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Specific Binding of the Soluble Lytic Transglycosylase to the Murein Sacculus of Escherichia coli

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Part of the book series: Federation of European Microbiological Societies Symposium Series ((FEMS,volume 65))

Abstract

Murein hydrolases, which are ubiquitous among bacteria (Ghuysen, 1968), represent a class of potentially autolytic enzymes and hence must be controlled strictly. However, little is known about the cellular control mechanism (Höltje and Tuomanen, 1991). This is in contrast to the detailed knowledge of the biochemistry of the murein synthesizing enzymes and their specific inhibition by a wide range of antibiotics. Due to this lack of information we are still far from understanding how the typical bacteriolytic response to inhibitors of murein synthesis is triggered (Tomasz, 1979).

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References

  • Beachey, E.H., Keck, W., de Pedro, M.A. and Schwarz, U. (1981) Exoenzymatic activity of transglycosylase isolated from Escherichia coli. Eur. J. Biochem. 116, 355–358.

    Article  PubMed  CAS  Google Scholar 

  • Betzner, A. and Keck, W. (1989) Molecular cloning, overexpression and mapping of the sit gene encoding the soluble lytic transglycosylase of Escherichia coli. Mol. Gen. Genet. 219, 489–491.

    Article  PubMed  CAS  Google Scholar 

  • Betzner, A.S., Ferreira, L.C.S., Höltje, J.-V. and Keck, W. (1990) Control of the soluble lytic transglycosylase by the stringent response in Escherichia coli. FEMS Microbiol Lett. 67, 161–164.

    Article  CAS  Google Scholar 

  • Engel, H., Kazemier, B. and Keck, W. (1991) Murein-metabolizing enzymes from Escherichia coli: sequence analysis and controlled overexpression of the sit gene which encodes the soluble lytic transglycosylase. J. Bacteriol. 173, 6773–6782.

    PubMed  CAS  Google Scholar 

  • Fortin, Y., Phoenix, P. and Drapeau, G.R. (1990) Mutations conferring resistance to azide in Escherichia coli occur primarily in the sec A gene. J. Bacteriol. 172,6670–6610.

    Google Scholar 

  • Ghuysen, J.-M. (1968) Use of bacteriolytic enzymes in determination of wall structure and their role in cell metabolism. Bacteriol. Rev. 32, 425–464.

    PubMed  CAS  Google Scholar 

  • Höltje, J.-V. and Tuomanen, E. J. (1991) The murein hydrolases of Escherichia coli: properties, functions and impact on the course of infections in vivo. J. Gen. Microbiol. 137, 441–454.

    Article  PubMed  Google Scholar 

  • Höltje, J.-V., Mirelman, D., Sharon, N. and Schwarz, U. (1975) Novel type of murein transglycosylase in Escherichia coli. J. Bacteriol. 124, 1067–1076.

    PubMed  Google Scholar 

  • Ito, K., Wittekind, M., Nomura, M., Shiba, K., Yura, T., Muira, A. and Nashimoto, H. (1983) A temperature-sensitive mutant of E. coli exhibiting slow processing of exported proteins. Cell 32, 789–797.

    Article  PubMed  CAS  Google Scholar 

  • Kumamoto, C.A. and Beckwith, J. (1983) Mutations in a new gene, sec B, cause defective protein localization in Escherichia coli. J. Bacteriol. 154, 253–260.

    PubMed  CAS  Google Scholar 

  • Linnett, O.E. and Beechey, O.D. (1979) Inhibitors of the ATP synthetase system. Methods Enzymol. 55, 474–518.

    Google Scholar 

  • Oliver, D. and Beckwith, J. (1981) E. coli mutant pleiotropically defective in the export of secreted proteins. Cell 25, 765–772.

    Article  PubMed  CAS  Google Scholar 

  • Sancar, A., Hack, A.M. and Rupp, W.D. (1979) Simple method for identification of plasmid-coded proteins. J. Bacteriol. 137, 692–693.

    PubMed  CAS  Google Scholar 

  • Tabor, S. and Richardson, C.C. (1985) A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes. Proc. Natl. Acad. Sci. USA 82, 1074–1078.

    Article  PubMed  CAS  Google Scholar 

  • Tomasz, A. (1979) The mechanism of the irreversible antimicrobial effect of penicillins: how the beta lactam antibiotics kill and lyse bacteria. Annual Rev. Microbiol. 33, 113–137.

    Article  CAS  Google Scholar 

  • Walderich, B. and Höltje, J.-V. (1991) Subcellular distribution of the soluble lytic transglycosylase. J. Bacteriol. 173, 5668–5676.

    PubMed  CAS  Google Scholar 

  • Wickner, W., Messen, A.J.M. and Haiti, F.-U. (1991) The enzymology of protein translocation across the Escherichia coli plasma membrane. Annu. Rev. Biochem. 60, 101–124.

    Article  PubMed  CAS  Google Scholar 

  • Witholt, B., Boekhout, M. Brock, M. Kingma, J. van Heerikhuizen, H. and de Leij, L. An efficient and reproducible procedure for the formation of spheroplasts from variously grown Escherichia coli. Anal. Biochem. 74, 160–170.

    Google Scholar 

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© 1993 Springer Science+Business Media New York

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Romeis, T., Höltje, JV. (1993). Specific Binding of the Soluble Lytic Transglycosylase to the Murein Sacculus of Escherichia coli . In: de Pedro, M.A., Höltje, JV., Löffelhardt, W. (eds) Bacterial Growth and Lysis. Federation of European Microbiological Societies Symposium Series, vol 65. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9359-8_27

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  • DOI: https://doi.org/10.1007/978-1-4757-9359-8_27

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4757-9361-1

  • Online ISBN: 978-1-4757-9359-8

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