Abstract
A broad variety of both Gram-positive and Gram-negative bacteria have been shown to have the ability to dissolve themselves (autolyze), particularly under “adverse” conditions (see Ghuysen and Shockman, 1973; Daneo-Moore and Shockman, 1977; Rogers et al., 1980; Shockman and Barrett, 1983; Doyle and Koch, 1987; Höltje and Tuomanen, 1991, for reviews). This process is now known to be initiated by the action of endogenous enzymes that hydrolyze specific bonds in the insoluble, osmotically protective, shape-maintaining and essential, peptidoglycan (murein) polymer of the bacterial cell wall. Hydrolysis of a sufficient number of bonds in a restricted area of the two- or three-dimensional peptidoglycan network, or a larger number of bonds in a broader area of the wall, creates a weak spot (or a generalized weakness in the structure), so that the wall can no longer protect the protoplast from its own internal osmotic pressure, so that the protoplast then explodes out through the weakened structure. Endogenous enzymes are now known that can hydrolyze virtually every bond in the peptidoglycan including: (i) glycosidases and transglycosidases, such as N-acetylmuramoylhydrolases (muramidases) and N-acetylglucosaminidases, (ii) N-acetylmuramoyl-L-alanine amidases, and (iii) various peptidases and transpeptidases, including DD- and LD-carboxypeptidases (Rogers et al., 1980).
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References
Barrett, J.F. and Shockman, G.D. (1984) Isolation and characterization of soluble peptidoglycan from, several strains of Streptococcus faecium. J. Bacteriol. 159, 511–519.
Barrett, J.F, Dolinger, D.L., Schramm, V.L., and Shockman, G.D. (1984a) The mechanism of soluble peptidoglycan hydrolysis by an autolytic muramidase. A processive exodisaccharidase. J. Biol. Chem. 259, 11818–11827.
Barrett, J.F, Schramm, V.L. and Shockman, G.D. (1984) Hydrolysis of soluble, linear, un-cross-linked peptidoglycans by endogenous bacterial N-acetylmuramoylhydrolases. J. Bacteriol. 159, 520–526.
Beck, B. and Park, J.T. (1976) Activity of three murein hydrolases during the cell division cycle of Escherichia coli as measured in toluene-treated cells. J. Bacteriol. 126, 1250–1260.
Beliveau, C, Potvin, C, Trudel, J, Asselin, A. and Bellemare, G. (1991) Cloning, sequencing, and expression in Escherichia coli of a Streptococcus faecalis autolysin. J. Bacteriol. 173, 5619–5623.
Biavasco, F, Pruzzo, C. and Thomas, C. (1988) Cloning and expression of the Staphylococcus aureus glucosaminidase in Escherichia coli. FEMS Microbiol. Lett. 49, 137–142.
Chatterjee, A.N., Wong, W, Young, F.E. and Gilpin, R.W. (1976) Isolation and characterization of a mutant of Staphylococcus aureus deficient in autolytic activity. J. Bacteriol. 125, 961–967.
Chu, C.-P, Kariyama, R, Daneo-Moore, L. and Shockman, G.D. (1992) Cloning and sequence analysis of the muramidase-2 gene from Enterococcus hirae. J. Bacteriol. 174, 1619–1625.
Cleveland, R. F, Höltje, J.-V, Wicken, A. J, Tomasz, A, Daneo-Moore, L. and Shockman, G.D. (1975) Inhibition of bacterial wall lysins by lipoteichoic acids and related compounds. Biochem. Biophys. Res. Commun. 67, 1128–1135.
Cleveland, R. F, Wicken, A. J, Daneo-Moore, L. and Shockman, G.D. (1976) Inhibition of wall autolysis in Streptococcus faecalis by lipoteichoic acid and lipids. J. Bacteriol. 126, 192–197.
Conover, M.J, Thompson, J.S. and Shockman, G.D. (1966) Autolytic enzyme of Streptococcus faecalis: release of soluble enzyme from cell walls. Biochem. Biophys. Res. Commun. 23, 713–719.
Cornett, J.B, Redman, B.E. and Shockman, G.D. (1978) Autolytic defective mutant of Streptococcus faecalis. J. Bacteriol. 133, 631–640.
Coyette, J, Perkins, H.R, Polacheck, I, Shockman, G.D. and Ghuysen, J.-M. (1974) Membrane-bound DD-carboxypeptidase and LD-transpeptidase of Streptococcus faecalis ATCC 9790. Eur. J. Biochem. 44, 459–468.
Coyette, J., Ghuysen, J.-M., Binot, F., Adriaens, P., Meesschaert, B. and Vanderhaeghe, H. (1977) Interactions between β-lactam antibiotics and isolated membranes of Streptococcus faecalis ATCC 9790. Eur. J. Biochem. 75, 231–239.
