J Bacteriol 184: 3749-3752.
    • (2002) J Bacteriol , vol.184 , pp. 3749-3752
    • Charpentier, X.1    Chalut, C.2    Remy, M.H.3    Masson, J.M.4
  • 14
    • 0034740520 scopus 로고    scopus 로고
    • FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co-localization with FtsZ during Escherichia coli cell division
    • Chen, J.C., and Beckwith, J. (2001) FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co-localization with FtsZ during Escherichia coli cell division. Mol Microbiol 42: 395-413.
    • (2001) Mol Microbiol , vol.42 , pp. 395-413
    • Chen, J.C.1    Beckwith, J.2
  • 15
    • 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, B.D., Geissler, B., Sadasivam, M., and 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
  • 16
    • 0026697767 scopus 로고
    • The proper ratio of FtsZ to FtsA is required for cell division to occur in Escherichia coli
    • Dai, K., and Lutkenhaus, J. (1992) The proper ratio of FtsZ to FtsA is required for cell division to occur in Escherichia coli. J Bacteriol 174: 6145-6151.
    • (1992) J Bacteriol , vol.174 , pp. 6145-6151
    • Dai, K.1    Lutkenhaus, J.2
  • 17
    • 0028231058 scopus 로고
    • Use of biotinylated beta-lactams and chemiluminescence for study and purification of penicillin-binding proteins in bacteria
    • Dargis, M., and Malouin, F. (1994) Use of biotinylated beta-lactams and chemiluminescence for study and purification of penicillin-binding proteins in bacteria. Antimicrob Agents Chemother 38: 973-980.
    • (1994) Antimicrob Agents Chemother , vol.38 , pp. 973-980
    • Dargis, M.1    Malouin, F.2
  • 18
    • 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
  • 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., Ogorzalek Loo, R.R., Xie, Y., Loo, J.A., and Gober, J.W. (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    Ogorzalek Loo, R.R.2    Xie, Y.3    Loo, J.A.4    Gober, J.W.5
  • 20
    • 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
  • 21
    • 0037701641 scopus 로고    scopus 로고
    • Probing the catalytic activity of a cell division-specific transpeptidase in vivo with beta-lactams
    • Eberhardt, C., Kuerschner, L., and Weiss, D.S. (2003) Probing the catalytic activity of a cell division-specific transpeptidase in vivo with beta-lactams. J Bacteriol 185: 3726-3734.
    • (2003) J Bacteriol , vol.185 , pp. 3726-3734
    • Eberhardt, C.1    Kuerschner, L.2    Weiss, D.S.3
  • 22
    • 0023370184 scopus 로고
    • Use of β-lactamase fusion vector to investigate the organization of the penicillin-binding protein 1B in the cytoplasmic membrane of Escherichia coli
    • Edelman, A., Bowler, L., Broome-Smith, J.K., and Spratt, B.G. (1987) Use of β-lactamase fusion vector to investigate the organization of the penicillin-binding protein 1B in the cytoplasmic membrane of Escherichia coli. Mol Microbiol 1: 101-106.
    • (1987) Mol Microbiol , vol.1 , pp. 101-106
    • Edelman, A.1    Bowler, L.2    Broome-Smith, J.K.3    Spratt, B.G.4
  • 23
    • 1542616355 scopus 로고    scopus 로고
    • MreB, the cell shape-determining bacterial actin homologue, co-ordinates cell wall morphogenesis in Caulobacter crescentus
    • Figge, R.M., Divakaruni, A.V., and Gober, J.W. (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
  • 25
    • 13944282888 scopus 로고    scopus 로고
    • Activation for catalysis of penicillin-binding protein 2a from methicillin-resistant Staphylococcus aureus by bacterial cell wall
    • Fuda, C., Hesek, D., Lee, M., Morio, K., Nowak, T., and Mobashery, S. (2005) Activation for catalysis of penicillin-binding protein 2a from methicillin-resistant Staphylococcus aureus by bacterial cell wall. J Am Chem Soc 127: 2056-2057.
    • (2005) J Am Chem Soc , vol.127 , pp. 2056-2057
    • Fuda, C.1    Hesek, D.2    Lee, M.3    Morio, K.4    Nowak, T.5    Mobashery, S.6
  • 26
    • 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 de Pedro, M.A. (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.
