Abstract
This article focusses on lytic enzyme systems available in E. coli and their potential use for cellular disruption. In the systems described here the genetic information for lysis would be carried within the microbial host, either integrated or naturally occurring on chromosomal DNA, or on extrachromosomal elements such as plasmids. Each microbe would carry complete information for endogenous enzymatic lysis, and lysis would occur in a controlled manner after being triggered by an external factor such as temperature or inducer addition. The lytic systems explored in this review include the autolytic enzymes, colicin lytic enzymes, and bacteriophage lytic enzymes from phage phiX174, T4, lambda, MS2 and Qβ. Many of the colicin lytic enzymes and all of the bacteriophage lytic enzymes described here have been cloned, and in some instances examined as cellular disruption methods. None of the E. coli autolytic enzymes have been cloned, but information pertinent for use as a disruption method is described.
Preview
Unable to display preview. Download preview PDF.
References
Hughes DE, Wimpenny JWT, Lloyd D (1971) The disintegration of microorganisms. In: Norris JR, Ribbons DW (eds) Methods in microbiology. Academic, New York, p 1
Scawen MD, Atkinson A, Darbyshire J (1980) Large-scale enzyme purification. In: Grant RA (ed), Applied protein chemistry, Applied Science Publishers, London, p 281
Darbyshire J (1981) Large scale enzyme extraction and recovery. In: Wiseman A (ed) Topics in enzyme and fermentation biotechnology, Ellis Horwood, New York, p 147
Engler CR (1985) Disruption of microbial cells. In: Moo-Young M (ed-in-chief) Cooney CL, Humphrey AE (eds) Comprehensive biotechnology, vol 2, Pergamon, New York, p 305
Auerbach JI, Rosenberg M (1987) US Patent # 4637980
Crabtree S, Cronan JE (1984) J. Bact. 158: 354
Henrich B, Plapp R (1984) J. Biochem. Biophys. Meth. 10: 25
Glover DM (1984) Gene cloning. Chapman and Hall, New York
Milewski EA (1984) The NIH guidelines for research involving recombinant DNA molecules. In: Bollon AP (ed) Recombinant DNA products: insulin, interferon and growth hormone, CRC Press, Boca Raton, p 156
Park JT (1987) The murein sacculus. In: F.C. Neidhardt (ed) Escherichia coli and Salmonella typhimurium. American Society for Microbiology, vol 1, Washington DC, p 7
Coakley WT, Bater AJ, Lloyd D (1977) Adv. Micro. Phys. 16: 279
Gmeiner J (1980) J. Bact. 143: 510
Braun V, Gnirke H, Henning U, Rehn K (1973) J. Bact. 114: 1264
Pelzer von H (1963) Z. Naturf. 18B: 950
Holtje JV, Mirelman D, Sharon N, Schwarz U (1975) J. Bact. 124: 1067
Tomasz A (1983) Mode of action of β-lactam antibiotics —a microbiologist's view. In: Demain AL, Solomon NA (eds) Antibiotics containing the β-lactam structure I, Springer, Berlin Heidelberg New York (vol 67/I)
Phaff HJ (1977) Enzymatic yeast cell wall degradation. In: Feeney RJ, Whitaker JR (eds) Food proteins: improvement through chemical and enzymatic modification, American Chemical Society, Washington DC, p 244 (no 160)
Belikov VM, Latov VK, Tsyriapkin VA, Sergeev VA (1976) Microbiologichesky Promyshlennost [Microbiological Industry] 3:1
Akin C, Murphy RM (1981) US patent 4285976
