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Volumn 181, Issue 10, 1999, Pages 3201-3211

Septal localization of penicillin-binding protein 1 in Bacillus subtilis

Author keywords

[No Author keywords available]

Indexed keywords

PENICILLIN BINDING PROTEIN;

EID: 0032909890     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.10.3201-3211.1999     Document Type: Article
Times cited : (51)

References (65)
  • 1
    • 0030921172 scopus 로고    scopus 로고
    • The bimodular G57-V577 polypeptide chain of the class B penicillin-binding protein 3 of Escherichia coli catalyzes peptide bond formation from thiolesters and does not catalyze glycan chain polymerization from the lipid II intermediate
    • Adam, M., C. Fraipont, N. Rhazi, M. Nguyen-Distèche, B. Lakaye, J.-M. Frère, B. Devreese, J. van Beeumen, Y. van Heijenoort, J. ran Heijenoort, and J.-M. Ghuysen. 1997. The bimodular G57-V577 polypeptide chain of the class B penicillin-binding protein 3 of Escherichia coli catalyzes peptide bond formation from thiolesters and does not catalyze glycan chain polymerization from the lipid II intermediate. J. Bacteriol. 179:6005-6009.
    • (1997) J. Bacteriol. , vol.179 , pp. 6005-6009
    • Adam, M.1    Fraipont, C.2    Rhazi, N.3    Nguyen-Distèche, M.4    Lakaye, B.5    Frère, J.-M.6    Devreese, B.7    Van Beeumen, J.8    Van Heijenoort, Y.9    Ran Heijenoort, J.10    Ghuysen, J.-M.11
  • 2
    • 8944221179 scopus 로고    scopus 로고
    • FtsZ ring formation in fts mutants
    • Addinall, S. G., E. Bi, and J. Lutkenhaus. 1996. FtsZ ring formation in fts mutants. J. Bacteriol. 178:3877-3884.
    • (1996) J. Bacteriol. , vol.178 , pp. 3877-3884
    • Addinall, S.G.1    Bi, E.2    Lutkenhaus, J.3
  • 3
    • 0030856502 scopus 로고    scopus 로고
    • Ftsn, a late recruitment to the septum in Escherichia coli
    • Addinall, S. G., C. Cao, and J. Lutkenhaus. 1997. FtsN, a late recruitment to the septum in Escherichia coli. Mol. Microbiol. 25:303-309.
    • (1997) Mol. Microbiol. , vol.25 , pp. 303-309
    • Addinall, S.G.1    Cao, C.2    Lutkenhaus, J.3
  • 4
    • 0030448723 scopus 로고    scopus 로고
    • FtsA is localized to the septum in an FtsZ-dependent manner
    • Addinall, S. G., and J. Lutkenhaus. 1996. FtsA is localized to the septum in an FtsZ-dependent manner. J. Bacteriol. 178:7167-7172.
    • (1996) J. Bacteriol. , vol.178 , pp. 7167-7172
    • Addinall, S.G.1    Lutkenhaus, J.2
  • 5
    • 0015541815 scopus 로고
    • The purification, composition and specificity of wheat-germ agglutinin
    • Allen, K. A., A. Neoberger, and N. Sharon. 1973. The purification, composition and specificity of wheat-germ agglutinin. Biochem. J. 131:155-162.
    • (1973) Biochem. J. , vol.131 , pp. 155-162
    • Allen, K.A.1    Neoberger, A.2    Sharon, N.3
  • 6
    • 0001134202 scopus 로고
    • Requirements for transformation in Bacillus subtilis
    • Anagnostopoulus, C., and J. Spizizen. 1961. Requirements for transformation in Bacillus subtilis. J. Bacteriol. 81:74-76.
    • (1961) J. Bacteriol. , vol.81 , pp. 74-76
    • Anagnostopoulus, C.1    Spizizen, J.2
  • 7
    • 0025020273 scopus 로고
    • Localization of penicillin-binding protein 1b in Escherichia coK: Immunoelectron microscopy and immunotransfer studies
    • Bayer, M. H., W. Keck, and M. E. Buyer. 1990. Localization of penicillin-binding protein 1b in Escherichia coK: immunoelectron microscopy and immunotransfer studies. J. Bacteriol. 172:125-135.
