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Volumn 180, Issue 13, 1998, Pages 3441-3447

Membrane-bound lytic endotransglycosylase in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOSYLTRANSFERASE;

EID: 0031748682     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.13.3441-3447.1998     Document Type: Article
Times cited : (49)

References (52)
  • 2
    • 0022462392 scopus 로고
    • Specific location of penicillin-binding proteins within the cell envelope of Escherichia coli
    • Barbas, J. A., J. Diaz, A. Rodriguez-Tebar, and D. Vazquez. 1986. Specific location of penicillin-binding proteins within the cell envelope of Escherichia coli. J. Bacteriol. 165:269-275.
    • (1986) J. Bacteriol. , vol.165 , pp. 269-275
    • Barbas, J.A.1    Diaz, J.2    Rodriguez-Tebar, A.3    Vazquez, D.4
  • 3
    • 0029149360 scopus 로고
    • Gene 19 of plasmid R1 is required for both efficient conjugative DNA transfer and bacteriophage R17 infection
    • Bayer, M., R. Eferl, G. Zellnig, K. Teferle, A. Dijkstra, G. Koraimann, and G. Högenauer. 1995. Gene 19 of plasmid R1 is required for both efficient conjugative DNA transfer and bacteriophage R17 infection. J. Bacteriol. 177:4279-4288.
    • (1995) J. Bacteriol. , vol.177 , pp. 4279-4288
    • Bayer, M.1    Eferl, R.2    Zellnig, G.3    Teferle, K.4    Dijkstra, A.5    Koraimann, G.6    Högenauer, G.7
  • 4
    • 0019452243 scopus 로고
    • Exoenzymatic activity of transglycosylase isolated from Escherichia coli
    • Beachey, E. H., W. Keck, M. A. de Pedro, and U. Schwarz. 1981. Exoenzymatic activity of transglycosylase isolated from Escherichia coli. Eur. J. Biochem. 116:355-358.
    • (1981) Eur. J. Biochem. , vol.116 , pp. 355-358
    • Beachey, E.H.1    Keck, W.2    De Pedro, M.A.3    Schwarz, U.4
  • 5
    • 0028093382 scopus 로고
    • Analysis of the sodium dodecyl sulfate-stable peptidoglycan autolysins of selected gramnegative pathogens by using renaturing polyacrylamide gel electrophoresis
    • Bernadsky, G., T. J. Beveridge, and A. J. Clarke. 1994. Analysis of the sodium dodecyl sulfate-stable peptidoglycan autolysins of selected gramnegative pathogens by using renaturing polyacrylamide gel electrophoresis. J. Bacteriol. 176:5225-5232.
    • (1994) J. Bacteriol. , vol.176 , pp. 5225-5232
    • Bernadsky, G.1    Beveridge, T.J.2    Clarke, A.J.3
  • 6
    • 0024306520 scopus 로고
    • Molecular cloning, overexpression and mapping of the slt gene encoding the soluble lytic transglycosylase of Escherichia coli
    • Betzner, A. S., and W. Keck. 1989. Molecular cloning, overexpression and mapping of the slt gene encoding the soluble lytic transglycosylase of Escherichia coli. Mol. Gen. Genet. 219:489-491.
    • (1989) Mol. Gen. Genet. , vol.219 , pp. 489-491
    • Betzner, A.S.1    Keck, W.2
  • 7
    • 0027495480 scopus 로고
    • Complementation of growth defects in an ampC deletion mutant of Escherichia coli
    • Bishop, R. E., and J. H. Weiner. 1993. Complementation of growth defects in an ampC deletion mutant of Escherichia coli. FEMS Microbiol. Lett. 114:349-354.
    • (1993) FEMS Microbiol. Lett. , vol.114 , pp. 349-354
    • Bishop, R.E.1    Weiner, J.H.2
  • 9
    • 77956860575 scopus 로고
    • Lipoproteins, structure, function, biosynthesis and model for protein export
    • J.-M. Ghuysen and R. Hakenbeck (ed.), Elsevier Science Publishing, Inc., New York, N.Y.
