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Volumn 51, Issue 3, 2004, Pages 749-764

Several distinct localization patterns for penicillin-binding proteins in Bacillus subtilis

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; GREEN FLUORESCENT PROTEIN; PENICILLIN BINDING PROTEIN;

EID: 1242320297     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2003.03854.x     Document Type: Article
Times cited : (124)

References (57)
  • 1
    • 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
  • 2
    • 0001134202 scopus 로고
    • Requirements for transformation in Bacillus subtilis
    • Anagnostopoulos, C., and Spizizen, J. (1961) Requirements for transformation in Bacillus subtilis. J Bacteriol 81: 741-746.
    • (1961) J Bacteriol , vol.81 , pp. 741-746
    • Anagnostopoulos, C.1    Spizizen, J.2
  • 3
    • 0032985757 scopus 로고    scopus 로고
    • Analysis of peptidoglycan structure from vegetative cells of Bacillus subtilis 168 and role of PBP 5 in peptidoglycan maturation
    • Atrih, A., Bacher, G., Allmaier, G., Williamson, M.P., and Foster, S.J. (1999) Analysis of peptidoglycan structure from vegetative cells of Bacillus subtilis 168 and role of PBP 5 in peptidoglycan maturation. J Bacteriol 181: 3956-3966.
    • (1999) J Bacteriol , vol.181 , pp. 3956-3966
    • Atrih, A.1    Bacher, G.2    Allmaier, G.3    Williamson, M.P.4    Foster, S.J.5
  • 4
    • 0026035515 scopus 로고
    • FtsZ in Bacillus subtilis is required for vegetative septation and for asymmetric septation during sporulation
    • Beall, B., and Lutkenhaus, J. (1991) FtsZ in Bacillus subtilis is required for vegetative septation and for asymmetric septation during sporulation. Genes Dev 5: 447-455.
    • (1991) Genes Dev , vol.5 , pp. 447-455
    • Beall, B.1    Lutkenhaus, J.2
  • 5
    • 0011343882 scopus 로고    scopus 로고
    • Detection of intra-cellular protein-protein interactions: Penicillin interactive proteins and morphogene proteins
    • Marshak, D. (ed.). Academic Press
    • Bhardwaj, S., and Day, R.A. (1997) Detection of intra-cellular protein-protein interactions: penicillin interactive proteins and morphogene proteins. In Techniques in Protein Chemistry, Vol. 8. Marshak, D. (ed.). Academic Press, pp. 469-480.
    • (1997) Techniques in Protein Chemistry , vol.8 , pp. 469-480
    • Bhardwaj, S.1    Day, R.A.2
  • 6
    • 0026553914 scopus 로고
    • Isolation and sequence analysis of dacB, which encodes a sporulation-specific penicillin-binding protein in Bacillus subtilis
    • Buchanan, C.E., and Ling, M.-L. (1992) Isolation and sequence analysis of dacB, which encodes a sporulation-specific penicillin-binding protein in Bacillus subtilis. J Bacteriol 174: 1717-1725.
    • (1992) J Bacteriol , vol.174 , pp. 1717-1725
    • Buchanan, C.E.1    Ling, M.-L.2
  • 7
    • 0020554044 scopus 로고
    • Evidence for diffuse growth of the cylindrical portion of the Escherichia coli murein sacculus
    • Burman, L.G., Raichler, J., and Park, J.T. (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
  • 8
    • 0029973636 scopus 로고    scopus 로고
    • FACS-optimized mutants of the green fluorescent protein (GFP)
    • Cormack, B.P., Valdivia, R.H., and Falkow, S. (1996) FACS-optimized mutants of the green fluorescent protein (GFP). Gene 173: 33-38.
