Biogenesis and secretion of overproduced protein in recombinant strains of Escherichia coli

Process Biochemistry

Volumn 40, Issue 2, 2005, Pages 509-518

  Badyakina, A O ^a   Nesmeyanova, M A ^a  

^a SKRYABIN INSTITUTE OF BIOCHEMISTRY AND PHYSIOLOGY OF MICROORGANISMS   (Russian Federation)

Author keywords

Cell envelope; Escherichia coli; Isoforms; PhoA biogenesis; PrePhoA; Secretion

Indexed keywords

BACTERIOLOGY; CLONING; GENES; PROTEINS; STRAIN; SYNTHESIS (CHEMICAL);

BIOGENESIS; LARGE-SCALE PRODUCTION; RECOMBINANT STRAIN; SECRETION;

ESCHERICHIA COLI;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 7444221391     PISSN: 00329592     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2004.02.012     Document Type: Review

References (70)

1. Debabov V.G. Metabolic engineering of microbial cell. Microbiologia (Russia). 68:1999;823-833
2. Ogawa J., Shimizu S. Microbial enzymes: new industrial applications from traditional screening methods. Trends Biotechnol. 17(1):1999;13-21
3. Aristidou A., Penttila M. Metabolic engineering applications to renewable resource utilization. Curr Opin Biotechnol. 11(2):2000;187-198
4. Ho N., Roberto F. Microbial catalysis and metabolic engineering. Appl Biochem Biotechnol. 105(1-3):2003;245-246
5. Nielsen J. Metabolic engineering. Appl Microbiol Biotechnol. 55:2001;263-283
6. Nicaud J.M., Mackman W., Holland I. Current status of secretion of foreign proteins by microorganisms. J Biotechnol. 3:1986;255-270
7. Swartz J.R. Advances in Escherichia coli production of therapeutic proteins. Curr Opin Biotechnol. 12:2001;195-201
8. Weikert C., Sauer U., Bailey J.E. An Escherichia coli host strain useful for efficient overproduction of secreted recombinant protein. Biotechnol Bioeng. 59:1998;386-391
9. Park S.J., Georgiou G., Lee S.Y. Secretory production of recombinant protein by a high cell density culture of a protease negative mutant Escherichia coli strain 164. Biotechnol Prog. 15:1999;164-167
10. Choi J.H., Jeong K.J., Kim S.C., Lee S.Y. Efficient secretory production of alkaline phosphatase by high cell density culture of recombinant Escherichia coli using the Bacillus sp. endoxylanase signal sequence. Appl Microbiol Biotechnol. 53:2000;640-645
11. Shokri A., Sanden A.M., Larsson G. Cell and process design for targeting of recombinant protein into the culture medium of Escherichia coli. Appl Microbiol Biotechnol. 60:2003;654-664
12. Naglac T.J., Wang H.Y. Recovery of a foreign protein from the periplasm of Escherichia coli by chemical permeabilization. Enzyme Microbiol Technol. 12:1990;603-611
13. Lazzaroni L.C., Portalier R. Genetic and biochemical characterization of periplasmic-leaky mutants of E. coli K12. J Bacteriol. 145:1981;1351-1358
14. Lazzaroni J.C., Fognini-Lefebvre N., Portalier R. Cloning of the excC and excD genes involved in the release of periplasmic proteins by E. coli K12. Mol Gen Genet. 218:1989;460-464
15. Lun C.A., Takahara M., Inouye M. Secretion cloning vectors for guiding the localization of protein in vivo. Curr Top Microbiol Immunol. 125:1986;61-74
16. Abrahamsen L., Moks T., Nilsson B., Uhlen M. Secretion of heterologous products to the culture medium of Escherichia coli. Nucleic Acid Res. 14:1986;7487-7500
17. Yong J., Choi J.N., Park S.S., Park C.S., Park K.H., Choi Y.D. Secretion of heterologous cyclodextrin glycosyltransferase of Bacillus sp. E1 from Escherichia coli. Biotechnol Lett. 18:1996;1223-1228
18. Blight M.A., Chervaux C., Holland I.B. Protein secretion pathways in Escherichia coli. Curr Opin Biotechnol. 5:1994;468-474