    • Braun, V., and H. C. Wu. 1994. Lipoproteins, structure, function, biosynthesis and model for protein export, p. 319-341. In J.-M. Ghuysen and R. Hakenbeck (ed.), Bacterial cell wall. Elsevier Science Publishing, Inc., New York, N.Y.
    • (1994) Bacterial Cell Wall , pp. 319-341
    • Braun, V.1    Wu, H.C.2
  • 10
    • 0018956590 scopus 로고
    • Analysis of gene control signals by DNA fusion and cloning in Escherichia coli
    • Casabadan, M. J., and S. N. Cohen. 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
  • 11
    • 0029645404 scopus 로고
    • Structure and mechanism of glycosyl hydrolases
    • Davies, G., and B. Henrissat. 1995. Structure and mechanism of glycosyl hydrolases. Structure 3:853-859.
    • (1995) Structure , vol.3 , pp. 853-859
    • Davies, G.1    Henrissat, B.2
  • 12
    • 0029739727 scopus 로고    scopus 로고
    • Identification of new members of the lytic transglycosylase family in Haemophilus influenzae and Escherichia coli
    • Dijkstra, A. J., W. Keck. 1996. Identification of new members of the lytic transglycosylase family in Haemophilus influenzae and Escherichia coli. Microb. Drug Resist. 2:141-145.
    • (1996) Microb. Drug Resist. , vol.2 , pp. 141-145
    • Dijkstra, A.J.1    Keck, W.2
  • 13
    • 0029842085 scopus 로고    scopus 로고
    • Peptidoglycan as a barrier to transenvelope transport
    • Dijkstra, A. J., and W. Keck. 1996. Peptidoglycan as a barrier to transenvelope transport. J. Bacteriol. 178:5555-5562.
    • (1996) J. Bacteriol. , vol.178 , pp. 5555-5562
    • Dijkstra, A.J.1    Keck, W.2
  • 15
    • 0029052325 scopus 로고
    • Cloning and expression of a murein hydrolase lipoprotein from Escherichia coli
    • Ehlert, K., J.-V. Höltje, and M. F. Templin. 1995. Cloning and expression of a murein hydrolase lipoprotein from Escherichia coli. Mol. Microbiol. 16: 761-768.
    • (1995) Mol. Microbiol. , vol.16 , pp. 761-768
    • Ehlert, K.1    Höltje, J.-V.2    Templin, M.F.3
  • 16
    • 0025804758 scopus 로고
    • Domains in microbial β-1,4-glycanases: Sequence conservation, function, and enzyme families
    • Gilkes, N. R., B. Henrissat, D. G. Kilburn, R. C. Miller, Jr., and R. A. Warren. 1991. Domains in microbial β-1,4-glycanases: sequence conservation, function, and enzyme families. Microbiol. Rev. 55:303-315.
    • (1991) Microbiol. Rev. , vol.55 , pp. 303-315
    • Gilkes, N.R.1    Henrissat, B.2    Kilburn, D.G.3    Miller Jr., R.C.4    Warren, R.A.5
  • 17
    • 0023765918 scopus 로고
    • Separation and quantification of muropeptides with high-performance liquid chromatography
    • Glauner, B. 1988. Separation and quantification of muropeptides with high-performance liquid chromatography. Anal. Biochem. 172:451-464.
    • (1988) Anal. Biochem. , vol.172 , pp. 451-464
    • Glauner, B.1
  • 18
    • 0025168851 scopus 로고
    • Growth pattern of the murein sacculus of Escherichia coli
    • Glauner, B., and J.-V. Höltje. 1990. Growth pattern of the murein sacculus of Escherichia coli. J. Biol. Chem. 265:18988-18996.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18988-18996
    • Glauner, B.1    Höltje, J.-V.2
  • 20
    • 0025012287 scopus 로고
    • Isolation and separation of the glycan strands from murein of Escherichia coli by reversed-phase high-performance liquid chromatography
    • Harz, H., K. Burgdorf, and J.-V. Höltje. 1990. Isolation and separation of the glycan strands from murein of Escherichia coli by reversed-phase high-performance liquid chromatography. Anal. Biochem. 190:120-128.