    • (1996) Gene , vol.173 , pp. 33-38
    • Cormack, B.P.1    Valdivia, R.H.2    Falkow, S.3
  • 9
    • 0037494988 scopus 로고    scopus 로고
    • Control of cell morphogenesis in bacteria: Two distinct ways to make a rod-shaped cell
    • Daniel, R.A., and Errington, J. (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
  • 10
    • 0028011141 scopus 로고
    • The Bacillus subtilis spoVD gene encodes a mother-cell-specific penicillin-binding protein required for spore morphogenesis
    • Daniel, R.A., Drake, S., Buchanan, C.E., Scholle, R., and Errington, J. (1994) The Bacillus subtilis spoVD gene encodes a mother-cell-specific penicillin-binding protein required for spore morphogenesis. J Mol Biol 235: 209-220.
    • (1994) J Mol Biol , vol.235 , pp. 209-220
    • Daniel, R.A.1    Drake, S.2    Buchanan, C.E.3    Scholle, R.4    Errington, J.5
  • 11
    • 0031824694 scopus 로고    scopus 로고
    • Characterization of the essential cell division gene ftsL (yllD) of Bacillus subtilis and its role in the assembly of the division apparatus
    • Daniel, R.A., Harry, E.J., Katis, V.L., Wake, R.G., and Errington, J. (1998) Characterization of the essential cell division gene ftsL (yllD) of Bacillus subtilis and its role in the assembly of the division apparatus. Mol Microbiol 29: 593-604.
    • (1998) Mol Microbiol , vol.29 , pp. 593-604
    • Daniel, R.A.1    Harry, E.J.2    Katis, V.L.3    Wake, R.G.4    Errington, J.5
  • 12
    • 0033985396 scopus 로고    scopus 로고
    • Role of penicillin-binding protein PBP 2B in assembly and functioning of the division machinery of Bacillus subtilis
    • Daniel, R.A., Harry, E.J., and Errington, J. (2000) Role of penicillin-binding protein PBP 2B in assembly and functioning of the division machinery of Bacillus subtilis. Mol Microbiol 35: 299-311.
    • (2000) Mol Microbiol , vol.35 , pp. 299-311
    • Daniel, R.A.1    Harry, E.J.2    Errington, J.3
  • 13
    • 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
  • 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
    • 0035817819 scopus 로고    scopus 로고
    • Prokaryotic origin of the actin cyloskeleton
    • van den Ent, F., Amos, L.A., and Löwe, J. (2001) Prokaryotic origin of the actin cyloskeleton. Nature 413: 39-44.
    • (2001) Nature , vol.413 , pp. 39-44
    • Van Den Ent, F.1    Amos, L.A.2    Löwe, J.3
  • 16
    • 0001904527 scopus 로고    scopus 로고
    • Structure and synthesis of cell wall, spore cortex, teichoic acids, S-layers, and capsules
    • Sonenshein, L., Losick, R., and Hoch, J.A. (eds). Washington, DC: American Society for Microbiology Press
    • Foster, S.J., and Popham, D.L. (2001) Structure and synthesis of cell wall, spore cortex, teichoic acids, S-layers, and capsules. In Bacillus subtilis and its Relatives: from Genes to Cells. Sonenshein, L., Losick, R., and Hoch, J.A. (eds). Washington, DC: American Society for Microbiology Press, pp. 21-41.
    • (2001) Bacillus Subtilis and Its Relatives: From Genes to Cells , pp. 21-41
    • Foster, S.J.1    Popham, D.L.2
  • 17
    • 0027972388 scopus 로고
    • Multiple mechanisms of membrane anchoring of Escherichia coli penicillin-binding proteins
    • Gittins, J.R., Phoenix, D.A., and Pratt, J.M. (1994) Multiple mechanisms of membrane anchoring of Escherichia coli penicillin-binding proteins. FEMS Microbiol Rev 13: 1-12.
    • (1994) FEMS Microbiol Rev , vol.13 , pp. 1-12
    • Gittins, J.R.1    Phoenix, D.A.2    Pratt, J.M.3
  • 18
    • 0030910954 scopus 로고    scopus 로고
    • Dynamic, mitotic-like behaviour of a bacterial protein required for accurate chromosome partitioning
    • Glaser, P., Sharpe, M.E., Raether, B., Perego, M., Ohlsen, K., and Errington, J. (1997) Dynamic, mitotic-like behaviour of a bacterial protein required for accurate chromosome partitioning. Genes Dev 11: 1160-1168.