    • (1990) J Bacteriol , vol.172 , pp. 5863-5870
    • Garcia Del Portillo, F.1    De Pedro, M.A.2
  • 27
    • 0025987074 scopus 로고
    • Identification of a new mutation in Escherichia coli that suppresses a pbpB (Ts) phenotype in the presence of penicillin-binding protein 1B
    • Garcia del Portillo, F., de Pedro, M.A., and Ayala, J.A. (1991) Identification of a new mutation in Escherichia coli that suppresses a pbpB (Ts) phenotype in the presence of penicillin-binding protein 1B. FEMS Microbiol Lett 68: 7-13.
    • (1991) FEMS Microbiol Lett , vol.68 , pp. 7-13
    • Garcia Del Portillo, F.1    De Pedro, M.A.2    Ayala, J.A.3
  • 28
    • 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
  • 29
    • 0031736387 scopus 로고    scopus 로고
    • Multimodular penicillin-binding proteins: An enigmatic family of orthologs and paralogs
    • Goffin, C., and Ghuysen, J.M. (1998) Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs. Microbiol Mol Biol Rev 62: 1079-1093.
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 1079-1093
    • Goffin, C.1    Ghuysen, J.M.2
  • 30
    • 0029808359 scopus 로고    scopus 로고
    • The non-penicillin-binding module of the tripartite penicillin-binding protein 3 of Escherichia coli is required for folding and/or stability of the penicillin-binding module and the membrane-anchoring module confers cell septation activity on the folded structure
    • Goffin, C., Fraipont, C., Ayala, J., Terrak, M., Nguyen-Disteche, M., and Ghuysen, J.M. (1996) The non-penicillin-binding module of the tripartite penicillin-binding protein 3 of Escherichia coli is required for folding and/or stability of the penicillin-binding module and the membrane-anchoring module confers cell septation activity on the folded structure. J Bacteriol 178: 5402-5409.
    • (1996) J Bacteriol , vol.178 , pp. 5402-5409
    • Goffin, C.1    Fraipont, C.2    Ayala, J.3    Terrak, M.4    Nguyen-Disteche, M.5    Ghuysen, J.M.6
  • 31
    • 0002426524 scopus 로고
    • 'Three for one' - A simple growth mechanism that guarantees a precise copy of the thin, rod-shaped murein sacculus of Escherichia coli
    • de Pedro, M.A., Höltje, J.V., and Löffelhardt, W. (eds). London: Plenum Press
    • Höltje, J.V. (1993) 'Three for one' - A simple growth mechanism that guarantees a precise copy of the thin, rod-shaped murein sacculus of Escherichia coli. In Bacterial Growth and Lysis-Metabolism and Structure of the Bacterial Sacculus. de Pedro, M.A., Höltje, J.V., and Löffelhardt, W. (eds). London: Plenum Press, pp. 419-426.
    • (1993) Bacterial Growth and Lysis-Metabolism and Structure of the Bacterial Sacculus , pp. 419-426
    • Höltje, J.V.1
  • 32
    • 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
  • 33
    • 0032885217 scopus 로고    scopus 로고
    • Delayed nucleoid segregation in Escherichia coli
    • Huls, P.G., Vischer, N.O., and Woldringh, C.L. (1999) Delayed nucleoid segregation in Escherichia coli. Mol Microbiol 33: 959-970.
    • (1999) Mol Microbiol , vol.33 , pp. 959-970
    • Huls, P.G.1    Vischer, N.O.2    Woldringh, C.L.3
  • 34
    • 0034687698 scopus 로고    scopus 로고
    • Identification of motifs in cholera toxin A1 polypeptide that are required for its interaction with human ADP-ribosylation factor 6 in a bacterial two-hybrid system
    • Jobling, M.G., and Holmes, R.K. (2000) Identification of motifs in cholera toxin A1 polypeptide that are required for its interaction with human ADP-ribosylation factor 6 in a bacterial two-hybrid system. Proc Natl Acad Sci USA 97: 14662-14667.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 14662-14667
    • Jobling, M.G.1    Holmes, R.K.2
  • 35
    • 0032510783 scopus 로고    scopus 로고
    • A bacterial two-hybrid system based on a reconstituted signal transduction pathway
    • Karimova, G., Pidoux, J., Ullmann, A., and Ladant, D. (1998) A bacterial two-hybrid system based on a reconstituted signal transduction pathway. Proc Natl Acad Sci USA 95: 5752-5756.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5752-5756
    • Karimova, G.1    Pidoux, J.2    Ullmann, A.3    Ladant, D.4
  • 36
    • 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., and 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
  • 37
    • 0021198846 scopus 로고
    • Overlapping of the coding regions for alpha and gamma components of penicillin-binding protein 1b in Escherichia coli
    • Kato, J., Suzuki, H., and Hirota, Y. (1984) Overlapping of the coding regions for alpha and gamma components of penicillin-binding protein 1b in Escherichia coli. Mol Gen Genet 196: 449-457.