    • (1990) J. Bacteriol. , vol.172 , pp. 125-135
    • Bayer, M.H.1    Keck, W.2    Buyer, M.E.3
  • 8
    • 0021886039 scopus 로고
    • Cell shape and division in Escherichia coli: Experiments with shape and division mutants
    • Begg, K. J., and W. D. Donachie. 1985. Cell shape and division in Escherichia coli: experiments with shape and division mutants. J. Bacteriol. 163:615-622.
    • (1985) J. Bacteriol. , vol.163 , pp. 615-622
    • Begg, K.J.1    Donachie, W.D.2
  • 9
    • 0026059127 scopus 로고
    • FtsZ ring structure associated with division in Escherichia coli
    • Bi, E., and J. Lutkenhaus. 1991. FtsZ ring structure associated with division in Escherichia coli. Nature 354:161-164.
    • (1991) Nature , vol.354 , pp. 161-164
    • Bi, E.1    Lutkenhaus, J.2
  • 11
    • 0032953197 scopus 로고    scopus 로고
    • Septal localization of FtsQ, an essential cell division protein in Escherichia coli
    • Chen, J. C., D. S. Weiss, J.-M. Ghigo, and J. Beckwith. 1999. Septal localization of FtsQ, an essential cell division protein in Escherichia coli. J. Bacteriol. 181:521-530.
    • (1999) J. Bacteriol. , vol.181 , pp. 521-530
    • Chen, J.C.1    Weiss, D.S.2    Ghigo, J.-M.3    Beckwith, J.4
  • 12
    • 0028117532 scopus 로고
    • Analysis of the expression and regulation of the gerB spore germination operon of Bacillus subtilis 168
    • Corfe, B. M., A. Moir, D. Popham, and P. Setlow. 1994. Analysis of the expression and regulation of the gerB spore germination operon of Bacillus subtilis 168. Microbiology 140:3079-3083.
    • (1994) Microbiology , vol.140 , pp. 3079-3083
    • Corfe, B.M.1    Moir, A.2    Popham, D.3    Setlow, P.4
  • 13
    • 0029956443 scopus 로고    scopus 로고
    • Direct quantitation of the number of individual penicillin-binding proteins per cell in Escherichia coli
    • Dougherty, T. J., K. Kennedy, R. E. Kessler, and M. J. Pucci. 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
  • 14
    • 0020584649 scopus 로고
    • Construction and properties of an integrable plasmid for Bacillus subtilis
    • Ferrari, F. A., A. Nguyen, D. Lang, and J. A. Hoch. 1983. Construction and properties of an integrable plasmid for Bacillus subtilis. J. Bacteriol. 154: 1513-1515.
    • (1983) J. Bacteriol. , vol.154 , pp. 1513-1515
    • Ferrari, F.A.1    Nguyen, A.2    Lang, D.3    Hoch, J.A.4
  • 15
    • 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
    • García del Portillo, F., M. A. de Pedro, and J. A. Ayala. 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. 84:7-14.
    • (1991) FEMS Microbiol. Lett. , vol.84 , pp. 7-14
    • García Del Portillo, F.1    De Pedro, M.A.2    Ayala, J.A.3
  • 16
    • 0024370481 scopus 로고
    • Lytic response of Escherichia coli cells to inhibitors of penicillin-binding proteins 1a and 1b as a timed event related to cell division
    • García del Portillo, F., M. A. de Pedro, D. Joseleau-Petit, and R. d'Dari. 1989. Lytic response of Escherichia coli cells to inhibitors of penicillin-binding proteins 1a and 1b as a timed event related to cell division. J. Bacteriol. 171:4217-4221.
    • (1989) J. Bacteriol. , vol.171 , pp. 4217-4221
    • García Del Portillo, F.1    De Pedro, M.A.2    Joseleau-Petit, D.3    D'Dari, R.4
  • 17
    • 0028173341 scopus 로고
    • Molecular structures of penicillin-binding proteins and β-lactamases
    • Ghuysen, J.-M. 1994. Molecular structures of penicillin-binding proteins and β-lactamases. Trends Microbiol. 2:372-380.