    • (1990) Anal. Biochem. , vol.190 , pp. 120-128
    • Harz, H.1    Burgdorf, K.2    Höltje, J.-V.3
  • 21
    • 0028825276 scopus 로고
    • Automated construction and graphical presentation of protein blocks from unaligned sequences
    • Henikoff, S., J. G. Henikoff, W. J. Alford, and S. Pietrokovski. 1995. Automated construction and graphical presentation of protein blocks from unaligned sequences. Gene 163:GC17-26.
    • (1995) Gene , vol.163
    • Henikoff, S.1    Henikoff, J.G.2    Alford, W.J.3    Pietrokovski, S.4
  • 22
    • 0016726181 scopus 로고
    • Novel type of murein transglycosylase in Escherichia coli
    • Höltje, J.-V., D. Mirelman, N. Sharon, and U. Schwarz. 1975. Novel type of murein transglycosylase in Escherichia coli. J. Bacteriol. 124:1067-1076.
    • (1975) J. Bacteriol. , vol.124 , pp. 1067-1076
    • Höltje, J.-V.1    Mirelman, D.2    Sharon, N.3    Schwarz, U.4
  • 23
    • 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
  • 24
    • 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
  • 25
    • 0019309069 scopus 로고
    • Accumulation of glyceride-containing precursor of the outer membrane lipoprotein in the cytoplasmic membrane of Escherichia coli treated with globomycin
    • Hussain, M., S. Ichihara, and S. Mizushima. 1980. Accumulation of glyceride-containing precursor of the outer membrane lipoprotein in the cytoplasmic membrane of Escherichia coli treated with globomycin. J. Biol. Chem. 255:3707-3712.
    • (1980) J. Biol. Chem. , vol.255 , pp. 3707-3712
    • Hussain, M.1    Ichihara, S.2    Mizushima, S.3
  • 26
    • 0025675856 scopus 로고
    • High efficiency transformation of Escherichia coli with plasmids
    • Inoue, H., H. Nojima, and H. Okayama. 1990. High efficiency transformation of Escherichia coli with plasmids. Gene 96:23-28.
    • (1990) Gene , vol.96 , pp. 23-28
    • Inoue, H.1    Nojima, H.2    Okayama, H.3
  • 27
    • 0026575959 scopus 로고
    • Protein D, the immunoglobulin D-binding protein of Haemophilus influenzae, is a lipoprotein
    • Janson, H., L.-O. Hedén, and A. Forsgren, 1992. Protein D, the immunoglobulin D-binding protein of Haemophilus influenzae, is a lipoprotein. Infect. Immun. 60:1336-1342.
    • (1992) Infect. Immun. , vol.60 , pp. 1336-1342
    • Janson, H.1    Hedén, L.-O.2    Forsgren, A.3
  • 30
    • 0023669069 scopus 로고
    • The physical map of the whole E. coli chromosome: Application of a new strategy for rapid analysis and sorting of a large genomic library
    • Kohara, Y., K. Akiyama, and K. Isono. 1987. The physical map of the whole E. coli chromosome: application of a new strategy for rapid analysis and sorting of a large genomic library. Cell 50:495-508.
    • (1987) Cell , vol.50 , pp. 495-508
    • Kohara, Y.1    Akiyama, K.2    Isono, K.3
  • 31
    • 0018844498 scopus 로고
    • Escherichia coli murein transglycosylase: Purification by affinity chromatography and interaction with polynucleotides
    • Kusser, W., and U. Schwarz. 1980. Escherichia coli murein transglycosylase: purification by affinity chromatography and interaction with polynucleotides. Eur. J. Biochem. 103:277-281.