Arnold WN (1981) Autolysis. In: Arnold WN (ed) Yeast cell envelopes: biochemistry, biophysics, and ultrastructure, vol 2, CRC Press, Boca Raton, p 129
Weissman C, Schein C (1982) Eur. Pat. Appl. EP # 61250
Rogers HJ (1979) The function of bacterial autolysins. In: Berkeley RCW, Gooday GW, Ellwood DC, (eds) Microbial polysaccharides and polysaccharases, Academic, New York
Leduc M, Kasra R, Singer H, Heijenoort J van (1984) FEMS Micro. Lett. 23: 137
Tomasz A (1984) Building and breaking of bonds in the cell wall of bacteria —the role for autolysins. In: Nombela C (ed) Microbial cell wall synthesis and autolysis, Elsevier, New York
Leduc M, Heijenoort J van (1980) J. Bact. 142: 52
Blasi U, Halfmann G, Lubitz W (1984) Induction of autolysis of Escherichia coli. In: C. Nombela (ed) Microbial cell wall synthesis and autolysis, Elsevier, New York
Halfmann G, Lubitz W (1986) J. Bact. 166: 683
Leduc M, Kasra R, Heijenoort J van (1982) J. Bact. 152: 26
Tuomanen E, Cozens R, Tosch W, Zak O, Tomasz A (1986) J. Gen. Micro. 132: 1297
Lubitz W, Halfmann G, Plapp R (1984) J. Gen. Micro. 130: 1079
Tuomanen E, Tomasz A (1986) J. Bact. 167: 1077
Leduc M, Frehel C, Heijenoort J van (1985) J. Bact. 161: 627
Kitano K, Tomasz A (1979) Antimicrob. Agents Chemother. 16: 838
Markert A, Zillig W (1965) Vir. 25: 88
Nomura M (1964) PNAS 52: 1514
Konisky J (1978) The bacteriocins. In: Ornston LN, Sokatch JR (eds) The bacteria, vol VI, Academic, New York, p 71
Luria SE, Suit JL (1982) Transmembrane channels produced by colicin molecules. In: Martinosi A (ed) Membranes and transport, vol 2, Plenum, New York, p 279
Cramer WA, Dankert JR, Uratani Y (1983) Biochim. Biophys. Acta 737: 173
Luria SE, Suit JL (1987) Colicins and Col plasmids. In: Neidhardt FC (ed) Escherichia coli and Salmonella typhimurium, vol 2, American Society for Microbiology, Washington DC, p 1615
Sabik JF, Suit JL, Luria SE (1983) J. Bact. 153: 1479
Hakkaart MJJ, Veltkamp E, Nijkamp HJJ (1981) Mol. Gen. Genet. 183: 318
Hakkaart MJJ, Veltkamp E, Nijkamp HJJ (1981) Gen. Genet. 183: 326
Pugsley AP, Schwarz M (1984) EMBO J. 3: 2393
Watson RJ, Lau PCK, Vernet T, Visentin LP (1984) Gene 29: 175
Jakes KS, Zinder ND (1984) J. Bact. 157: 582
Lloubes R, Baty D, Lazdunski C (1986) Nucl. Acids Res. 14: 2621
van den Elzen PJM, Walters HHB, Veltkamp E, Nijkamp HJJ (1983) Nucl. Acids Res. 11: 2465
Cole ST, Saint-Joanis B, Pugsley AP (1985) Mol. Gen. Genet. 198: 465
Chan PT, Ohmori H, Tomizawa J, Lebowitz J (1985) J. Biol. Chem. 260: 8925
Pugsley AP, Schwarz M (1983) J. Bact. 156: 109
Altieri J, Suit JL, Fan M-LJ, Luria SE (1986) J. Bact. 168: 648
Howard SP, Leduc M, van Heijenoort J, Lazdunski C (1987) FEMS Micro. Lett. 42: 147
Kobayashi T, Kato C, Kudo T, Horikoshi K (1986) J. Bact. 166: 8
Kudo T, Kato C, Horikoshi K (1983) J. Bact. 156: 949
Kato C, Kobayashi T, Kudo T, Furusato T, Murakami Y, Tanaka T, Baba H, Oishi T, Ohtsuka E, Ikehara M, Yanagida T, Kato H, Moriyama S, Horikoshi K (1987) Gene 54: 197
Sher IH, Mallette MF (1952) J. Biol. Chem. 200: 257
Young R, Way J, Way S, Yin J, Syvanen M (1979) J. Mol. Biol. 132: 307
Reader RW, Siminovitch L (1971) Vir. 43: 623
Bienkowska-Szewczyk K, Lipinska B, Taylor A (1981) Mol. Gen. Genet. 184: 111
Altman E, Young K, Garrett J, Altman RA, Young R (1985) J. Vir. 53: 1008