    • (1997) Genes Dev , vol.11 , pp. 1160-1168
    • Glaser, P.1    Sharpe, M.E.2    Raether, B.3    Perego, M.4    Ohlsen, K.5    Errington, J.6
  • 19
    • 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
  • 20
    • 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
  • 21
    • 0032716126 scopus 로고    scopus 로고
    • Gene disruption studies of penicillin-binding proteins 1a, 1b, and 2a in Streptococcus pneumoniae
    • Hoskins, J., Matsushima, P., Mullen, D.L., Tang, J., Zhao, G., Meier, T.I., et al. (1999) Gene disruption studies of penicillin-binding proteins 1a, 1b, and 2a in Streptococcus pneumoniae. J Bacteriol 181: 6552-6555.
    • (1999) J Bacteriol , vol.181 , pp. 6552-6555
    • Hoskins, J.1    Matsushima, P.2    Mullen, D.L.3    Tang, J.4    Zhao, G.5    Meier, T.I.6
  • 22
    • 0020528758 scopus 로고
    • Altered arrangement of proteins in the spore coat of a germination mutant of Bacillus subtilis
    • Jenkinson, H.F. (1983) Altered arrangement of proteins in the spore coat of a germination mutant of Bacillus subtilis. J Gen Microbiol 129: 1945-1958.
    • (1983) J Gen Microbiol , vol.129 , pp. 1945-1958
    • Jenkinson, H.F.1
  • 23
    • 0035937396 scopus 로고    scopus 로고
    • Control of cell shape in bacteria: Helical, actin-like filaments in Bacillus subtilis
    • Jones, L.J.F., Carballido-López, R., and Errington, J. (2001) Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis. Cell 104: 913-922.
    • (2001) Cell , vol.104 , pp. 913-922
    • Jones, L.J.F.1    Carballido-López, R.2    Errington, J.3
  • 24
    • 0029006115 scopus 로고
    • Salt stress is an environmental signal affecting degradative enzyme synthesis in Bacillus subtilis
    • Kunst, F., and Rapoport, G. (1995) Salt stress is an environmental signal affecting degradative enzyme synthesis in Bacillus subtilis. J Bacteriol 177: 2403-2407.
    • (1995) J Bacteriol , vol.177 , pp. 2403-2407
    • Kunst, F.1    Rapoport, G.2
  • 25
    • 0030927986 scopus 로고    scopus 로고
    • Direct evidence for active segregation of oriC regions of the Bacillus subtilis chromosome and co-localization with the Spo0J partitioning protein
    • Lewis, P.J., and Errington, J. (1997) Direct evidence for active segregation of oriC regions of the Bacillus subtilis chromosome and co-localization with the Spo0J partitioning protein. Mol Microbiol 25: 945-954.
    • (1997) Mol Microbiol , vol.25 , pp. 945-954
    • Lewis, P.J.1    Errington, J.2
  • 26
    • 0033521857 scopus 로고    scopus 로고
    • GFP vectors for controlled expression and dual labelling of protein fusions in Bacillus subtilis
    • Lewis, P.J., and Marston, A.L. (1999) GFP vectors for controlled expression and dual labelling of protein fusions in Bacillus subtilis. Gene 227: 101-109.
    • (1999) Gene , vol.227 , pp. 101-109
    • Lewis, P.J.1    Marston, A.L.2
  • 27
    • 0037315095 scopus 로고    scopus 로고
    • Peptidoglycan synthesis in the absence of Class A penicillin-binding proteins in Bacillus subtilis
    • McPherson, D.C., and Popham, D.L. (2003) Peptidoglycan synthesis in the absence of Class A penicillin-binding proteins in Bacillus subtilis. J Bacteriol 185: 1423-1431.