    • (1994) Trends Microbiol. , vol.2 , pp. 372-380
    • Ghuysen, J.-M.1
  • 18
    • 0029808359 scopus 로고    scopus 로고
    • The non-penicillin-binding module of the tripartite penicillin-binding protein 3 of Escherichia coli is required for the folding and/or stability of the penicillin-binding module and the membrane-anchoring module confers cell septation activity on the folded structure
    • Goffin, C., C. Fraipont, J. Ayala, M. Terrak, M. Nguyen-Distèche, and J.-M. Ghuysen. 1996. The non-penicillin-binding module of the tripartite penicillin-binding protein 3 of Escherichia coli is required for the 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-Distèche, M.5    Ghuysen, J.-M.6
  • 19
    • 0031444158 scopus 로고    scopus 로고
    • Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. coli
    • Hale, C. A., and P. A. J. de Boer. 1997. Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. coli. Cell 88:175-185.
    • (1997) Cell , vol.88 , pp. 175-185
    • Hale, C.A.1    De Boer, P.A.J.2
  • 20
    • 0029017527 scopus 로고
    • Use of immunofluorescence to visualize cell-specific gene expression during sporulation in Bacillus subtilis
    • Harry, E. J., K. Pogliano, and R. Losick. 1995. Use of immunofluorescence to visualize cell-specific gene expression during sporulation in Bacillus subtilis. J. Bacteriol. 177:3386-3393.
    • (1995) J. Bacteriol. , vol.177 , pp. 3386-3393
    • Harry, E.J.1    Pogliano, K.2    Losick, R.3
  • 21
    • 0030818705 scopus 로고    scopus 로고
    • The membrane-bound cell division protein DivIB is localized to the division site in Bacillus subtilis
    • Harry, E. J., and R. G. Wake. 1997. The membrane-bound cell division protein DivIB is localized to the division site in Bacillus subtilis. Mol. Microbiol. 25:275-283.
    • (1997) Mol. Microbiol. , vol.25 , pp. 275-283
    • Harry, E.J.1    Wake, R.G.2
  • 22
    • 0031991771 scopus 로고    scopus 로고
    • Cell cycle-dependent duplication and bidirectional migration of SeqA-associated DNA-protein complexes in E. coli
    • Hiraga, S., C. Inchinose, H. Niki, and M. Yamazoe. 1998. Cell cycle-dependent duplication and bidirectional migration of SeqA-associated DNA-protein complexes in E. coli. Mol. Cell 1:381-387.
    • (1998) Mol. Cell , vol.1 , pp. 381-387
    • Hiraga, S.1    Inchinose, C.2    Niki, H.3    Yamazoe, M.4
  • 23
    • 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
  • 24
    • 0019289889 scopus 로고
    • Dual enzyme activities of cell wall peptidoglycan synthesis, peptidoglycan transglycosylase and penicillin-sensitive transpeptidase, in purified preparations of Escherichia coli penicillin-binding protein 1A
    • Ishino, F., K. Mitsui, S. Tamaki, and M. Matsuhashi. 1980. Dual enzyme activities of cell wall peptidoglycan synthesis, peptidoglycan transglycosylase and penicillin-sensitive transpeptidase, in purified preparations of Escherichia coli penicillin-binding protein 1A. Biochem. Biophys. Res. Commun. 97:287-293.
    • (1980) Biochem. Biophys. Res. Commun. , vol.97 , pp. 287-293
    • Ishino, F.1    Mitsui, K.2    Tamaki, S.3    Matsuhashi, M.4
  • 25
    • 0030662451 scopus 로고    scopus 로고
    • The Bacillus subtilis division protein DivIC is a highly abundant membrane-bound protein that localizes to the division site
    • Katis, V. L., E. J. Harry, and R. G. Wake. 1997. The Bacillus subtilis division protein DivIC is a highly abundant membrane-bound protein that localizes to the division site. Mol. Microbiol. 26:1047-1055.
    • (1997) Mol. Microbiol. , vol.26 , pp. 1047-1055
    • Katis, V.L.1    Harry, E.J.2    Wake, R.G.3
  • 26
    • 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., H. Suzuki, and Y. Hirota. 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
  • 27
    • 0031016478 scopus 로고    scopus 로고
    • Two polypeptide products of the Escherichia coli cell division gene ftsW and a possible role for FtsW in FtsZ function
    • Khattar, M. M., S. G. Addinall, K. H. Stedul, D. S. Boyle, J. Lutkenhaus, and W. D. Donachie. 1997. Two polypeptide products of the Escherichia coli cell division gene ftsW and a possible role for FtsW in FtsZ function. J. Bacteriol. 179:784-793.
