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Volumn 25, Issue 4, 1997, Pages 671-681

Localization of the Escherichia coli cell division protein FtsI (PBP3) to the division site and cell pole

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; BINDING SITE; CELL DIVISION; CELL GROWTH; CELL POLARITY; CELLULAR DISTRIBUTION; ESCHERICHIA COLI; IMMUNOELECTRON MICROSCOPY; NONHUMAN; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTEIN SYNTHESIS;

EID: 0030881627     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1997.5041869.x     Document Type: Article
Times cited : (93)

References (49)
  • 1
    • 8944221179 scopus 로고    scopus 로고
    • FtsZ ring formation in fts mutants
    • Addinall, S.G., Bi, E., and Lutkenhaus, J. (1996) FtsZ ring formation in fts mutants. J Bacterial 178: 3877-3884.
    • (1996) J Bacterial , vol.178 , pp. 3877-3884
    • Addinall, S.G.1    Bi, E.2    Lutkenhaus, J.3
  • 2
    • 0030448723 scopus 로고    scopus 로고
    • FtsA is localized to the septum in an FtsZ-dependent manner
    • Addinall, S.G., and Lutkenhaus, J. (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
  • 3
    • 0006723686 scopus 로고
    • New methods in electron microscopy help elucidate the structure of the murein sacculus and the distribution of penicillin-binding proteins
    • de Pedro, M.A., Höltje, J.-V., and Loffelhardt, W. (eds). New York: Plenum Press
    • Beveridge, T.J. (1993) New methods in electron microscopy help elucidate the structure of the murein sacculus and the distribution of penicillin-binding proteins. In Bacterial Growth and Lysis: Metabolism and Structure of the Bacterial Sacculus. de Pedro, M.A., Höltje, J.-V., and Loffelhardt, W. (eds). New York: Plenum Press, pp. 57-69.
    • (1993) Bacterial Growth and Lysis: Metabolism and Structure of the Bacterial Sacculus , pp. 57-69
    • Beveridge, T.J.1
  • 4
    • 0026059127 scopus 로고
    • FtsZ ring structure associated with division in Escherichia coli
    • Bi, E., and Lutkenhaus, J. (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
  • 5
    • 0026687729 scopus 로고
    • An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins
    • Bork, P., Sander, C., and Valencia, V. (1992) An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins. Proc Natl Acad Sci USA 89: 7290-7294.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 7290-7294
    • Bork, P.1    Sander, C.2    Valencia, V.3
  • 6
    • 0019511038 scopus 로고
    • Evidence for involvement of penicillin-binding protein 3 in murein synthesis during septation but not during cell elongation
    • Botta, G.A., and Park, J.T. (1981) Evidence for involvement of penicillin-binding protein 3 in murein synthesis during septation but not during cell elongation. J Bacteriol 145: 333-340.
    • (1981) J Bacteriol , vol.145 , pp. 333-340
    • Botta, G.A.1    Park, J.T.2
  • 7
    • 0024445203 scopus 로고
    • Membrane topology of penicillin-binding protein 3 of Escherichia coli
    • Bowler, L.D., and Spratt, B.G. (1989) Membrane topology of penicillin-binding protein 3 of Escherichia coli. Mol Microbiol 3: 1277-1286.
    • (1989) Mol Microbiol , vol.3 , pp. 1277-1286
    • Bowler, L.D.1    Spratt, B.G.2
  • 8
    • 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
  • 9
    • 0025803531 scopus 로고
    • The FtsQ protein of Escherichia coli: Membrane topology, abundance, and cell division phenotypes due to overproduction and insertion mutations
    • Carson, M.J., Barondess, J., and Beckwith, J. (1991) The FtsQ protein of Escherichia coli: membrane topology, abundance, and cell division phenotypes due to overproduction and insertion mutations. J Bacteriol 173: 2187-2195.
    • (1991) J Bacteriol , vol.173 , pp. 2187-2195
    • Carson, M.J.1    Barondess, J.2    Beckwith, J.3
  • 10
    • 0029844403 scopus 로고    scopus 로고
    • Differential trafficking and timed localization of two chitin synthase proteins, Chs2p and Chs3p
    • Chuang, J.S., and Schekman, R. (1996) Differential trafficking and timed localization of two chitin synthase proteins, Chs2p and Chs3p. J Cell Biol 135: 597-610.
    • (1996) J Cell Biol , vol.135 , pp. 597-610
    • Chuang, J.S.1    Schekman, R.2
  • 12
    • 0000926337 scopus 로고
    • Cell division: Parameter values and the process
    • Neidhardt, F.C. et al. (eds). Washington, DC: American Society for Microbiology
    • Donachie, W.D., and Robinson, A.C. (1987) Cell division: parameter values and the process. In Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology. Neidhardt, F.C. et al. (eds). Washington, DC: American Society for Microbiology, pp. 1578-1593.