19. Cornelis P. Expressing genes in different Escherichia coli compartments. Curr Opin Biotechnol. 11:2000;450-454
20. Lazzaroni J.C., Atlan D., Portalier R.C. Excretion of alkaline phosphatase by Escherichia coli K12 pho constitutive mutants transformed with plasmids carrying the alkaline phosphatase structural gene. J Bacteriol. 164:1985;1376-1380
21. Pages J.M., Anba J., Lazdunski C. Conditions leading to secretion of a normally periplasmic protein in E. coli. J Bacteriol. 169:1987;1386-1390
22. Bernadac A., Bolla J.M., Lazdunski C., Inouye M., Pages J.M. Precise localization of an overproduced periplasmic protein in Escherichia coli: use of double immunogold labelling. Biol Ce1l. 161:1987;141-147
23. Bogdanov M.V., Tarakhovsky Y.S., Manuvakhova M.S., Gongadze G.G., Nesmeyanova M.A. Compositional and structural peculiarities of the envelope of Escherichia coli secreting alkaline phosphatase into medium. Biol Membr (in Russian). 6:1989;301-308
24. Nesmeyanova M.A., Zakharova M.V., Fedotikova E.T., Lysina O.P. Secretion into the medium of periplasmic alkaline phosphatase in Escherichia coli cells transformed by plasmids with the phoA gene. Biotechnology (Russian). 6:1990;20-22
25. Nesmeyanova M.A., Karamyshev A.L., Tsfasman I.M., Fedotikova E.T. Transformation of various E. coli strains by multicopy plasmids with phoA gene results in secretion of periplasmic alkaline phosphatase into the medium and accumulation off its presursor. Mol Biol (Moscow). 25:1991;770-778
26. Tsfasman I.M., Suzina N.E., Badyakina A.O., Nesmeyanova M.A. Secretion of periplasmic PhoA protein during its supersynthesis into the medium using outer membrane vesicles. Features of chemical composition of the vesicles and membranes of Escherichia coli secreting cells. Mol Biol (Moscow). 25:1991;974-988
27. Nesmeyanova M.A., Tsfasman I.M., Karamyshev A.L., Suzina N.E. Secretion of the overproduced periplasmic PhoA protein into the medium and accumulation of its precursor in phoA-transformed Escherichia coli strains: involvement of outer membrane vesicles. World J Microbiol Biotechnol. 7:1991;394-406
28. Tsfasman I.M., Badyakina A.O., Nagornaya N.E., Nesmeyanova M.A. Features of the biogenesis of Escherichia coli alkaline phosphatase during its supersynthesis. Mol Biol (Moscow). 27:1993;805-816
29. Nesmeyanova MA, Karamyshev AL, Kalinin AE, Tsfasman IM, Badyakina AO, Khmelnitsky MJ, et al. E. coli alkaline phosphatase biogenesis: influnce of oversynthesis and amino acid substitions. In: Cellular and molecular biology of phosphate and phosphorylated compounds. In: Silver S, et al., editors. Microorganisms. Washington, DC: American Society for Microbiology; 1994. p. 264-9.
30. Badyakina A.O., Suzina N.E., Dmitriev V.V., Tarakhovsky Y.S., Tsfasman I.M., Nesmeyanova M.A. Changes in biogenesis and secretion into the medium of periplasmic alkaline phosphatase encoded by the phoA gene constituent of a plasmid in Escherichia coli DH1. Biochemistry (Moscow). 60:1995;505-516
31. Nesmeyanova M.A., Kalinin A.E., Karamyshev A.L., Mikhaleva N.I., Krupyanko V.I. Overproduction, secretion, isolation and properties of recombinant alkaline phosphatase encoded in Escherichia coli. Proc Biochem. 32:1996;1-7
32. Badyakina A.O., Koryakina Y.A., Suzina N.E., Nesmeyanova M.A. Unbalanced phospholipid composition of the Escherichia coli membranes increases the efficiency of the periplasmic alkaline phosphatase secretion into the medium. Biochemistry (Moscow). 68:2003;917-925