Garrett J, Fusselman R, Hise J, Chiou L, Smith-Grillo D, Schulz J, Young R (1981) Mol. Gen. Genet. 182: 326
Garrett JM, Young R (1982) J. Vir. 44: 886
Friedman DI, Olsen ER, Georgopoulos C, Tilly K, Herskowitz I, Banuett F (1984) Micro. Rev. 48: 299
Tsugita A, Inouye M (1968) J. Biol. Chem. 243: 391
Josslin R (1970) Vir 40: 719
Mukai F, Streisinger G, Miller B (1967) Vir. 33: 398
Wetzel RB (1985) Eur. Pat. Appl. EP # 155189
Perry LJ, Heyneker HL, Wetzel R (1985) Gene 38: 259
Raj CVS, Wu HC (1973) J. Bact. 1973: 656
Bachmann B (1987) Linkage map of Escherichia coli K-12, edition 7. In: Neidhardt FC (ed) Escherichia coli and Salmonella typhimurium, vol 2, American Society for Microbiology, Washington DC, p 807
Hutchinson CA, Sinsheimer RL (1963) J. Mol. Biol. 7: 206
Hutchinson CA, Sinsheimer RL (1966) J. Mol. Biol. 18: 429
Young KD, Young R (1982) J. Vir. 44: 993
Henrich B, Lubitz W, Plapp R (1982) Mol Gen. Genet. 185: 493
Barrell BG, Air GM, Hutchinson CA (1976) Nature 264: 34
Lubitz W, Plapp R (1980) Curr. Micro. 4: 301
Dabora RL (1989) Studies on the action of the cloned phiX174 lysis gene E, Thesis. Massachusetts Institute of Technology, Cambridge, Massachusetts
Pollock TJ, Tessman ES, Tessman I (1978) J. Vir. 28: 408
Lubitz W, Schmid R, Plapp R (1981) Curr. Micro. 5: 45
Blasi U, Geisen R, Lubitz W, Henrich B, Plapp R (1983) Localization of the bacteriophage phiX174 lysis gene product in the cell envelope of Escherichia coli. In: Hakenbeck T (ed) The target of penicillin, Walter de Gruyter, New York
Maratea D, Young K, Young R (1985) Gene 40: 39
Buckley KJ, Hayashi M (1986) Mol. Gen. Genet. 204: 120
Blasi U, Lubitz W (1985) J. Gen. Vir. 66: 1209
Blasi U, Harkness RE, Witte A, Halfmann G, Lubitz W (1986) Endogenous induction of bacterial lysis by cloned phiX174 gene E product. In: Seidl PH, Schleifer KH (eds) Biological properties of peptidoglycan, Walter de Gruyter, New York
Lubitz W, Harkness RE, Ishiguro E (1984) J. Bact. 159: 385
Witte A, Lubitz W, Bakker EP (1987) J. Bact. 169: 1750
Wadle D, Henrich B, Plapp R (1986) Curr. Micro. 14: 65
Kastelein RA, Remaut E, Fiers W, Van Duin J (1982) Nature 295: 35
Coleman J, Inouye M, Atkins J (1983) J. Bact. 153: 1098
Holtje JV, van Duin J (1984) MS2-phage induced lysis of E. coli depends upon the activity of the bacterial autolysins. In: Nombela C (ed) Microbial cell wall synthesis and autolysis, Elsevier, New York
Holtje JV, Fiedler W, Rotering H, Walderich B, van Duin J (1988) J. Biol. Chem. 263: 3539
Kennedy EP (1982) PNAS 79: 1092
Goessens WHF, Driessen AJM, Wilschut J, van Duin J (1988) EMBO J. 7: 867
Winter RB, Gold L (1983) Cell 33: 877
Harkness RE, Lubitz W (1987) FEMS Micro. Lett. 48: 9
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 1990 Springer-Verlag
About this paper
Cite this paper
Dabora, R.L., Cooney, C.L. (1990). Intracellular lytic enzyme systems and their use for disruption of Escherichia coli . In: Applied Molecular Genetics. Advances in Biochemical Engineering/Biotechnology, vol 43. Springer, Berlin, Heidelberg. https://doi.org/10.1007/BFb0009077
Download citation
DOI: https://doi.org/10.1007/BFb0009077
Published:
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-540-52794-7
Online ISBN: 978-3-540-47151-6
eBook Packages: Springer Book Archive