    • (1987) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , pp. 1578-1593
    • Donachie, W.D.1    Robinson, A.C.2
  • 13
    • 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
  • 15
    • 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
  • 16
    • 0030910954 scopus 로고    scopus 로고
    • Dynamic, mitotic-like behavior 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 behavior 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
  • 17
    • 0027062784 scopus 로고
    • FtsL, an essential cytoplasmic membrane protein involved in cell division in Escherichia coli
    • Guzman, L., Barondess, J.J., and Beckwith, J. (1992) FtsL, an essential cytoplasmic membrane protein involved in cell division in Escherichia coli. J Bacteriol 174: 7716-7728.
    • (1992) J Bacteriol , vol.174 , pp. 7716-7728
    • Guzman, L.1    Barondess, J.J.2    Beckwith, J.3
  • 18
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman, L.M., Belin, D., 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
  • 19
    • 0030756250 scopus 로고    scopus 로고
    • Domain-swapping analysis of FtsI, FtsL, and FtsQ: Bitopic membrane proteins essential for cell division in Escherichia coli
    • in press
    • Guzman, L.M., Weiss, D.S., and Beckwith, J. (1997) Domain-swapping analysis of FtsI, FtsL, and FtsQ: bitopic membrane proteins essential for cell division in Escherichia coli. J. Bacteriol (in press).
    • (1997) J. Bacteriol
    • Guzman, L.M.1    Weiss, D.S.2    Beckwith, J.3
  • 20
    • 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 de Boer, P.A.J. (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
  • 21
    • 0030818705 scopus 로고    scopus 로고
    • The membrane-bound cell division protein PivlB is localized to the division site in Bacillus subtilis
    • in press
    • Harry, E.J., and Wake, R.G. (1997) The membrane-bound cell division protein PivlB is localized to the division site in Bacillus subtilis. Mol Microbiol (in press).
    • (1997) Mol Microbiol
    • Harry, E.J.1    Wake, R.G.2
  • 22
    • 0029820401 scopus 로고    scopus 로고
    • A hypothetical holoenzyme involved in the replication of the murein sacculus of Escherichia coli
    • Höltje, 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
    • Höltje, J.-V.1
  • 23
    • 0019819673 scopus 로고
    • Peptidoglycan synthetic enzyme activities of highly purified penicillin-binding protein 3 in Escherichia coli: A septum-forming reaction sequence
    • Ishino, F., and Matsuhashi, M. (1981) Peptidoglycan synthetic enzyme activities of highly purified penicillin-binding protein 3 in Escherichia coli: A septum-forming reaction sequence. Biochem Biophys Res Commun 101: 905-911.
    • (1981) Biochem Biophys Res Commun , vol.101 , pp. 905-911
    • Ishino, F.1    Matsuhashi, M.2
  • 24
    • 0023161124 scopus 로고
    • Lateral diffusion of proteins in membranes
    • Jacobson, K., Ishihara, A., and Inman, R. (1987) Lateral diffusion of proteins in membranes. Annu Rev Physiol 49: 163-175.
    • (1987) Annu Rev Physiol , vol.49 , pp. 163-175
    • Jacobson, K.1    Ishihara, A.2    Inman, R.3
  • 25
    • 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., Addinall, S.G., Stedul, K.H., Boyle, D.S., Lutkenhaus, J., and Donachie, W.D. (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
  • 26
    • 0029918758 scopus 로고    scopus 로고
    • Transcription factor SpoOA switches the localization of the cell division protein FtsZ from a medial to a bipolar pattern in Bacillus subtilis
    • Levin, P., and Losick, R. (1996) Transcription factor SpoOA 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.1    Losick, R.2
  • 27
    • 0031001565 scopus 로고    scopus 로고
    • Bipolar localization of a chromosome partition protein in Bacillus subtilis
    • Lin, D.C.H., Levin, P.A., and Grossman, A.D. (1997) Bipolar localization of a chromosome partition protein in Bacillus subtilis. Proc Natl Acad Sci USA 94: 4721-4726.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4721-4726
    • Lin, D.C.H.1    Levin, P.A.2    Grossman, A.D.3
  • 28
    • 0027184918 scopus 로고
    • FtsZ ring in bacterial cytokinesis
    • Lutkenhaus, J. (1993) FtsZ ring in bacterial cytokinesis. Mol Microbiol 9: 403-409.