Croux, C. and García, J.-L. (1991) Sequence of the lye gene encoding the autolytic lysozyme of Clostridium acetobutylicum ATCC 824: comparison with other lytic enzymes. Gene 104, 25–31.
Daneo-Moore, L. and Shockman, G.D. (1977) The Bacterial Cell Surface in Growth and Division, In “Cell Surface Reviews, vol. 4. The Synthesis, Assembly, and Turnover of Cell Surface Components” (Poste, G. and Nicolson, G.L., Eds.), pp. 597–715. Elsevier/North Holland, Amsterdam.
Dolinger, D.L., Schramm, V.L. and Shockman, G.D. (1988) Covalent modification of the β-l,4-N-acetylmuramoylhydrolase of Streptococcus faecium with 5-mercaptouridine monophosphate. Proc. Natl. Acad. Sci. USA 85, 6667–6671.
Dolinger, D.L., Daneo-Moore, L. and Shockman, G.D. (1989) The second peptidoglycan hydrolase of Streptococcus faecium ATCC 9790 covalently binds penicillin. J. Bacteriol. 171, 4355–4361.
Doyle, R.J. and Koch, A.L. (1987) The functions of autolysins in the growth and division of Bacillus subtilis. Crit. Rev. Microbiol. 15, 169–222.
El Kharroubi, A., Jacques, P., Piras, G., Van Beeumen, J., Coyette, J. and Ghuysen, J.-M. (1991) The Enterococcus hirae R40 penicillin-binding protein 5 and the methicillin-resistant Staphylococcus aureus penicillin-binding protein 2′ are similar. Biochem. J. 280, 463–469.
Fan, D.P. and Beckman, M.M. (1973) Mutant of Bacillus subtilis with a temperaturesensitive autolytic amidase. J. Bacteriol. 14, 798–803.
Fein, J.E. and Rogers, H. J. (1976) Autolytic enzyme-deficient mutants of Bacillus subtilis 168. J. Bacteriol. 127, 1427–1442.
Foster, S.J. (1991) Cloning, expression, sequence analysis and biochemical characterization of an autolytic amidase of Bacillus subtilis 168 trpC2. J. Gen. Microbiol. 137, 1987–1998.
García, E., García, J.L., Ronda, C, García, P. and Lopez, R. (1985) Cloning and expression of the pneumococcal autolysin gene of Escherichia coli. Mol. Gen. Genet. 201, 225–230.
García, J.L., Sanchez-Puelles, J.M., García, P., Lopez, R., Ronda, C. and García, E. (1986) Molecular characterization of an autolysin-defective mutant of Streptococcus pneumoniae. Biochem. Biophys. Res. Comm. 137, 614–619.
García, E., García, J.L., García, P., Arraras, A., Sanchez-Puelles, J.M. and Lopez, R. (1988) Molecular evolution of lytic enzymes of Streptococcus pneumoniae and its bacteriophages. Proc. Natl. Acad. Sci. USA 85, 914–918.
García, P., García, J.L, García, E., Sanchez-Puelles, J.M. and Lopez, R. (1990) Modular organization of the lytic enzymes of Streptococcus pneumoniae and its bacteriophages. Gene 86, 81–88.
Garvey, K.J., Saedi, M.S. and Ito, J. (1986). Nucleotide sequence of Bacillus phage φ29 genes 14 and 15: homology of gene 15 with other phage lysozymes. Nucleic Acid Res. 14, 10001–10008.
Ghuysen, J.-M. (1991) Serine β-lactamases and penicillin-binding proteins. Ann. Rev. Microbiol. 45, 37–67.
Ghuysen, J.-M. and Shockman, G.D. (1973) Biosynthesis of Peptidoglycan, in “Bacterial Membranes and Walls” (Leive, L., Ed.), pp. 37–130. Marcel Dekker, New York.
Hakenbeck, R. and Messer, W. (1974) Activity of murein hydrolases and membrane synthesis in synchronized Escherichia coli B/r. Ann. Microbiol. Inst. Pasteur 125B, 163–166s.
Hartmann, R., Bock-Hennig, S.B. and Schwarz, U. (1974) Murein hydrolases in the envelope of Escherichia coli. Eur. J. Biochem. 41, 203–208.
Herbold, D.R. and Glaser, L. (1975 a) Bacillus subtilis N-acetylmuramic acid L-alanine amidase. J. Biol. Chem. 250, 1676–1682.
Herbold, D.R. and Glaser, L. (1915b) Interaction of Af-acetylmuramic acid L-alanine amidase with cell wall polymers. J. Biol. Chem. 250, 7231–7238.
Higgins, M. L., Pooley, H. M. and Shockman, G.D. (1970) Site of initiation of cellular autolysis in Streptococcus faecalis as seen by electron microscopy. J. Bacteriol. 103, 504–512.
