Abstract
O-acetylated peptidoglycan was purified from Proteus mirabilis grown in the presence of specifically radiolabelled glucosamine derivatives, and the migration of the radiolabel was monitored. Mild-base hydrolysis of the isolated peptidoglycan (to release ester-linked acetate) from cells grown in the presence of 40 microM [acetyl-3H]N-acetyl-D-glucosamine resulted in the release of [3H]acetate, as detected by high-pressure liquid chromatography. The inclusion of either acetate, pyruvate, or acetyl phosphate, each at 1 mM final concentration, did not result in a diminution of mild-base-released [3H]acetate levels. No such release of [3H]acetate was observed with peptidoglycan isolated from either Escherichia coli incubated with the same radiolabel or P. mirabilis grown with [1,6-3H]N-acetyl-D-glucosamine or D-[1-14C]glucosamine. These observations support a hypothesis that O acetylation occurs by N----O acetyl transfer within the sacculus. A decrease in [3H]acetate release by mild-base hydrolysis was observed with the peptidoglycan of P. mirabilis cultures incubated in the presence of antagonists of peptidoglycan biosynthesis, penicillin G and D-cycloserine. The absence of free-amino sugars in the peptidoglycan of P. mirabilis but the detection of glucosamine in spent culture broths implies that N----O transacetylation is intimately associated with peptidoglycan turnover.
Full text
PDF






Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- ABRAMS A. O-acetyl groups in the cell wall of Streptococcus faecalis. J Biol Chem. 1958 Feb;230(2):949–959. [PubMed] [Google Scholar]
- BRUMFITT W. The mechanism of development of resistance to lysozyme by some gram-positive bacteria and its results. Br J Exp Pathol. 1959 Oct;40:441–451. [PMC free article] [PubMed] [Google Scholar]
- BRUMFITT W., WARDLAW A. C., PARK J. T. Development of lysozyme-resistance in Micrococcus lysodiekticus and its association with an increased O-acetyl content of the cell wall. Nature. 1958 Jun 28;181(4626):1783–1784. doi: 10.1038/1811783a0. [DOI] [PubMed] [Google Scholar]
- Blake C. C., Johnson L. N., Mair G. A., North A. C., Phillips D. C., Sarma V. R. Crystallographic studies of the activity of hen egg-white lysozyme. Proc R Soc Lond B Biol Sci. 1967 Apr 18;167(1009):378–388. doi: 10.1098/rspb.1967.0035. [DOI] [PubMed] [Google Scholar]
- Blundell J. K., Perkins H. R. Effects of beta-lactam antibiotics on peptidoglycan synthesis in growing Neisseria gonorrhoeae, including changes in the degree of O-acetylation. J Bacteriol. 1981 Aug;147(2):633–641. doi: 10.1128/jb.147.2.633-641.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Dobrogosz W. J. N-acetylglucosamine assimilation in Escherichia coli and its relation to catabolite repression. J Bacteriol. 1968 Feb;95(2):585–591. doi: 10.1128/jb.95.2.585-591.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Dougherty T. J. Involvement of a change in penicillin target and peptidoglycan structure in low-level resistance to beta-lactam antibiotics in Neisseria gonorrhoeae. Antimicrob Agents Chemother. 1985 Jul;28(1):90–95. doi: 10.1128/aac.28.1.90. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Dougherty T. J. Peptidoglycan biosynthesis in Neisseria gonorrhoeae strains sensitive and intrinsically resistant to beta-lactam antibiotics. J Bacteriol. 