    • (2003) J Bacteriol , vol.185 , pp. 1423-1431
    • McPherson, D.C.1    Popham, D.L.2
  • 28
    • 0034816354 scopus 로고    scopus 로고
    • Two class A high-molecular-weight penicillin-binding proteins of Bacillus subtilis play redundant roles in sporulation
    • McPherson, D.C., Driks, A., and Popham, D.L. (2001) Two class A high-molecular-weight penicillin-binding proteins of Bacillus subtilis play redundant roles in sporulation. J Bacteriol 183: 6046-6053.
    • (2001) J Bacteriol , vol.183 , pp. 6046-6053
    • McPherson, D.C.1    Driks, A.2    Popham, D.L.3
  • 29
    • 0021191674 scopus 로고
    • Insertion and fate of the cell wall in Bacillus subtilis
    • Mobley, H.L.T., Koch, A.L., Doyle, R.J., and Streips, U.N. (1984) Insertion and fate of the cell wall in Bacillus subtilis. J Bacteriol 158: 169-179.
    • (1984) J Bacteriol , vol.158 , pp. 169-179
    • Mobley, H.L.T.1    Koch, A.L.2    Doyle, R.J.3    Streips, U.N.4
  • 30
    • 0029820892 scopus 로고    scopus 로고
    • Identification and characterization of pbpC, the gene encoding Bacillus subtilis penicillin-binding protein 3
    • Murray, T., Popham, D.L., and Setlow, P. (1996) Identification and characterization of pbpC, the gene encoding Bacillus subtilis penicillin-binding protein 3. J Bacteriol 178: 6001-6005.
    • (1996) J Bacteriol , vol.178 , pp. 6001-6005
    • Murray, T.1    Popham, D.L.2    Setlow, P.3
  • 31
    • 0030971549 scopus 로고    scopus 로고
    • Identification and characterization of pbpA encoding Bacillus subtilis penicillin-binding protein 2A
    • Murray, T., Popham, D.L., and Setlow, P. (1997) Identification and characterization of pbpA encoding Bacillus subtilis penicillin-binding protein 2A. J Bacteriol 179: 3021-3029.
    • (1997) J Bacteriol , vol.179 , pp. 3021-3029
    • Murray, T.1    Popham, D.L.2    Setlow, P.3
  • 32
    • 0032425550 scopus 로고    scopus 로고
    • Analysis of outgrowth of Bacillus subtilis spores lacking penicillin-binding protein 2a
    • Murray, T., Popham, D.L., Pearson, C.B., Hand, A.R., and Setlow, P. (1998) Analysis of outgrowth of Bacillus subtilis spores lacking penicillin-binding protein 2a. J Bacteriol 180: 6493-6502.
    • (1998) J Bacteriol , vol.180 , pp. 6493-6502
    • Murray, T.1    Popham, D.L.2    Pearson, C.B.3    Hand, A.R.4    Setlow, P.5
  • 33
    • 0033014014 scopus 로고    scopus 로고
    • Mutational analysis of the Streptococcus pneumoniae bimodular class A penicillin-binding proteins
    • Paik, J., Kern, I., Lurz, R., and Hakenbeck, R. (1999) Mutational analysis of the Streptococcus pneumoniae bimodular class A penicillin-binding proteins. J Bacteriol 181: 3852-3856.
    • (1999) J Bacteriol , vol.181 , pp. 3852-3856
    • Paik, J.1    Kern, I.2    Lurz, R.3    Hakenbeck, R.4
  • 34
    • 0031715449 scopus 로고    scopus 로고
    • Characterization of dacC, which encodes a new low-molecular-weight penicillin-binding protein in Bacillus subtilis
    • Pedersen, L.B., Murray, T., Popham, D.L., and Setlow, P. (1998) Characterization of dacC, which encodes a new low-molecular-weight penicillin-binding protein in Bacillus subtilis. J Bacteriol 180: 4967-4973.
    • (1998) J Bacteriol , vol.180 , pp. 4967-4973
    • Pedersen, L.B.1    Murray, T.2    Popham, D.L.3    Setlow, P.4
  • 35
    • 0032909890 scopus 로고    scopus 로고
    • Septal localization of penicillin-binding protein 1 in Bacillus subtilis
    • Pedersen, L.B., Angert, E.R., and Setlow, P. (1999) Septal localization of penicillin-binding protein 1 in Bacillus subtilis. J Bacteriol 181: 3201-3211.