33. Torriani-Gorini A. The birth and growth of the Pho regulon. In: Torriani A, Rothman F, Silver S, Wright A, Yagil E, editors. Phosphate metabolism and cellular regulation in microorganisms. Washington, DC: American Society for Microbiology; 1987. p. 3-11.
34. Hoffman C.S., Wright A. Fusions of secreted proteins to alkaline phosphatase: an approach for studying protein secretion. Proc. Natl Acad. Sci USA. 82:1985;5107-5111
35. Chang C.N., Inouye H., Model P., Beckwith J. Processing of alkaline phosphatase precursor to the mature enzyme by on Escherichia coli inner membrane preparation. J Bacteriol. 142:1980;726-728
36. Nakata A, Shinagawa H, Rothman FG. Molecular mechanism of isozyme formation of alkaline phosphatase. In: Torriani-Gorini A, Rothman FG, Silver S, Wright A, Yagil E, editors. Escherichia coli, phosphate metabolism and cellular regulation in microorganisms. Washington, DC: American Society for Microbiology; 1987. p. 139-41.
37. Sambrook J, Fritsch EF, Maniatis T. Molecular cloning. A laboratory manual. New York: Cold Spring Harbor Laboratory, vols. 1-3; 1989. p. 1626.
38. Wood W.B. Host specificity of DNA produced by Escherichia coli: bacterial mutations affecting the restriction and modification of DNA. J Mol Biol. 16:1966;118-133
39. Low B. Formation of merodiploids in matings with a class of Rec recipient strains of Escherichia coli K12. Proc Natl Acad Sci USA. 60:1968;160
40. Bolivar F., Rodriguez R.L., Greene P.J., Betlach M.C., Heynecker H.L., Boyer H.W., et al. Constraction and characterization of new cloning vehicles. II. A multipurpose cloning system. Gene. 2:1977;95-113
41. Karamyshev A.L., Shlyapnikov M.G., Khmelnitsky M.I., Nesmeyanova M.A., Ksenzenko V.N. Biogenesis and secretion of alkaline phosphatase and its mutated forms in Escherichia coli. I. Site-directed mutations in alkaline phosphatase gene. Mol Biol (Moscow). 28:1994;99-104
42. Mikhaleva N.I., Golovastov V.V., Zolov S.N., Bogdanov M.V., Dowhan W., Nesmeyanova M.A. Depletion of phosphatidilethanolamine affects secretion of Escherichia coli alkaline phosphatase and its transcriptional expression. FEBS Lett. 493:2001;85-90
43. Lazdunski C., Baty D., Pages I. Procaine, a local anesthetic. Interacting with the cell membrane inhibits the processing of precursor forms of periplasmic proteins in Escherichia coli. Eur J Biochem. 96:1979;49-57
44. Pages J.M., Anba J., Bernadac A., Shinagawa H., Nakata A., Lazdunski C. Normal presursors of periplasmic proteins accumulated in the cytoplasm are not exported post-translationally in Escherichia coli. Eur J Biochem. 143:1984;499-505
45. Ito K., Bassford P.I., Beckwith J. Protein localization in E. coli. Is there a common step in the secretion of periplasmic and outer membrane proteins? Cell. 24:1981;707-718
46. Walter P., Lingappa V.R.A. Mechanism of protein translocation across the endoplasmic membrane. Ann Rev Cell Biol. 2:1986;499-516
47. Hardy S.J.S., Randall L.S. A kinetic partitioning model of selective binding of nonnative proteins by the bacterial chaperone SecB. Science. 251:1991;439-443
48. Mikhaleva N.I., Kalinin A.E., Molotkovsky Y.G., Nesmeyanova M.A. Interaction of the E. coli alkaline phosphatase precursor with model phospholipid membranes. Biochemistry (Moscow). 62:1997;184-190
49. Schlessinger MY, Block W, Kelley PM. Isozymes. In: Markert B, editor. Molecular structure. New York, NY: Academic Press; 1975. p. 333-42.
50. Nesmeyanova M.A., Motlokh O.B., Kolot M.N., Kulaev I.S. Multiples forms of alkaline phosphatase from Escherichia coli cells with repressed and derepressed biosynthesis of the enzyme. J Bacteriol. 146:1981;453-459