1983 Jan;153(1):429–435. doi: 10.1128/jb.153.1.429-435.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Doyle R. J., Chaloupka J., Vinter V. Turnover of cell walls in microorganisms. Microbiol Rev. 1988 Dec;52(4):554–567. doi: 10.1128/mr.52.4.554-567.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Dupont C., Clarke A. J. Dependence of lysozyme-catalysed solubilization of Proteus mirabilis peptidoglycan on the extent of O-acetylation. Eur J Biochem. 1991 Feb 14;195(3):763–769. doi: 10.1111/j.1432-1033.1991.tb15764.x. [DOI] [PubMed] [Google Scholar]
- Fleck J., Mock M., Minck R., Ghuysen J. M. The cell envelope in Proteus vulgaris P 18. Isolation and characterization of the peptidoglycan component. Biochim Biophys Acta. 1971 Jun 1;233(3):489–503. doi: 10.1016/0005-2736(71)90149-0. [DOI] [PubMed] [Google Scholar]
- Fleming T. J., Wallsmith D. E., Rosenthal R. S. Arthropathic properties of gonococcal peptidoglycan fragments: implications for the pathogenesis of disseminated gonococcal disease. Infect Immun. 1986 May;52(2):600–608. doi: 10.1128/iai.52.2.600-608.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
- GHUYSEN J. M., STROMINGER J. L. STRUCTURE OF THE CELL WALL OF STAPHYLOCOCCUS AUREUS, STRAIN COPENHAGEN. II. SEPARATION AND STRUCTURE OF DISACCHARIDES. Biochemistry. 1963 Sep-Oct;2:1119–1125. doi: 10.1021/bi00905a036. [DOI] [PubMed] [Google Scholar]
- Gmeiner J., Kroll H. P. Murein biosynthesis and O-acetylation of N-acetylmuramic acid during the cell-division cycle of Proteus mirabilis. Eur J Biochem. 1981 Jun;117(1):171–177. doi: 10.1111/j.1432-1033.1981.tb06317.x. [DOI] [PubMed] [Google Scholar]
- Gmeiner J., Sarnow E. Murein biosynthesis in synchronized cells of Proteus mirabilis. Quantitative analysis of O-acetylated murein subunits and of chain terminators incorporated into the sacculus during the cell cycle. Eur J Biochem. 1987 Mar 2;163(2):389–395. doi: 10.1111/j.1432-1033.1987.tb10811.x. [DOI] [PubMed] [Google Scholar]
- Goodell E. W., Higgins C. F. Uptake of cell wall peptides by Salmonella typhimurium and Escherichia coli. J Bacteriol. 1987 Aug;169(8):3861–3865. doi: 10.1128/jb.169.8.3861-3865.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Grabow W. O., Smit J. A. Methionine synthesis in Proteus mirabilis. J Gen Microbiol. 1967 Jan;46(1):47–57. doi: 10.1099/00221287-46-1-47. [DOI] [PubMed] [Google Scholar]
- Hoyle B. D., Beveridge T. J. Metal binding by the peptidoglycan sacculus of Escherichia coli K-12. Can J Microbiol. 1984 Feb;30(2):204–211. doi: 10.1139/m84-031. [DOI] [PubMed] [Google Scholar]
- Karkhanis Y. D., Zeltner J. Y., Jackson J. J., Carlo D. J. A new and improved microassay to determine 2-keto-3-deoxyoctonate in lipopolysaccharide of Gram-negative bacteria. Anal Biochem. 1978 Apr;85(2):595–601. doi: 10.1016/0003-2697(78)90260-9. [DOI] [PubMed] [Google Scholar]
- Lear A. L., Perkins H. R. Degrees of O-acetylation and cross-linking of the peptidoglycan of Neisseria gonorrhoeae during growth. J Gen Microbiol. 1983 Mar;129(3):885–888. doi: 10.1099/00221287-129-3-885. [DOI] [PubMed] [Google Scholar]
- Lear A. L., Perkins H. R. O-acetylation of peptidoglycan in Neisseria gonorrhoeae. Investigation of lipid-linked intermediates and glycan chains newly incorporated into the cell wall. J Gen Microbiol. 1986 Sep;132(9):2413–2420. doi: 10.1099/00221287-132-9-2413. [DOI] [PubMed] [Google Scholar]