    • (1997) J. Bacteriol. , vol.179 , pp. 784-793
    • Khattar, M.M.1    Addinall, S.G.2    Stedul, K.H.3    Boyle, D.S.4    Lutkenhaus, J.5    Donachie, W.D.6
  • 28
    • 0030731108 scopus 로고    scopus 로고
    • The complete genome sequence of the gram-positive bacterium Bacillus subtilis
    • Kunst, F., N. Ogasawara, I. Moszer, A. M. Albertini, G. Alloni, et al. 1997. The complete genome sequence of the gram-positive bacterium Bacillus subtilis. Nature 390:249-256.
    • (1997) Nature , vol.390 , pp. 249-256
    • Kunst, F.1    Ogasawara, N.2    Moszer, I.3    Albertini, A.M.4    Alloni, G.5
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0015239543 scopus 로고
    • The stability of messenger ribonucleic acid during sporulation in Bacillus subtilis
    • Leighton, T. J., and R. H. Doi. 1971. The stability of messenger ribonucleic acid during sporulation in Bacillus subtilis. J. Biol. Chem. 254:3189-3195.
    • (1971) J. Biol. Chem. , vol.254 , pp. 3189-3195
    • Leighton, T.J.1    Doi, R.H.2
  • 31
    • 0029918758 scopus 로고    scopus 로고
    • Transcription factor Spo0A switches the localization of the cell division protein FtsZ from a medial to a bipolar pattern in Bacillus subtilis
    • Levin, P. A., and R. Losick. 1996. Transcription factor Spo0A switches the localization of the cell division protein FtsZ from a medial to a bipolar pattern in Bacillus subtilis. Genes Dev. 10:478-488.
    • (1996) Genes Dev. , vol.10 , pp. 478-488
    • Levin, P.A.1    Losick, R.2
  • 33
    • 0031856847 scopus 로고    scopus 로고
    • Localization and function of earty cell division proteins in filamentous Escherichia coli cells lacking phosphatidylethanolamine
    • Mileykovskaya, E., Q. Sun, W. Margolin, and W. Dowhan. 1998. Localization and function of earty cell division proteins in filamentous Escherichia coli cells lacking phosphatidylethanolamine. J. Bacteriol. 180:4252-4257.
    • (1998) J. Bacteriol. , vol.180 , pp. 4252-4257
    • Mileykovskaya, E.1    Sun, Q.2    Margolin, W.3    Dowhan, W.4
  • 34
    • 0030971549 scopus 로고    scopus 로고
    • Identification and characterization of pbpA encoding Bacillus subtilis penicillin-binding protein 2A
    • Murray, T., D. L. Popham, and P. Setlow. 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
  • 35
    • 0031721528 scopus 로고    scopus 로고
    • Bacillus subtilis cells lacking penicillin-binding protein 1 require increased levels of divalent cations for growth
    • Murray, T., D. L. Popham, and P. Setlow. 1998. Bacillus subtilis cells lacking penicillin-binding protein 1 require increased levels of divalent cations for growth, J. Bacteriol. 180:4555-4563.
    • (1998) J. Bacteriol. , vol.180 , pp. 4555-4563
    • Murray, T.1    Popham, D.L.2    Setlow, P.3
  • 36
    • 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
  • 37
    • 0031912354 scopus 로고    scopus 로고
    • Morphogenesis of Escherichia coli
    • Nanninga, N. 1998. Morphogenesis of Escherichia coli. Microbiol. Mol. Biol. Rev. 62:110-129.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 110-129
    • Nanninga, N.1
  • 39
    • 0344632175 scopus 로고    scopus 로고
    • National Institutes of Health, Bethesda, Md. 9 September 1998, last date accessed
    • NIH Image program. National Institutes of Health, Bethesda, Md. http:// rsb.info.gov/nih-image. [9 September 1998, last date accessed.]
  • 41
    • 0031018531 scopus 로고    scopus 로고
    • Inactivation of FtsI inhibits constriction of the FtsZ cytokinetic ring and delays the assembly of FtsZ rings at potential division sites
    • Pogliano, J., K. Pogliano, D. S. Weiss, R. Losick, and J. Beckwith. 1997. Inactivation of FtsI inhibits constriction of the FtsZ cytokinetic ring and delays the assembly of FtsZ rings at potential division sites. Proc. Natl. Acad. Sci. USA 94:559-564.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 559-564
    • Pogliano, J.1    Pogliano, K.2    Weiss, D.S.3    Losick, R.4    Beckwith, J.5
  • 42
    • 0029610802 scopus 로고
    • Visualization of the subcellular location of sporulation proteins in Bacillus subtilis using immunorluorescence microscopy
    • Pogliano, K., E. Harry, and R. Losick. 1995. Visualization of the subcellular location of sporulation proteins in Bacillus subtilis using immunorluorescence microscopy. Mol. Microbiol. 18:459-470.