    • (1984) Mol Gen Genet , vol.196 , pp. 449-457
    • Kato, J.1    Suzuki, H.2    Hirota, Y.3
  • 38
    • 0021862671 scopus 로고
    • Dispensability of either penicillin-binding protein-1a or -1b involved in the essential process for cell elongation in Escherichia coli
    • Kato, J., Suzuki, H., and Hirota, Y. (1985) Dispensability of either penicillin-binding protein-1a or -1b involved in the essential process for cell elongation in Escherichia coli. Mol Gen Genet 200: 272-277.
    • (1985) Mol Gen Genet , vol.200 , pp. 272-277
    • Kato, J.1    Suzuki, H.2    Hirota, Y.3
  • 39
    • 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., et al. (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
  • 40
    • 0023245332 scopus 로고
    • Two distinct transpeptidation reactions during murein synthesis in Escherichia coli
    • Kraus, W., and Höltje, J.-V. (1987) Two distinct transpeptidation reactions during murein synthesis in Escherichia coli. J Bacteriol 169: 3099-3103.
    • (1987) J Bacteriol , vol.169 , pp. 3099-3103
    • Kraus, W.1    Höltje, J.-V.2
  • 41
    • 0016841078 scopus 로고
    • Electrophoretic resolution of the 'major outer membrane protein' of Escherichia coli K12 into four bands
    • Lutgenberg, B.J., Meijers, J., Peters, R., van der Hoek, P., and van Alphen, L. (1975) Electrophoretic resolution of the 'major outer membrane protein' of Escherichia coli K12 into four bands. FEBS Lett 58: 254-258.
    • (1975) FEBS Lett , vol.58 , pp. 254-258
    • Lutgenberg, B.J.1    Meijers, J.2    Peters, R.3    Van Der Hoek, P.4    Van Alphen, L.5
  • 42
    • 14144256353 scopus 로고    scopus 로고
    • Active site restructuring regulates ligand recognition in class A penicillin-binding proteins
    • Macheboeuf, P., Di Guilmi, A.M., Job, V., Vernet, T., Dideberg, O., and Dessen, A. (2005) Active site restructuring regulates ligand recognition in class A penicillin-binding proteins. Proc Natl Acad Sci USA 102: 577-582.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 577-582
    • Macheboeuf, P.1    Di Guilmi, A.M.2    Job, V.3    Vernet, T.4    Dideberg, O.5    Dessen, A.6
  • 43
    • 0033812829 scopus 로고    scopus 로고
    • Differential functionalities of amphiphilic peptide segments of the cell-septation penicillin-binding protein 3 of Escherichia coli
    • Marrec-Fairley, M., Piette, A., Gallet, X., Brasseur, R., Hara, H., Fraipont, C., et al. (2000) Differential functionalities of amphiphilic peptide segments of the cell-septation penicillin-binding protein 3 of Escherichia coli. Mol Microbiol 37: 1019-1031.
    • (2000) Mol Microbiol , vol.37 , pp. 1019-1031
    • Marrec-Fairley, M.1    Piette, A.2    Gallet, X.3    Brasseur, R.4    Hara, H.5    Fraipont, C.6
  • 44
    • 0025120340 scopus 로고
    • Machinery for cell growth and division: Penicillin-binding proteins and other proteins
    • Matsuhashi, M., Wachi, M., and Ishino, F. (1990) Machinery for cell growth and division: penicillin-binding proteins and other proteins. Res Microbiol 141: 89-103.
    • (1990) Res Microbiol , vol.141 , pp. 89-103
    • Matsuhashi, M.1    Wachi, M.2    Ishino, F.3
  • 45
    • 0041836122 scopus 로고    scopus 로고
    • Overproduction of inactive variants of the murein synthase PBP1B causes lysis in Escherichia coli
    • Meisel, U., Höltje, J.V., and Vollmer, W. (2003) Overproduction of inactive variants of the murein synthase PBP1B causes lysis in Escherichia coli. J Bacteriol 185: 5342-5348.
    • (2003) J Bacteriol , vol.185 , pp. 5342-5348
    • Meisel, U.1    Höltje, J.V.2    Vollmer, W.3
  • 46
    • 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
  • 47
  • 50
    • 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    Fraipont, C.2    Den Blaauwen, T.3    Aarsman, M.E.4    Pastoret, S.5    Nguyen-Disteche, M.6
  • 51
    • 13444259776 scopus 로고    scopus 로고
    • Recruitment of penicillin-binding protein PBP2 to the division site of Staphylococcus aureus is dependent on its transpeptidation substrates
    • Pinho, M.G., and Errington, J. (2005) Recruitment of penicillin-binding protein PBP2 to the division site of Staphylococcus aureus is dependent on its transpeptidation substrates. Mol Microbiol 55: 799-807.