Hinks, R. P., Daneo-Moore, L. and Shockman, G.D. (1978) Cellular autolytic activity in synchronized populations of Streptococcus faecium. J. Bacteriol. 133, 822–829.
Höltje, J.-V. and Tomasz, A. (1975) Lipoteichoic acid: A specific inhibitor of autolysin activity in Pneumococcus. Proc. Natl. Acad. Sci. USA 72, 1690–1694.
Höltje, J.-V. and Tuomanen, E.I. (1991) The murein hydrolases of Escherichia coli: properties, functions, and impact on the course of infections in vivo. J. Gen. Microbiol. 137, 441–454.
Jayaswal, R.K., Lee, Y.-I. and Wilkinson, B.J. (1990) Cloning and expression of a Staphylococcus aureus gene encoding a peptidoglycan hydrolase activity. J. Bacteriol. 172, 5783–5788.
Jolliffe, L.K., Doyle, R.J. and Streips, U.N. (1981) Energized membrane and cellular autolysis in Bacillus subtilis. Cell 25, 753–763.
Jones, C.J., Homma, M. and Macnab, R.M. (1989) L-, P-, and M-ring proteins of the flagellar basal body of Salmonella typhimurium: Gene sequences and deduced protein sequences. J. Bacteriol. 171, 3890–3900.
Joris, B., Englebert, S., Chu, C.-P., Kariyama, R., Daneo-Moore, L., Shockman, G.D. and Ghuysen, J.-M. (1992) Modular design of the Enterococcus hirae muramidase2 and Streptococcus faecalis autolysin. FEMS Microbiol. Lett., in press.
Joseph, R. and Shockman, G.D. (1976) Autolytic formation of protoplasts (autoplasts) of Streptococcus faecalis: location of active and latent autolysin. J. Bacteriol. 127, 1482–1493.
Kariyama, R. and Shockman, G.D. (1992) Extracellular and cellular distribution of muramidase-2 and muramidase-1 of Enterococcus hirae ATCC 9790. J. Bacteriol., in press.
Kawamura, T. and Shockman, G.D. (1983a) Evidence for the presence of a second peptidoglycan hydrolase in Streptococcus faecium. FEMS Microbiol. Lett. 19, 65–69.
Kawamura, T. and Shockman, G.D. (1983b) Purification and some properties of the endogenous, autolytic N-acetylmuramoylhydrolase of Streptococcus faecium, a bacterial glycoenzyme. J. Biol. Chem. 258, 9514–9521.
Köhler, S., Leimeister-Wächter, L., Chakraborty, T., Lottspeich, F. and Goebel, W. (1990) The gene coding for protein p60 of Listeria monocytogenes and its use as a specific probe for Listeria monocytogenes. Inf. Immun. 58, 1943–1950.
Koyama, T., Yamada, M. and Matsuhashi, M. (1977) Formation of regular packets of Staphylococcus aureus cells. J. Bacteriol. 129, 1518–1523.
Kuroda, A. and Sekiguchi, J. (1990) Cloning, sequencing, and genetic mapping of a Bacillus subtilis cell wall hydrolase gene. J. Gen. Microbiol. 136, 2209–2216.
Kuroda, A. and Sekiguchi, J. (1991) Molecular cloning and sequencing of a major Bacillus subtilis autolysin gene. J. Bacteriol. 173, 7304–7312.
Nakagawa, J. and Matsuhashi, M. (1982) Molecular divergence of a major peptidoglycan synthetase with transglycosylase-transpeptidase activities in Escherichia coli—penicillin-binding protein IBs. Biochem. Biophys. Res. Commun. 105, 1–11.
Nakagawa, J., Tamake, S., Tomioka, S. and Matsuhashi, M. (1984) Functional biosynthesis of cell wall peptidoglycan by polymorphic bifunctional polypeptides. J. Biol. Chem. 259, 13937–13946.
Paces, V., Uleek, C. and Urbanek, D. (1986) Nucleotide sequence of the late region of Bacillus subtilis phage PZA, a close relative of phi 29. Gene 44, 107–114.
Pooley, H.M. and Shockman, G.D. (1969) Relationship between the latent form and the active form of the autolytic enzyme of Streptococcus faecalis. J. Bacteriol. 100, 617–624.
Pooley, H.M. and Shockman, G.D. (1970) Relationship between the location of autolysin, cell wall synthesis, and the development of resistance to cellular autolysis in Streptococcus faecalis after inhibition of protein synthesis. J. Bacteriol. 103, 457–466.
Pooley, H.M., Shockman, G.D., Higgins, M.L. and Porres-Juan, J. (1972) Some properties of two autolytic-defective mutants of Streptococcus faecalis ATCC 9790. J. Bacteriol. 109, 423–431.