    • (1995) Mol. Microbiol. , vol.18 , pp. 459-470
    • Pogliano, K.1    Harry, E.2    Losick, R.3
  • 43
    • 0030925483 scopus 로고    scopus 로고
    • E transcription factor from the forespore and the SpoIIE phosphatase from the mother cell contributes to establishment of cell-specific gene expression during sporulation in Bacillus subtilis
    • E transcription factor from the forespore and the SpoIIE phosphatase from the mother cell contributes to establishment of cell-specific gene expression during sporulation in Bacillus subtilis. J. Bacteriol. 179:3331-3341.
    • (1997) J. Bacteriol. , vol.179 , pp. 3331-3341
    • Pogliano, K.1    Hofmeister, A.E.M.2    Losick, R.3
  • 44
    • 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 P. Setlow. 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
  • 45
    • 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 P. Setlow. 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
  • 46
    • 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 P. Setlow. 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
  • 47
    • 0029874913 scopus 로고    scopus 로고
    • Phenotypes of Bacillus subtilis mutants lacking multiple class A high-molecular-weight penicillin-binding proteins
    • Popham, D. L., and P. Setlow. 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
  • 48
    • 0030934312 scopus 로고    scopus 로고
    • Cloning and characterization of the ponA gene encoding penicillin-binding protein 1 from Neisseria gonorrhoeae and Neisseria meningitidis
    • Ropp, P. A., and R. A. Nicholas. 1997. Cloning and characterization of the ponA gene encoding penicillin-binding protein 1 from Neisseria gonorrhoeae and Neisseria meningitidis. J. Bacteriol. 179:2783-2787.
    • (1997) J. Bacteriol. , vol.179 , pp. 2783-2787
    • Ropp, P.A.1    Nicholas, R.A.2
  • 49
    • 0030901357 scopus 로고    scopus 로고
    • Bacterial cell division: The cycle of the ring
    • Rothfield, L. I., and S. S. Justice. 1997. Bacterial cell division: the cycle of the ring. Cell 88:581-584.
    • (1997) Cell , vol.88 , pp. 581-584
    • Rothfield, L.I.1    Justice, S.S.2
  • 50
    • 0025325983 scopus 로고
    • The "megaprimer" method of site-directed mutagenesis
    • Sarkar, G., and S. S. Sommer. 1990. The "megaprimer" method of site-directed mutagenesis. BioTechniques 8:404-407.
    • (1990) BioTechniques , vol.8 , pp. 404-407
    • Sarkar, G.1    Sommer, S.S.2
  • 51
    • 0026090060 scopus 로고
    • Synthesis of a Bacillus subtilis small, acid-soluble spore protein in Escherichia coli causes cell DNA to assume some characteristics of spore DNA
    • Setlow, B., A. R. Hand, and P. Setlow. 1991. Synthesis of a Bacillus subtilis small, acid-soluble spore protein in Escherichia coli causes cell DNA to assume some characteristics of spore DNA. J. Bacteriol. 173:1642-1653.
    • (1991) J. Bacteriol. , vol.173 , pp. 1642-1653
    • Setlow, B.1    Hand, A.R.2    Setlow, P.3
  • 52
    • 0031932320 scopus 로고    scopus 로고
    • Bacillus subtilis cell cycle as studied by fluorescence microscopy: Constancy of cell length at initiation of DNA replication and evidence for active nucleoid partitioning
    • Sharpe, M. E., P. M. Hauser, R. G. Sharpe, and J. Errington. 1998. Bacillus subtilis cell cycle as studied by fluorescence microscopy: constancy of 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
  • 54
    • 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
  • 55
    • 0030058939 scopus 로고    scopus 로고
    • Monofunctional biosynthetic peptidoglycan transglycosylases
    • Spratt, B. G., J. Zhou, M. Taylor, and M. J. Merrick. 1996. Monofunctional biosynthetic peptidoglycan transglycosylases. Mol. Microbiol. 19:639-647.