    • (2005) Mol Microbiol , vol.55 , pp. 799-807
    • Pinho, M.G.1    Errington, J.2
  • 52
    • 0035845487 scopus 로고    scopus 로고
    • An acquired and a native penicillin-binding protein cooperate in building the cell wall of drug-resistant staphylococci
    • Pinho, M.G., de Lencastre, H., and Tomasz, A. (2001) An acquired and a native penicillin-binding protein cooperate in building the cell wall of drug-resistant staphylococci. Proc Natl Acad Sci USA 98: 10886-10891.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10886-10891
    • Pinho, M.G.1    De Lencastre, H.2    Tomasz, A.3
  • 53
    • 0022489523 scopus 로고
    • Activity of penicillin-binding protein 3 from Escherichia coli
    • Pisabarro, A.G., Prats, R., Vaquez, D., and Rodriguez-Tebar, A. (1986) Activity of penicillin-binding protein 3 from Escherichia coli. J Bacteriol 168: 199-206.
    • (1986) J Bacteriol , vol.168 , pp. 199-206
    • Pisabarro, A.G.1    Prats, R.2    Vaquez, D.3    Rodriguez-Tebar, A.4
  • 54
    • 0028016512 scopus 로고
    • Specific interaction of penicillin-binding proteins 3 and 7/8 with soluble lytic transglycosylase in Escherichia coli
    • Romeis, T., and Höltje, J.V. (1994) Specific interaction of penicillin-binding proteins 3 and 7/8 with soluble lytic transglycosylase in Escherichia coli. J Biol Chem 269: 21603-21607.
    • (1994) J Biol Chem , vol.269 , pp. 21603-21607
    • Romeis, T.1    Höltje, J.V.2
  • 55
    • 3242759827 scopus 로고    scopus 로고
    • PBP1 is a component of the Bacillus subtilis cell division machinery
    • Scheffers, D.J., and Errington, J. (2004) PBP1 is a component of the Bacillus subtilis cell division machinery. J Bacteriol 186: 5153-5156.
    • (2004) J Bacteriol , vol.186 , pp. 5153-5156
    • Scheffers, D.J.1    Errington, J.2
  • 56
    • 1242320297 scopus 로고    scopus 로고
    • Several distinct localization patterns for penicillin-binding proteins in Bacillus subtilis
    • Scheffers, D.J., Jones, L.J., and Errington, J. (2004) Several distinct localization patterns for penicillin-binding proteins in Bacillus subtilis. Mol Microbiol 51: 749-764.
    • (2004) Mol Microbiol , vol.51 , pp. 749-764
    • Scheffers, D.J.1    Jones, L.J.2    Errington, J.3
  • 57
    • 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
  • 58
    • 0022155718 scopus 로고
    • Discovery and development of the monobactams
    • Sykes, R.B., and Bonner, D.P. (1985) Discovery and development of the monobactams. Rev Infect Dis 7 (Suppl. 4): S579-S593.
    • (1985) Rev Infect Dis , vol.7 , Issue.4 SUPPL.
    • Sykes, R.B.1    Bonner, D.P.2
  • 59
    • 0017679507 scopus 로고
    • Thermosensitive mutation in Escherichia coli simultaneously causing defects in penicillin-binding protein-1Bs and in enzyme activity for peptidoglycan synthesis in vitro
    • Tamaki, S., Nakajima, S., and Matsuhashi, M. (1977) Thermosensitive mutation in Escherichia coli simultaneously causing defects in penicillin-binding protein-1Bs and in enzyme activity for peptidoglycan synthesis in vitro. Proc Natl Acad Sci USA 74: 5472-5476.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 5472-5476
    • Tamaki, S.1    Nakajima, S.2    Matsuhashi, M.3
  • 60
    • 0023147125 scopus 로고
    • Genetic and morphological characterization of ftsB and nrdB mutants of Escherichia coli
    • Taschner, P.E., Verest, J.G., and Woldringh, C.L. (1987) Genetic and morphological characterization of ftsB and nrdB mutants of Escherichia coli. J Bacteriol 169: 19-25.