- Lear A. L., Perkins H. R. Progress of O-acetylation and cross-linking of peptidoglycan in Neisseria gonorrhoeae grown in the presence of penicillin. J Gen Microbiol. 1987 Jul;133(7):1743–1750. doi: 10.1099/00221287-133-7-1743. [DOI] [PubMed] [Google Scholar]
- Martin H. H., Gmeiner J. Modification of peptidoglycan structure by penicillin action in cell walls of Proteus mirabilis. Eur J Biochem. 1979 Apr;95(3):487–495. doi: 10.1111/j.1432-1033.1979.tb12988.x. [DOI] [PubMed] [Google Scholar]
- Martin H. H. In vitro synthesis of peptidoglycan by spheroplasts of Proteus mirabilis grown in the presence of penicillin. Arch Microbiol. 1984 Nov;139(4):371–375. doi: 10.1007/BF00408382. [DOI] [PubMed] [Google Scholar]
- Martin H. H., Maskos C., Burger R. D-alanyl-D-alanine carboxypeptidase in the bacterial form and L-form of Proteus mirabilis. Eur J Biochem. 1975 Jul 1;55(2):465–473. doi: 10.1111/j.1432-1033.1975.tb02183.x. [DOI] [PubMed] [Google Scholar]
- Morihara K., Oka T. Effect of secondary interaction on the enzymatic activity of trypsin-like enzymes from Streptomyces. Arch Biochem Biophys. 1973 Jun;156(2):764–771. doi: 10.1016/0003-9861(73)90330-5. [DOI] [PubMed] [Google Scholar]
- Negro A., Garbisa S., Gotte L., Spina M. The use of reverse-phase high-performance liquid chromatography and precolumn derivatization with dansyl chloride for quantitation of specific amino acids in collagen and elastin. Anal Biochem. 1987 Jan;160(1):39–46. doi: 10.1016/0003-2697(87)90611-7. [DOI] [PubMed] [Google Scholar]
- Rosenthal R. S., Folkening W. J., Miller D. R., Swim S. C. Resistance of O-acetylated gonococcal peptidoglycan to human peptidoglycan-degrading enzymes. Infect Immun. 1983 Jun;40(3):903–911. doi: 10.1128/iai.40.3.903-911.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rosenthal R. S., Gfell M. A., Folkening W. J. Influence of protein synthesis inhibitors on regulation of extent of O-acetylation of gonococcal peptidoglycan. Infect Immun. 1985 Jul;49(1):7–13. doi: 10.1128/iai.49.1.7-13.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sidow T., Johannsen L., Labischinski H. Penicillin-induced changes in the cell wall composition of Staphylococcus aureus before the onset of bacteriolysis. Arch Microbiol. 1990;154(1):73–81. doi: 10.1007/BF00249181. [DOI] [PubMed] [Google Scholar]
- Smith T. J., Hanna P. E. N-acetyltransferase multiplicity and the bioactivation of N-arylhydroxamic acids by hamster hepatic and intestinal enzymes. Carcinogenesis. 1986 May;7(5):697–702. doi: 10.1093/carcin/7.5.697. [DOI] [PubMed] [Google Scholar]
- Snowden M. A., Perkins H. R., Wyke A. W., Hayes M. V., Ward J. B. Cross-linking and O-acetylation of newly synthesized peptidoglycan in Staphylococcus aureus H. J Gen Microbiol. 1989 Nov;135(11):3015–3022. doi: 10.1099/00221287-135-11-3015. [DOI] [PubMed] [Google Scholar]
- Swim S. C., Gfell M. A., Wilde C. E., 3rd, Rosenthal R. S. Strain distribution in extents of lysozyme resistance and O-acetylation of gonococcal peptidoglycan determined by high-performance liquid chromatography. Infect Immun. 1983 Nov;42(2):446–452. doi: 10.1128/iai.42.2.446-452.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]