    • (1993) Mol Microbiol , vol.9 , pp. 403-409
    • Lutkenhaus, J.1
  • 29
    • 0029851154 scopus 로고    scopus 로고
    • Colocalization of cell division proteins FtsZ and FtsA to cytoskeletal structures in living Escherichia coli cells by using green fluorescent protein
    • Ma, X., Ehrhardt, D., and Margolin, W. (1996) Colocalization of cell division proteins FtsZ and FtsA to cytoskeletal structures in living Escherichia coli cells by using green fluorescent protein. Proc Natl Acad Sci USA 93: 12998-13003.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 12998-13003
    • Ma, X.1    Ehrhardt, D.2    Margolin, W.3
  • 30
    • 0030901361 scopus 로고    scopus 로고
    • Cell cycle-dependent polar localization of chromosome partitioning proteins in Caulobacter crescentus
    • Mohl, D.A., and Gober, J.W. (1997) Cell cycle-dependent polar localization of chromosome partitioning proteins in Caulobacter crescentus. Cell 88: 675-684.
    • (1997) Cell , vol.88 , pp. 675-684
    • Mohl, D.A.1    Gober, J.W.2
  • 31
    • 0024439293 scopus 로고
    • Determination of the cleavage site involved in C-terminal processing of penicillin-binding protein 3 of Escherichia coli
    • Nagasawa, H., Sakagami, Y., Suzuki, A., Suzuki, H., Hara, H., and Hirota, Y. (1989) Determination of the cleavage site involved in C-terminal processing of penicillin-binding protein 3 of Escherichia coli. J Bacteriol 171: 5890-5893.
    • (1989) J Bacteriol , vol.171 , pp. 5890-5893
    • Nagasawa, H.1    Sakagami, Y.2    Suzuki, A.3    Suzuki, H.4    Hara, H.5    Hirota, Y.6
  • 33
    • 0031018531 scopus 로고    scopus 로고
    • Inactivation of FtsI inhibits constriction of the FtsZ cytokinetic ring and delays assembly of FtsZ rings at potential division sites
    • Pogliano, J., Pogliano, K., Weiss, D.S., Losick, R., and Beckwith, J. (1997) Inactivation of FtsI inhibits constriction of the FtsZ cytokinetic ring and delays 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
  • 34
    • 0029610802 scopus 로고
    • Visualization of the subcellular location of sporulation proteins in Bacillus subtilis using immunofluorescence microscopy
    • Pogliano, K., Harry, E., and Losick, R. (1995) Visualization of the subcellular location of sporulation proteins in Bacillus subtilis using immunofluorescence microscopy. Mol Microbiol 18: 459-470.
    • (1995) Mol Microbiol , vol.18 , pp. 459-470
    • Pogliano, K.1    Harry, E.2    Losick, R.3
  • 36
    • 0026778964 scopus 로고
    • Escherichia coli cell-division gene ftsZ encodes a novel GTP-binding protein
    • RayChaudhuri, D., and Park, J.T. (1992) Escherichia coli cell-division gene ftsZ encodes a novel GTP-binding protein. Nature 359: 251-254.
    • (1992) Nature , vol.359 , pp. 251-254
    • Raychaudhuri, D.1    Park, J.T.2
  • 37
    • 0028016512 scopus 로고
    • Specific interactions of penicillin-binding proteins 3 and 7/8 with soluble lytic transglycosylase in Escherichia coli
    • Romies, T., and Höltje, J.-V. (1994) Specific interactions 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
    • Romies, T.1    Höltje, J.-V.2
  • 38
    • 0027961077 scopus 로고
    • Correlation between the structure and biochemical function of FtsA, an essential cell division protein of the actin family
    • Sanchez, M., Valencia, A., Ferrandez, M.J., Sander, C., and Vicente, M. (1994) Correlation between the structure and biochemical function of FtsA, an essential cell division protein of the actin family. EMBO J 13: 4919-4925.
    • (1994) EMBO J , vol.13 , pp. 4919-4925
    • Sanchez, M.1    Valencia, A.2    Ferrandez, M.J.3    Sander, C.4    Vicente, M.5
  • 39
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • Singer, S.J., and Nicolson, G.L. (1972) The fluid mosaic model of the structure of cell membranes. Science 175: 720-731.
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 40
    • 0017327167 scopus 로고
    • Properties of the penicillin-binding proteins of Escherichia coli K-12
    • Spratt, B.G. (1977) Properties of the penicillin-binding proteins of Escherichia coli K-12. Eur J Biochem 72: 341-342.
