1887

Abstract

H growing exponentially was labelled with -acetyl[C]glucosamine, which became incorporated into the peptidoglycan. The portion of peptidoglycan not linked to teichoic acid (60–75% of the whole) was degraded with muramidase to yield disaccharide-peptide monomers and dimers, trimers and oligomers formed by biosynthetic cross-linking of the monomers. The degree of -acetylation of these fragments was also examined. Pulse-chase experiments showed that the proportion of label initially in the monomer fraction immediately after the 1 min pulse declined rapidly during a 3 min chase, while the oligomer fraction (fragments greater than trimer) gained the radioactivity proportionately. The radioactivity of the dimer and trimer fractions remained virtually unchanged. At 4 min after the commencement of labelling (i.e. approx. one-tenth of a generation time) final values had been reached. The -acetylation of all fragments had achieved final values even at 1 min, except for the monomer fraction, which showed an increase from 40% to 60% during the first 3 min of chase. Although -acetylation was clearly a very rapid process, no -acetylated peptidoglycan lipid-intermediates could be detected.

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1989-11-01
2022-01-28
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References

  1. Anderson J. S., Matsuhashi M., Haskin M. A., Strominger J. L. 1967; Biosynthesis of the peptidoglycan of bacterial cell wall. II. Phospholipid carriers in the reaction sequence. Journal of Biological Chemistry 242:3180–3190
    [Google Scholar]
  2. Blümel P., Uecker W., Giesbrecht P. 1979; Zero order kinetics of cell wall turnover in Staphylococcus aureus. Archives of Microbiology 121:103–110
    [Google Scholar]
  3. Burman L. G., Park J. T. 1984; Molecular model for elongation of the murein sacculus of Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America 81:1844–1848
    [Google Scholar]
  4. Dezéleé P., Shockman G. D. 1975; Studies of the formation of peptide cross-links in the cell wall peptidoglycan of Streptococcus faecalis. Journal of Biological Chemistry 250:6806–6816
    [Google Scholar]
  5. Dougherty T. J. 1983a; Synthesis and modification of the peptidoglycan in Neisseria gonorrhoeae. FEMS Microbiology Letters 17:51–53
    [Google Scholar]
  6. Dougherty T. J. 1983b; Peptidoglycan synthesis in Neisseria gonorrhoeae strains sensitive and intrinsically resistant to β-lactam antibiotics. Journal of Bacteriology 153:429–435
    [Google Scholar]
  7. Ghuysen J. -M., Strominger J. L. 1963; Structure of the cell wall of Staphylococcus aureus strain Copenhagen II. Separation and structure of disaccharides. Biochemistry 2:1119–1125
    [Google Scholar]
  8. Ghuysen J. -M., Dierickx L., Coyette J., Leyh-Bouille M., Guinand M., Campbell J. N. 1969; An improved technique for the preparation of Streptomyces peptidases and N-acetylmuramyl-l-alanine amidase active on bacterial wall peptidoglycans. Biochemistry 8:213–219
    [Google Scholar]
  9. Gmeiner J., Kroll H. -P. 1981; Murein biosynthesis and O-acetylation of N-acetylmuramic acid during the cell division cycle of Proteus mirabilis. European Journal of Biochemistry 117:171–177
    [Google Scholar]
  10. Gmeiner J., Sarnow E. 1987; Murein biosynthesis in synchronized cells of Proteus mirabilis. Quantitative analysis of O-acetylated murein sub-units and of chain terminaors incorporated into the sacculus during the cell cycle. European Journal of Biochemistry 163:389–395
    [Google Scholar]
  11. Hash J. H., Rothlauf M. V. 1967; The N, O- diacetylmuramidase of Chalaropsis species. Purification and crystallization. Journal of Biological Chemistry 242:5586–5590
    [Google Scholar]
  12. Heinrikson R. L., Meredith S. C. 1984; Amino acid analysis by reverse phase high-performance liquid chromatography: precolumn derivatisation with phenylisothiocyanate. Analytical Biochemistry 136:65–67
    [Google Scholar]
  13. Higashi Y., Strominger J. L., Sweeley C. C. 1967; Structure of a lipid intermediate in cell wall biosynthesis; a derivative of C55-isoprenoid alcohol. Proceedings of the National Academy of Sciences of the United States of America 57:1878–1884
    [Google Scholar]
  14. Johannsen L., Labischinski H., Reinecke B., Giesbrecht P. 1983; Changes in the chemical structure of walls of Staphylococcus aureus grown in the presence of chloramphenicol. FEMS Microbiology tetters 16:313–316
    [Google Scholar]
  15. Lear A. L., Perkins H. R. 1983; Degrees of O-acetylation and cross-linking of the peptidoglycan of Neisseria gonorrhoeae during growth. Journal of General Microbiology 129:885–888
    [Google Scholar]
  16. Lear A. L., Perkins H. R. 1986; O-Acetylation of peptidoglycan in Neisseria gonorrhoeae. Investigation of lipid-linked intermediates and glycan chains newly incorporated into the cell wall. Journal of General Microbiology 132:2413–2420
    [Google Scholar]
  17. Mandelstam M. H., Strominger J. L. 1961; On the structure of the cell wall of Staphylococcus aureus (Copenhagen). Biochemical and Biophysical Research Communications 5:466–471
    [Google Scholar]
  18. Martin H. H., Gmeiner J. 1979; Modification of peptidoglycan structure by penicillin-action in cell walls of Proteus mirabilis. European Journal of Biochemistry 95:487–495
    [Google Scholar]
  19. Matsuhashi M., Dietrich C. P., Strominger J. L. 1967; Biosynthesis of the peptidoglycan of bacterial cell walls. III. The role of soluble ribonucleic acid and of lipid intermediates in glycine incorporation in Staphylococcus aureus. Journal of Biological Chemistry 242:3191–3206
    [Google Scholar]
  20. Oldmixon E. H., Dezéleé P., Ziskin M. C., Shockman G. D. 1976; Monomer addition as a mechanism of forming peptide cross-links in the cell wall peptidoglycan of Streptococcus faecalis ATCC 9790. European Journal of Biochemistry 68:271–280
    [Google Scholar]
  21. De Pedro M. A., Schwarz U. 1981; Heterogeneity of newly inserted and pre-existing murein in the sacculus of Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America 78:5856–5866
    [Google Scholar]
  22. Siewert G., Strominger J. L. 1968; Biosynthesis of the peptidoglycan of bacterial cell walls. Formation of the isoglutamine amino group in the cell wall of Staphylococcus aureus. Journal of Biological Chemistry 243:783–790
    [Google Scholar]
  23. Tipper D. J., Strominger J. L. 1968; Biosynthesis of the peptidoglycan of bacterial cell walls. XII. Inhibition of cross-linking by penicillins and cephalosporins: studies in Staphylococcus aureus in vivo. Journal of Biological Chemistry 243:3169–3179
    [Google Scholar]
  24. Ward J. B. 1981; Teichoic and teichuronic acids: biosynthesis, assembly and location. Microbiological Reviews 45:211–243
    [Google Scholar]
  25. Wyke A. W., Ward J. B., Hayes M. V., Curtis N. A. C. 1981; A role in vivo for penicillin binding protein 4 of Staphylococcus aureus. European Journal of Biochemistry 119:389–393
    [Google Scholar]
  26. Yokoyama K., Mizuguchi H., Araki Y., Kaya S., Ito E. 1989; Biosynthesis of linkage units for teichoic acids in Gram-positive bacteria: distribution of related enzymes and their specificities for UDP-sugars and lipid-linked intermediates. Journal of Bacteriology 171:940–946
    [Google Scholar]
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