51. Mikhaleva N.I., Zolov S.N., Suzina N.E., Melkozernov A.N., Nesmeyanova M.A. Permeability of the Escherichia coli outer membrane to ethidium ions and periplasmic alkaline phosphatase during enhanced synthesis of the alkaline phosphatase. Biochemistry (Moscow). 60:1995;881-887
52. Leive L. The barrier function of the Gram-negative envelope. Ann N Y Acad Sci. 235:1974;109-129
53. Lambert B., Le Pecq J.B. Effect of mutation, electric membrane potential and metabolic inhibitors on the accesibility of nucleic acids to ethidium bromide in Escherichia coli cells. Biochemistry. 83:1984;166-176
54. Irkhin A.I., Kondrashenko T.N., Puchkov E.O. Sensitivity of Escherichia coli cell membranes to various classes of detergents. Mikrobiologiya. 58:1989;217-221
55. Elbach P, Weiss J, Forst S. In: Op den Kamp JAF, et al., editors. Lipids and membranes: past, present and future. Amsterdam: Elsevier; 1986. p. 259-86.
56. Mizuno M., Kameyama Y., Yashiro K., Yokota Y. Properties of membranes phospholipids and their fatty acyl compositions of secretory granules from rat parotid gland. Cell Biol Int Rep. 11:1987;629-636
57. Pugsley A.P., Scwarts M. Colicin E release: lysis, leakage or secretion? Possible role of a phospolipase. EMBO J. 3:1984;2993-2997
58. Dekker N., Verheij H.M., Tommassen J. Bacteriocin release protein triggers dimerization of outer membrane phospholipase A in vivo. J Bacteriol. 181:1999;3281-3283
59. Lindsay S.S., Wheeler B., Sanderson K.E., Costertone J.W., Cheng K.J. The release of alkaline phosphatase and of lipopolysaccharide during the growth of rough strains of Salmonella typhimurium. Can J Microbiol. 19:1980;335-343
60. Ali JA, Johnson A, Franco DJ, Metzger TD, Connell JG, Morris Jr Sozhamannan S. Mutations in the extracellular protein secretion pathway genes (eps) interfere with rugose polysaccharide production in and motility of Vibrio cholerae. Infect Immun 2000;68:1967-74.
61. Iredell J.R., Manning P.A. Outer membrane translocation arrest of the tcpa pilin subunit in rfb mutants of Vibrio cholerae O1 strain 569B. J Bacteriol. 179:1997;2038-2046
62. Yem D., Wu H. Physiological characterization of an E. coli mutant altered in the structure of murein-lipoprotein. J Bacteriol. 133:1978;1418-1426
63. Bernadac A., Gavioli M., Lazzaroni J.C., Raina S., Lloubes R. Escherichia coli tol-pal mutants form outer membrane vesicles. J Bacteriol. 180:1998;4872-4878
64. Dowhan W. Molecular basis for membrane phospholipid diversity: why are there so many lipids? Annu Rev Biochem. 66:1997;199-232
65. Beveridge T.J. Structures of Gram-negative cell walls and their derived membrane vesicles. J Bacteriol. 181:1999;4725-4733
66. Nesmeyanova M.A., Bogdanov M.V. Participation of acid phospholipids in protein translocation across the bacterial cytoplasmic membrane. FEBS Lett. 257:1989;203-207
67. VanVoorst F., de Kruijff B. Role of lipids in the translocation of protein across membranes. Biochem J. 347:2000;601-612
68. Kusters R., Dowhan W., de Kruijff B. Negatively charged phospholipids restore prePhoE translocation across phosphatidylglycerol-depleted Escherichia coli inner membrane vesicles. J. Biol. Chem. 266:1991;8659-8662
69. De Chavigni A., Heacock P.N., Dowhan W. Sequence and inactivation of the pss gene of Escherichia coli phosphatidylethanolamine may not be essential for cell viability. J. Biol. Chem. 266:1991;5323-5332
70. Nicaido H., Varra M. Molecular basis of bacterial outer membrane permeability. Microbiol Rev. 49:1985;1-32