    • (1987) J Bacteriol , vol.169 , pp. 19-25
    • Taschner, P.E.1    Verest, J.G.2    Woldringh, C.L.3
  • 61
    • 0024095422 scopus 로고
    • An amino acid substitution in penicillin-binding protein 3 creates pointed polar caps in Escherichia coli
    • Taschner, P.E.M., Ypenburg, N., Spratt, B.G., and Woldringh, C.L. (1988) An amino acid substitution in penicillin-binding protein 3 creates pointed polar caps in Escherichia coli. J Bacteriol 170: 4828-4837.
    • (1988) J Bacteriol , vol.170 , pp. 4828-4837
    • Taschner, P.E.M.1    Ypenburg, N.2    Spratt, B.G.3    Woldringh, C.L.4
  • 62
    • 0032874101 scopus 로고    scopus 로고
    • The catalytic, glycosyl transferase and acyl transferase modules of the cell wall peptidoglycan-polymerizing penicillin-binding protein 1b of Escherichia coli
    • Terrak, M., Ghosh, T.K., van Heijenoort, J., Van Beeumen, J., Lampilas, M., Aszodi, J., et al. (1999) The catalytic, glycosyl transferase and acyl transferase modules of the cell wall peptidoglycan-polymerizing penicillin-binding protein 1b of Escherichia coli. Mol Microbiol 34: 350-364.
    • (1999) Mol Microbiol , vol.34 , pp. 350-364
    • Terrak, M.1    Ghosh, T.K.2    Van Heijenoort, J.3    Van Beeumen, J.4    Lampilas, M.5    Aszodi, J.6
  • 63
    • 0033525526 scopus 로고    scopus 로고
    • Demonstration of molecular interactions between the murein polymerase PBP1B, the lytic transglycosylase MltA, and the scaffolding protein MipA of Escherichia coli
    • Vollmer, W., von Rechenberg, M., and Höltje, J.V. (1999) Demonstration of molecular interactions between the murein polymerase PBP1B, the lytic transglycosylase MltA, and the scaffolding protein MipA of Escherichia coli. J Biol Chem 274: 6726-6734.
    • (1999) J Biol Chem , vol.274 , pp. 6726-6734
    • Vollmer, W.1    Von Rechenberg, M.2    Höltje, J.V.3
  • 64
    • 25144481661 scopus 로고    scopus 로고
    • Dancing around the divisome: Asymmetric chromosome segregation in Escherichia coli
    • Wang, X., Possoz, C., and Sherratt, D.J. (2005) Dancing around the divisome: asymmetric chromosome segregation in Escherichia coli. Genes Dev 19: 2367-2377.
    • (2005) Genes Dev , vol.19 , pp. 2367-2377
    • Wang, X.1    Possoz, C.2    Sherratt, D.J.3
  • 65
    • 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
  • 66
    • 0030881627 scopus 로고    scopus 로고
    • Localization of the Escherichia coli cell division protein FtsI (PBP3) to the division site and cell pole
    • Weiss, D.S., Pogliano, K., Carson, M., Guzman, L.M., Fraipont, C., Nguyen-Disteche, M., et al. (1997) Localization of the Escherichia coli cell division protein FtsI (PBP3) to the division site and cell pole. Mol Microbiol 25: 671-681.
    • (1997) Mol Microbiol , vol.25 , pp. 671-681
    • Weiss, D.S.1    Pogliano, K.2    Carson, M.3    Guzman, L.M.4    Fraipont, C.5    Nguyen-Disteche, M.6
  • 67
    • 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
  • 68
    • 0347915664 scopus 로고    scopus 로고
    • Genetic analysis of the cell division protein FtsI (PBP3): Amino acid substitutions that impair septal localization of FtsI and recruitment of FtsN
    • Wissel, M.C., and Weiss, D.S. (2004) Genetic analysis of the cell division protein FtsI (PBP3): amino acid substitutions that impair septal localization of FtsI and recruitment of FtsN. J Bacteriol 186: 490-502.
    • (2004) J Bacteriol , vol.186 , pp. 490-502
    • Wissel, M.C.1    Weiss, D.S.2
  • 69
    • 0025990145 scopus 로고
    • Penicillin-binding protein 1B of Escherichia coli exists in dimeric forms
    • Zijderveld, C.A., Aarsman, M.E., den Blaauwen, T., and Nanninga, N. (1991) Penicillin-binding protein 1B of Escherichia coli exists in dimeric forms. J Bacteriol 173: 5740-5746.
    • (1991) J Bacteriol , vol.173 , pp. 5740-5746
    • Zijderveld, C.A.1    Aarsman, M.E.2    Den Blaauwen, T.3    Nanninga, N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.