    • (1999) J Bacteriol , vol.181 , pp. 3201-3211
    • Pedersen, L.B.1    Angert, E.R.2    Setlow, P.3
  • 36
    • 0034603830 scopus 로고    scopus 로고
    • Characterization of ywhE, which encodes a putative high-molecular-weight class A penicillin-binding protein in Bacillus subtilis
    • Pedersen, L.B., Ragkousi, K., Cammett, T.J., Melly, E., Sekowska, A., Schopick, E., et al. (2000) Characterization of ywhE, which encodes a putative high-molecular-weight class A penicillin-binding protein in Bacillus subtilis. Gene 246: 187-196.
    • (2000) Gene , vol.246 , pp. 187-196
    • Pedersen, L.B.1    Ragkousi, K.2    Cammett, T.J.3    Melly, E.4    Sekowska, A.5    Schopick, E.6
  • 38
    • 0027203788 scopus 로고
    • Cloning, nucleotide sequence, and regulation of the Bacillus subtilis pbpF gene, which codes for a putative class a high-molecular-weight penicillin-binding protein
    • Popham, D.L., and Setlow, P. (1993) Cloning, nucleotide sequence, and regulation of the Bacillus subtilis pbpF gene, which codes for a putative class A high-molecular-weight penicillin-binding protein. J Bacteriol 175: 4870-4876.
    • (1993) J Bacteriol , vol.175 , pp. 4870-4876
    • Popham, D.L.1    Setlow, P.2
  • 39
    • 0028104377 scopus 로고
    • Cloning, nucleotide sequence, mutagenesis, and mapping of the Bacillus subtilis pbpD gene, which codes for penicillin-binding protein 4
    • Popham, D.L., and Setlow, P. (1994) Cloning, nucleotide sequence, mutagenesis, and mapping of the Bacillus subtilis pbpD gene, which codes for penicillin-binding protein 4. J Bacteriol 176: 7197-7205.
    • (1994) J Bacteriol , vol.176 , pp. 7197-7205
    • Popham, D.L.1    Setlow, P.2
  • 40
    • 0028835462 scopus 로고
    • Cloning, nucleotide sequence, and mutagenesis of the Bacillus subtilis ponA operon, which codes for penicillin-binding protein (PBP) 1 and a PBP-related factor
    • Popham, D.L., and Setlow, P. (1995) Cloning, nucleotide sequence, and mutagenesis of the Bacillus subtilis ponA operon, which codes for penicillin-binding protein (PBP) 1 and a PBP-related factor. J Bacteriol 177: 326-335.
    • (1995) J Bacteriol , vol.177 , pp. 326-335
    • Popham, D.L.1    Setlow, P.2
  • 41
    • 0029874913 scopus 로고    scopus 로고
    • Phenotypes of Bacillus subtilis mutants lacking multiple class a high-molecular-weight penicillin-binding proteins
    • Popham, D.L., and Setlow, P. (1996) Phenotypes of Bacillus subtilis mutants lacking multiple class a high-molecular-weight penicillin-binding proteins. J Bacteriol 178: 2079-2085.
    • (1996) J Bacteriol , vol.178 , pp. 2079-2085
    • Popham, D.L.1    Setlow, P.2
  • 42
    • 0032932349 scopus 로고    scopus 로고
    • Roles of low-molecular-weight penicillin-binding proteins in Bacillus subtilis spore peptidoglycan synthesis and spore properties
    • Popham, D.L., Gilmore, M.E., and Setlow, P. (1999) Roles of low-molecular-weight penicillin-binding proteins in Bacillus subtilis spore peptidoglycan synthesis and spore properties. J Bacteriol 181: 126-132.