    • (1996) Mol. Microbiol. , vol.19 , pp. 639-647
    • Spratt, B.G.1    Zhou, J.2    Taylor, M.3    Merrick, M.J.4
  • 56
    • 0018855285 scopus 로고
    • In vitro peptidoglycan polymerization catalyzed by penicillin binding protein 1b of Escherichia coli K12
    • Suzuki, H., V. van Heijenoort, T. Tamura, J. Mizoguchi, Y. Hirota, and J. van Heijenoort 1980. In vitro peptidoglycan polymerization catalyzed by penicillin binding protein 1b of Escherichia coli K12. FEBS Lett. 110:245-249.
    • (1980) FEBS Lett. , vol.110 , pp. 245-249
    • Suzuki, H.1    Van Heijenoort, V.2    Tamura, T.3    Mizoguchi, J.4    Hirota, Y.5    Van Heijenoort, J.6
  • 57
    • 0023992940 scopus 로고
    • Division behavior and shape changes in isogenic ftsZ, ftsQ, ftsA, pbpB, and ftsE cell division mutants of Escherichia coli during temperature shift experiments
    • Taschner, P. E. M., P. G. Huls, E. Pas, and C. L. Woldringh. 1988. Division behavior and shape changes in isogenic ftsZ, ftsQ, ftsA, pbpB, and ftsE cell division mutants of Escherichia coli during temperature shift experiments. J. Bacteriol. 170:1533-1540.
    • (1988) J. Bacteriol. , vol.170 , pp. 1533-1540
    • Taschner, P.E.M.1    Huls, P.G.2    Pas, E.3    Woldringh, C.L.4
  • 58
    • 0026623124 scopus 로고
    • Membrane intermediates in the peptidoglycan metabolism of Escherichia coli: Possible roles of PBP1b and PBP3
    • 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 PBP1b and PBP3. 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
  • 59
    • 0032453738 scopus 로고    scopus 로고
    • FtsI and FtsW are localized to the septum in Escherichia coli
    • Wang, L., M. K. Khattar, W. D. Donachie, and J. Lutkenhaus. 1998. FtsI and FtsW are localized to the septum in Escherichia coli. J. Bacteriol. 180:2810-2816.
    • (1998) J. Bacteriol. , vol.180 , pp. 2810-2816
    • Wang, L.1    Khattar, M.K.2    Donachie, W.D.3    Lutkenhaus, J.4
  • 60
    • 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., J. C. Chen, J.-M. Ghigo, D. Boyd, and J. Beckwith. 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
  • 62
    • 0025873897 scopus 로고
    • On the role of high molecular weight penicillin-binding proteins in the cell cycle of Escherichia coli
    • Wientjes, F. B., and N. Nanninga. 1991. On the role of 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
  • 63
    • 0027489263 scopus 로고
    • Cloning and sequencing of the cell division gene pbpB. which encodes penicillin-binding protein 2B in Bacillus subtilis
    • Yanouri, A., R. A. Daniel, J. Errington, and C. E. Buchanan. 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
  • 64
    • 0022389693 scopus 로고
    • Lysis of Escherichia coli by β-lactam antibiotics: Deletion analysis of the role of penicillin-binding proteins 1A and IB
    • Yousif, S. Y., J. K. Broome-Smith, and B. G. Spratt 1985. Lysis of Escherichia coli by β-lactam antibiotics: deletion analysis of the role of penicillin-binding proteins 1A and IB. J. Gen. Microbiol. 131:2839-2845.
    • (1985) J. Gen. Microbiol. , vol.131 , pp. 2839-2845
    • Yousif, S.Y.1    Broome-Smith, J.K.2    Spratt, B.G.3
  • 65
    • 0031933996 scopus 로고    scopus 로고
    • Localization of cell division protein FtsK to the Escherichia coli septum and identification of a potential N-terminal targeting domain
    • Yu, X.-C., A. H. Tran, Q. Sun, and W. Margolin. 1998. Localization of cell division protein FtsK to the Escherichia coli septum and identification of a potential N-terminal targeting domain. J. Bacteriol. 180:1296-1304.
    • (1998) J. Bacteriol. , vol.180 , pp. 1296-1304
    • Yu, X.-C.1    Tran, A.H.2    Sun, Q.3    Margolin, W.4


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