Potvin, C, Leclerc, D., Tremblay, G., Asselin, A. and Bellemare, G. (1988) Cloning, sequencing and expression of a Bacillus bacteriolytic enzyme in Escherichia coli. Mol. Gen Genet 214, 241–248.
Rogers, H.J., Perkins, H.R. and Ward, J.B. (1980) “Microbial Cell Walls and Membranes,” pp. 437–460. Chapman and Hall, New York.
Saedi, M.S., Garvey, K.J. and Ito, J. (1987) Cloning and purification of a unique lysozyme produced by Bacillus phage 029. Proc. Natl. Acad. Sci. USA 84, 955–958.
Sekiguchi, J., Ezaki, B., Kodama, K. and Akamatsu, T. (1988) Molecular cloning of a gene affecting the autolysin level and flagellation in Bacillus subtilis. J. Gen. Microbiol. 134, 1611–1621.
Shockman, G.D. (1965) Symposium on the fine structure and replication of bacteria and their parts. IV. Unbalanced cell-wall synthesis: autolysis and cell-wall thickening. Bacteriol. Rev. 29, 345–358.
Shockman, G.D. and Barrett, J.F. (1983) Structure, function, and Assembly of cell walls of Gram-positive bacteria. Ann. Rev. Microbiol. 37, 501–527.
Shockman, G.D. and Cheney, M.C. (1969) Autolytic enzyme system of Streptococcus faecalis. V. Nature of the autolysin-cell wall complex and its relationship to properties of the autolytic enzyme of Streptococcus faecalis. J. Bacteriol. 98,1199–1207.
Shockman, G.D., Thompson, J.S. and Conover, M.J. (1967) The autolytic enzyme system of Streptococcus faecalis. II. Partial characterization of the autolysin and its substrate. Biochemistry 6, 1054–1065.
Shockman, G.D., Daneo-Moore, L. and Higgins, M.L. (1974) Problems of cell wall and membrane growth, enlargement and division. Ann. N.Y. Acad. Sci. 235, 161–197.
Shockman, G.D., Daneo-Moore, L., Cornett, J.B. and Mychajlonka, M. (1979) Does penicillin kill bacteria? Rev. Infect. Dis. 1, 787–796.
Shockman, G.D, Daneo-Moore, L., McDowell, T.D. and Wong, W. (1982) The Relationship Between Inhibition of Cell Wall Synthesis and Bacterial Lethality, in “The Chemistry and Biology of β-Lactam Antibiotics” (Gorman, M. and Morin, R.B, Eds.), vol. 3, pp. 303–338. Academic Press, New York.
Shockman, G.D, Kawamura, T, Barrett, J.F. and Dolinger, D. (1983) The Autolytic System of Streptococcus faecium, in “The Target of Penicillin — International FEMS Symposium on the Murein Sacculus of Bacterial Cell Walls — Architecture and Growth” (Hakenbeck, R, Höltje, J.-V. and Labischinski, H, Eds.), pp. 165–172. W. de Gruyter & Co, Berlin, New York.
Shockman, G.D., Dolinger, D.L. and Daneo-Moore, L. (1988) The Autolytic Peptidoglycan Hydrolases of Streptococcus faecium: Two Unusual Enzymes, in “Antibiotic Inhibition of Bacteriai Cell Wall Assembly and Function” (Actor, P., Daneo-Moore, L., Higgins, M.L., Salton, M.R.J. and Shockman, G.D., Eds.), pp. 195–210. American Society for Microbiology, Washington, DC.
Shungu, D.L., Cornett, J.B. and Shockman, G.D. (1979) Morphological and physiological study of autolytic-defective Streptococcus faecium strains. J. Bacteriol. 138, 598–608.
Tomasz, A. (1979a) From penicillin-binding proteins to the lysis and death of bacteria: A 1979 view. Rev. Inf. Dis., 1, 434–467.
Tomasz, A. (1979) The mechanism of the irreversible antimicrobial effects of penicillins: How the beta-lactam antibiotics kill and lyse bacteria. Ann. Rev. Microbiol. 33, 113–37.
Uhlen, M., Guss, B., Wilsson, B, Gatenbeck, S, Phillipson, L. and Linberg, M. (1984) Complete sequence of the staphylococcal gene encoding protein A. J. Biol. Chem. 259, 1695–1702.
Walderich, B. and Höltje, J.-V. (1991) Subcellular distribution of the soluble lytic transglycosylase in Escherichia coli. J. Bacteriol. 173, 5668–5676.
Wang, X., Wilkinson, B.J. and Jayaswal, R.K. (1991) Sequence analysis of a Staphylococcus aureus gene encoding ä peptidoglycan hydrolase activity. Gene 102, 105–109.
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Shockman, G.D., Chu, CP., Kariyama, R., Tepper, L.K., Daneo-Moore, L. (1993). Peptidoglycan (Murein) Hydrolases: Unusual Enzymes for Unusual Substrates. 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_25
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