    • (1999) J Bacteriol , vol.181 , pp. 126-132
    • Popham, D.L.1    Gilmore, M.E.2    Setlow, P.3
  • 44
    • 0022395367 scopus 로고
    • Cell wall and DNA cosegregation in Bacillus subtilis studied by electron microscope autoradiography
    • Schlaeppi, J.-M., Schaefer, O., and Karamata, D. (1985) Cell wall and DNA cosegregation in Bacillus subtilis studied by electron microscope autoradiography. J Bacteriol 164: 130-135.
    • (1985) J Bacteriol , vol.164 , pp. 130-135
    • Schlaeppi, J.-M.1    Schaefer, O.2    Karamata, D.3
  • 45
    • 0031932320 scopus 로고    scopus 로고
    • Bacillus subtilis cell cycle as studied by fluorescence microscopy: Constancy of the cell length at initiation of DNA replication and evidence for active nucleoid partitioning
    • Sharpe, M.E., Hauser, P.M., Sharpe, R.G., and Errington, J. (1998) Bacillus subtilis cell cycle as studied by fluorescence microscopy: constancy of the cell length at initiation of DNA replication and evidence for active nucleoid partitioning. J Bacteriol 180: 547-555.
    • (1998) J Bacteriol , vol.180 , pp. 547-555
    • Sharpe, M.E.1    Hauser, P.M.2    Sharpe, R.G.3    Errington, J.4
  • 46
    • 0034022103 scopus 로고    scopus 로고
    • Improved resolution of hydrophobic penicillin-binding proteins and their covalently linked complexes on a modified C18 reversed phase column
    • Simon, M.J., and Day, R.A. (2000) Improved resolution of hydrophobic penicillin-binding proteins and their covalently linked complexes on a modified C18 reversed phase column. Anal Lett 33: 861-867.
    • (2000) Anal Lett , vol.33 , pp. 861-867
    • Simon, M.J.1    Day, R.A.2
  • 47
    • 0013096299 scopus 로고
    • Distinct penicillin-binding proteins involved in the division, elongation and shape of Escherichia coli K-12
    • Spratt, B.G. (1975) Distinct penicillin-binding proteins involved in the division, elongation and shape of Escherichia coli K-12. Proc Natl Acad Sci USA 72: 2999-3003.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 2999-3003
    • Spratt, B.G.1
  • 48
    • 0014533169 scopus 로고
    • Commitment to sporulation in Bacillus subtilis and its relationship to the development of actinomycin resistance
    • Sterlini, J.M., and Mandelstam, J. (1969) Commitment to sporulation in Bacillus subtilis and its relationship to the development of actinomycin resistance. Biochem J 113: 29-37.
    • (1969) Biochem J , vol.113 , pp. 29-37
    • Sterlini, J.M.1    Mandelstam, J.2
  • 49
    • 0022542474 scopus 로고
    • Reduced heat resistance of mutant spores after cloning and mutagenesis of the Bacillus subtilis gene encoding penicillin- binding protein 5
    • Todd, J.A., Roberts, A.N., Johnstone, K., Piggot, P.J., Winter, G., and Ellar, D.J. (1986) Reduced heat resistance of mutant spores after cloning and mutagenesis of the Bacillus subtilis gene encoding penicillin-binding protein 5. J Bacteriol 167: 257-264.
    • (1986) J Bacteriol , vol.167 , pp. 257-264
    • Todd, J.A.1    Roberts, A.N.2    Johnstone, K.3    Piggot, P.J.4    Winter, G.5    Ellar, D.J.6
  • 50
    • 0031737309 scopus 로고    scopus 로고
    • A vector for systematic gene inactivation in Bacillus subtilis
    • Vagner, V., Dervyn, E., and Ehrlich, S.D. (1998) A vector for systematic gene inactivation in Bacillus subtilis. Microbiol 144: 3097-3104.