    • (1977) Eur J Biochem , vol.72 , pp. 341-342
    • Spratt, B.G.1
  • 41
    • 0016837552 scopus 로고
    • Penicillin-binding proteins and cell shape in E. coli
    • Spratt, B.G., and Pardee, A.B. (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
  • 42
    • 0023974826 scopus 로고
    • An Escherichia coli mutation preventing degradation of abnormal periplasmic proteins
    • Strauch, K.L., and Beckwith, J. (1988) An Escherichia coli mutation preventing degradation of abnormal periplasmic proteins. Proc Natl Acad Sci USA 85: 1576-1580.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 1576-1580
    • Strauch, K.L.1    Beckwith, J.2
  • 43
    • 0023571657 scopus 로고
    • High-copy-number and low-copy-number plasmid vectors for lacZ α-complementation and chloramphenicol- or kanamycin-resistance selection
    • Takeshita, S., Masahiro, S., Toba, M., Masahashi, W., and Hashimoto-Gotoh, T. (1987) High-copy-number and low-copy-number plasmid vectors for lacZ α-complementation and chloramphenicol- or kanamycin-resistance selection. Gene 61: 63-74.
    • (1987) Gene , vol.61 , pp. 63-74
    • Takeshita, S.1    Masahiro, S.2    Toba, M.3    Masahashi, W.4    Hashimoto-Gotoh, T.5
  • 44
    • 0022641871 scopus 로고
    • Interaction of FtsA and PBP3 proteins in the Escherichia coli septum
    • Tormo, A., Ayala, J.A., de Pedro, M.A., and Vincente, M. (1986) Interaction of FtsA and PBP3 proteins in the Escherichia coli septum. J Bacteriol 166: 985-992.
    • (1986) J Bacteriol , vol.166 , pp. 985-992
    • Tormo, A.1    Ayala, J.A.2    De Pedro, M.A.3    Vincente, M.4
  • 45
    • 0029781806 scopus 로고    scopus 로고
    • Affinity chromatography as a means to study multienzyme complexes involved in murein synthesis
    • von Rechenberg, M., Ursinus, A., and Höltje, J.-V. (1996) Affinity chromatography as a means to study multienzyme complexes involved in murein synthesis. Microb Drug Resistance 2: 155-157.
    • (1996) Microb Drug Resistance , vol.2 , pp. 155-157
    • Rechenberg, M.1    Ursinus, A.2    Höltje, J.-V.3
  • 46
    • 0026802221 scopus 로고
    • Quantitative determination of FtsA at different growth rates in Escherichia coli using monoclonal antibodies
    • Wang, H., and Gayda, R.C. (1992) Quantitative determination of FtsA at different growth rates in Escherichia coli using monoclonal antibodies. Mol Microbiol 6: 2517-2524.
    • (1992) Mol Microbiol , vol.6 , pp. 2517-2524
    • Wang, H.1    Gayda, R.C.2
  • 47
    • 0030901736 scopus 로고    scopus 로고
    • Bipolar localization of the replication origin regions of chromosomes in vegetative and sporulating cells of B. subtilis
    • Webb, C.D., Teleman, A., Gordon, S., Straight, A., Belmont, A., Lin, D.C., Grossman, A.D., and Losick, R. (1997) Bipolar localization of the replication origin regions of chromosomes in vegetative and sporulating cells of B. subtilis. Cell 88: 667-674.
    • (1997) Cell , vol.88 , pp. 667-674
    • Webb, C.D.1    Teleman, A.2    Gordon, S.3    Straight, A.4    Belmont, A.5    Lin, D.C.6    Grossman, A.D.7    Losick, R.8
  • 48
    • 0024381715 scopus 로고
    • Rate and topography of peptidoglycan synthesis during cell division in Escherichia coli: Concept of a leading edge
    • Wientjes, F.B., and Nanninga, N. (1989) Rate and topography of peptidoglycan synthesis during cell division in Escherichia coli: concept of a leading edge. J Bacteriol 171: 3412-3419.
    • (1989) J Bacteriol , vol.171 , pp. 3412-3419
    • Wientjes, F.B.1    Nanninga, N.2
  • 49
    • 0020558201 scopus 로고
    • Labeling pattern of major penicillin-binding proteins of Escherichia coli during the division cycle
    • Wientjes, F.B., Olihoek, A.J.M., Schwarz, U., and Nanninga, N. (1983) Labeling pattern of major penicillin-binding proteins of Escherichia coli during the division cycle. J Bacteriol 153: 1287-1293.
    • (1983) J Bacteriol , vol.153 , pp. 1287-1293
    • Wientjes, F.B.1    Olihoek, A.J.M.2    Schwarz, U.3    Nanninga, N.4


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