    • (1980) Eur. J. Biochem. , vol.103 , pp. 277-281
    • Kusser, W.1    Schwarz, U.2
  • 32
    • 0030955326 scopus 로고    scopus 로고
    • Outer membrane localization of murein hydrolases: MltA, a third lipoprotein lytic transglycosylase in Escherichia coli
    • Lommatzsch, J., M. Templin, A. Kraft, W. Vollmer, and J.-V. Höltje. 1997. Outer membrane localization of murein hydrolases: MltA, a third lipoprotein lytic transglycosylase in Escherichia coli. J. Bacteriol. 179:5465-5470.
    • (1997) J. Bacteriol. , vol.179 , pp. 5465-5470
    • Lommatzsch, J.1    Templin, M.2    Kraft, A.3    Vollmer, W.4    Höltje, J.-V.5
  • 33
    • 0016841078 scopus 로고
    • Electrophoretic resolution of the "major outer membrane protein" of Escherichia coli K12 into four bands
    • Lugtenberg, B., J. Meijers, R. Peters, P. van der Hoek, and L. van Alphen. 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
    • Lugtenberg, B.1    Meijers, J.2    Peters, R.3    Van Der Hoek, P.4    Van Alphen, L.5
  • 34
  • 35
    • 0029999636 scopus 로고    scopus 로고
    • A family of lysozyme-like virulence factors in bacterial pathogens of plants and animals
    • Mushegian, A. R., K. J. Fullner, E. V. Koonin, and E. W. Nester. 1996. A family of lysozyme-like virulence factors in bacterial pathogens of plants and animals. Proc. Natl. Acad. Sci. USA 93:7321-7326.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7321-7326
    • Mushegian, A.R.1    Fullner, K.J.2    Koonin, E.V.3    Nester, E.W.4
  • 36
    • 0024101177 scopus 로고
    • Cloning, sequencing and expression of a Bacillus bacteriolytic enzyme in Escherichia coli
    • Potvin, C., D. Leclerc, G. Tremblay, A. Asselin, and G. Bellemare. 1988. Cloning, sequencing and expression of a Bacillus bacteriolytic enzyme in Escherichia coli. Mol. Gen. Genet. 21:241-248.
    • (1988) Mol. Gen. Genet. , vol.21 , pp. 241-248
    • Potvin, C.1    Leclerc, D.2    Tremblay, G.3    Asselin, A.4    Bellemare, G.5
  • 38
    • 0028016512 scopus 로고
    • Specific interaction of penicillin-binding proteins 3 and 7/8 with the soluble lytic transglycosylase in Escherichia coli
    • Romeis, T., and J.-V. Höltje. 1994. Specific interaction of penicillin-binding proteins 3 and 7/8 with the soluble lytic transglycosylase in Escherichia coli. J. Biol. Chem. 269:21603-21607.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21603-21607
    • Romeis, T.1    Höltje, J.-V.2
  • 39
    • 0027240681 scopus 로고
    • Characterization of three different lytic transglycosylases in Escherichia coli
    • Romeis, T., W. Vollmer, and J.-V. Höltje. 1993. Characterization of three different lytic transglycosylases in Escherichia coli. FEMS Microbiol. Lett. 111:141-146.
    • (1993) FEMS Microbiol. Lett. , vol.111 , pp. 141-146
    • Romeis, T.1    Vollmer, W.2    Höltje, J.-V.3
  • 42
    • 0014674516 scopus 로고
    • Autolytic enzymes and cell division of Escherichia coli
    • Schwarz, U., A. Asmus, and H. Frank. 1969. Autolytic enzymes and cell division of Escherichia coli. J. Mol. Biol. 41:419-429.
    • (1969) J. Mol. Biol. , vol.41 , pp. 419-429
    • Schwarz, U.1    Asmus, A.2    Frank, H.3
  • 44
    • 0017327167 scopus 로고
    • Properties of the penicillin-binding proteins of Escherichia coli K12
    • Spratt, B. G. 1977. Properties of the penicillin-binding proteins of Escherichia coli K12. Eur. J. Biochem. 72:341-352.