    • (1998) Microbiol , vol.144 , pp. 3097-3104
    • Vagner, V.1    Dervyn, E.2    Ehrlich, S.D.3
  • 51
    • 0042561877 scopus 로고    scopus 로고
    • Rod shape determination by the Bacillus subtilis Class B penicillin-binding proteins encoded by pbpA and pbpH
    • Wei, Y., Havasy, T., McPherson, D.C., and Popham, D.L. (2003) Rod shape determination by the Bacillus subtilis Class B penicillin-binding proteins encoded by pbpA and pbpH. J Bacteriol 185: 4717-4726.
    • (2003) J Bacteriol , vol.185 , pp. 4717-4726
    • Wei, Y.1    Havasy, T.2    McPherson, D.C.3    Popham, D.L.4
  • 52
    • 0030881627 scopus 로고    scopus 로고
    • Localization of the Escherichia coli cell division protein Ftsl (PBP3) to the division site and cell pole
    • Weiss, D.S., Pogliano, K., Carson, M., Guzman, L.-M., Fraipont, C., Nguyen-Distèche, M., et al. (1997) Localization of the Escherichia coli cell division protein Ftsl (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-Distèche, M.6
  • 53
    • 0023134582 scopus 로고
    • Topography of peptidoglycan synthesis during elongation and polar cap formation in a cell division mutant of Escherichia coli MC4100
    • Woldringh, C.L., Huls, P., Pas, E., Brakenhoff, G.J., and Nanninga, N. (1987) Topography of peptidoglycan synthesis during elongation and polar cap formation in a cell division mutant of Escherichia coli MC4100. J Gen Microbiol 133: 575-586.
    • (1987) J Gen Microbiol , vol.133 , pp. 575-586
    • Woldringh, C.L.1    Huls, P.2    Pas, E.3    Brakenhoff, G.J.4    Nanninga, N.5
  • 54
    • 0026634121 scopus 로고
    • Characterization of a Bacillus subtilis sporulation operon that includes genes for an RNA polymerase σ factor and for a putative DD-carboxypeptidase
    • Wu, J.-J., Schuch, R., and Piggot, P.J. (1992) Characterization of a Bacillus subtilis sporulation operon that includes genes for an RNA polymerase σ factor and for a putative DD-carboxypeptidase. J Bacteriol 174: 4885-4892.
    • (1992) J Bacteriol , vol.174 , pp. 4885-4892
    • Wu, J.-J.1    Schuch, R.2    Piggot, P.J.3
  • 55
    • 0141677790 scopus 로고    scopus 로고
    • RacA and the Soj-Spo0J system combine to effect polar chromosome segregation in sporulating Bacillus subtilis
    • Wu, L.J., and Errington, J. (2003) RacA and the Soj-Spo0J system combine to effect polar chromosome segregation in sporulating Bacillus subtilis. Mol Microbiol 49: 1463-1475.
    • (2003) Mol Microbiol , vol.49 , pp. 1463-1475
    • Wu, L.J.1    Errington, J.2
  • 56
    • 0027489263 scopus 로고
    • Cloning and sequencing of the cell division gene pbpB, which encodes penicillin-binding protein 2B in Bacillus subtilis
    • Yanouri, A., Daniel, R.A., Errington, J., and Buchanan, C.E. (1993) Cloning and sequencing of the cell division gene pbpB, which encodes penicillin-binding protein 2B in Bacillus subtilis. J Bacteriol 175: 7604-7616.
    • (1993) J Bacteriol , vol.175 , pp. 7604-7616
    • Yanouri, A.1    Daniel, R.A.2    Errington, J.3    Buchanan, C.E.4
  • 57
    • 0032908481 scopus 로고    scopus 로고
    • Bocillin FL, a sensitive and commercially available reagent for detection of penicillin-binding proteins
    • Zhao, G., Meier, T.I., Kahl, S.D., Gee, K.R., and Blaszczak, L.C. (1999) Bocillin FL, a sensitive and commercially available reagent for detection of penicillin-binding proteins. Antimicrob Agents Chemother 43: 1124-1128.
    • (1999) Antimicrob Agents Chemother , vol.43 , pp. 1124-1128
    • Zhao, G.1    Meier, T.I.2    Kahl, S.D.3    Gee, K.R.4    Blaszczak, L.C.5


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