    • (1977) Eur. J. Biochem. , vol.72 , pp. 341-352
    • Spratt, B.G.1
  • 45
    • 0016669460 scopus 로고
    • Bacterial-cell wall peptidoglycan fragments produced by phage lambda or Vi II endolysin and containing 1,6-anhydro-N-acetylmuramic acid
    • Taylor, A., B. C. Das, and J. van Heijenoort. 1975. Bacterial-cell wall peptidoglycan fragments produced by phage lambda or Vi II endolysin and containing 1,6-anhydro-N-acetylmuramic acid. J. Biochem. 53:47-54.
    • (1975) J. Biochem. , vol.53 , pp. 47-54
    • Taylor, A.1    Das, B.C.2    Van Heijenoort, J.3
  • 46
    • 14444282989 scopus 로고    scopus 로고
    • Unpublished results
    • Templin, M. F. Unpublished results.
    • Templin, M.F.1
  • 47
    • 0028874610 scopus 로고
    • Structure of the 70-kDa soluble lytic transglycosylase complexed with bulgecin A. Implications for the enzymatic mechanism
    • Thunnissen, A.-M., H. J. Rozeboom, K. H. Kalk, and B. W. Dijkstra. 1995. Structure of the 70-kDa soluble lytic transglycosylase complexed with bulgecin A. Implications for the enzymatic mechanism. Biochemistry 34:12729-12737.
    • (1995) Biochemistry , vol.34 , pp. 12729-12737
    • Thunnissen, A.-M.1    Rozeboom, H.J.2    Kalk, K.H.3    Dijkstra, B.W.4
  • 48
    • 0002852556 scopus 로고
    • Murein hydrolases: Enzymes in search of a physiological function
    • R. Hakenbeck, J.-V. Höltje, and H. Labischinski (ed.), Walter de Gruyter and Co., Berlin, Germany
    • Tomasz, A. 1983. Murein hydrolases: enzymes in search of a physiological function, p. 155-172. In R. Hakenbeck, J.-V. Höltje, and H. Labischinski (ed.), The target of penicillin. Walter de Gruyter and Co., Berlin, Germany.
    • (1983) The Target of Penicillin , pp. 155-172
    • Tomasz, A.1
  • 49
    • 0027979985 scopus 로고
    • Purification and properties of a membrane-bound lytic transglycosylase from Escherichia coli
    • Ursinus, A., and J.-V, Höltje. 1994. Purification and properties of a membrane-bound lytic transglycosylase from Escherichia coli. J. Bacteriol. 176: 338-343.
    • (1994) J. Bacteriol. , vol.176 , pp. 338-343
    • Ursinus, A.1    Höltje, J.-V.2
  • 50
    • 0025939650 scopus 로고
    • Subcellular distribution of the soluble lytic transglycosylase in Escherichia coli
    • Walderich, B., and J.-V. Höltje. 1991. Subcellular distribution of the soluble lytic transglycosylase in Escherichia coli. J. Bacteriol. 173:5668-5676.
    • (1991) J. Bacteriol. , vol.173 , pp. 5668-5676
    • Walderich, B.1    Höltje, J.-V.2
  • 51
    • 84873775015 scopus 로고
    • Bagshaped macromolecules: A new outlook on bacterial cell walls
    • Weidel, W., and H. Pelzer. 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
  • 52
    • 0024279918 scopus 로고
    • A single amino acid determinant of the membrane localization of lipoproteins in E. coli
    • Yamaguchi, K., F. Yu, and M. Inouye. 1988. A single amino acid determinant of the membrane localization of lipoproteins in E. coli. Cell 53:423-432.
    • (1988) Cell , vol.53 , pp. 423-432
    • Yamaguchi, K.1    Yu, F.2    Inouye, M.3


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