Growth-rate recovery of escherichia coli cultures carrying a multicopy plasmid, by engineering of the pentose-phosphate pathway

Biotechnology and Bioengineering

Volumn 87, Issue 4, 2004, Pages 485-494

  Flores, Salvador ^a   De Anda Herrera, Ramón ^a   Gosset, Guillermo ^a   Bolívar, Francisco G ^a  

^a INSTITUTO DE BIOTECNOLOGÍA   (Mexico)

Author keywords

Growth rate recovery; Pentose pathway engineering; Zwf gene expression

Indexed keywords

BIOLOGICAL TRANSFORMATION; GROWTH RATES; MULTICOPY GENES; PEPTIDES; PLASMIDS;

BIOMEDICAL ENGINEERING; BIOTECHNOLOGY; CELL CULTURE; DNA; ENERGY ABSORPTION; GENES; GROWTH KINETICS; METABOLISM; PROTEINS; SYNTHESIS (CHEMICAL);

ESCHERICHIA COLI;

ADENOSINE TRIPHOSPHATE; MESSENGER RNA; PLASMID DNA; PROINSULIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

ARTICLE; BACTERIAL GROWTH; BACTERIUM CULTURE; BIOSYNTHESIS; ENZYME ACTIVITY; ENZYME ASSAY; ESCHERICHIA COLI; GENE; GENE OVEREXPRESSION; GENETIC ENGINEERING; GENOTYPE; GLYCOLYSIS; GROWTH RATE; NONHUMAN; PENTOSE PHOSPHATE CYCLE; PLASMID; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN DETERMINATION; STRAIN DIFFERENCE; ZWF GENE;

CELL PROLIFERATION; ENZYME ACTIVATION; ESCHERICHIA COLI; GENE DOSAGE; GENE EXPRESSION REGULATION, BACTERIAL; GLUCOSEPHOSPHATE DEHYDROGENASE; PENTOSE PHOSPHATE PATHWAY; PLASMIDS; PROTEIN ENGINEERING; SIGNAL TRANSDUCTION;

ESCHERICHIA COLI; INSERTION SEQUENCES; JONES;

EID: 4344663365     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/bit.20137     Document Type: Article

References (48)

1. Ahmad S, Glavas NA, Bragg PD. 1992. A mutation at Gly314 of the β subunit of the Escherichia coli pyridine nucleotide transhydrogenase abolishes activity and affects the NADP(H)-induced conformational change. Eur J Biochem 207:733-739.
2. Amann E, Ochts B, Karl-Josef A. 1988. Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli. Gene 69:301-315.
3. Bolívar F, Rodríguez RL, Greene PJ, Betlach MC, Heynecker HL, Boyer HW, Crosa JH, Falkow S. 1977. Construction and characterization of new cloning vehicles. II. A multipurpose cloning system. Gene 2:95-113.
4. Boonstra B, French CE, Wainwright I, Bruce NC. 1999. The udhA gene of Escherichia coli encodes a soluble pyridine nucleotide transhydrogenase. J Bacteriol 181:1030-1034.
5. Boonstra B, Rathbone DA, French CE, Walker EH, Bruce NC. 2000. Cofactor regeneration by a soluble pyridine nucleotide transhydrogenase for biological production of hydromorphone. Appl Environ Microbiol 66:5161-5166.
6. Canonaco F, Hess TA, Heri S, Wang T, Szyperski T, Sauer U. 2001. Metabolic flux response to phosphoglucose isomerase knock-out in Escherichia coli and impact of overexpression of the soluble transhydrogenase UdhA. FEMS Microbiol Lett 204:247-252.
7. Csonka LN, Fraenkel DG. 1972. Pathways of NADPH formation in Escherichia coli. J Biol Chem 252:3382-3391.
8. Chang ACY, Cohen SN. 1978. Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid. J Bacteriol 134:1141-1156.
9. Chotani G, Dodge T, Hsu A, Kumar M, LaDuca R, Trimbur D, Weyler W, Sanford K. 2000. The commercial production of chemicals using pathway engineering. Biochim Biophys Acta 1543:434-455.
10. Chou C-H, Bennett GN, San KY. 1994. Effect of modified glucose uptake using genetic engineering techniques on high-level recombinant protein production in Escherichia coli dense cultures. Biotechnol Bioeng 44:952-960.
11. Covarrubias L, Cervantes L, Covarrubias A, Soberon X, Vichido I, Blanco A, Kupersztoch-Pornoy YM, Bolívar F. 1981. Construction and characterization of new cloning vehicles. V. Mobilization and coding properties of pBR322 and several deletion derivatives including pBR327 and pBR328. Gene 13:25-35.
12. Da Silva NA, Bailey JE. 1986. Theoretical growth yield estimates for recombinant cells. Biotechnol Bioeng 28:741-746.
13. Emmerling M, Dauner M, Ponti A, Fiaux J, Hochuli M, Szyperski T, Wuthrich K, Bailey JE, Sauer U. 2002. Metabolic flux responses to pyruvate kinase knockout in Escherichia coli. J Bacteriol 184:152-164.
14. Edwards JS, Palsson BO. 2000. Metabolic flux balance analysis and the in silico analysis of Escherichia coli K-12 gene deletions. BMC Bioinformatics 1:1 (http://biomedcentral.com/1471-2105/1/1).
15. Farmer WR, Liao JC. 1997. Reduction of aerobic acetate production by Escherichia coli. Appl Environ Microbiol 63:3205-3210.
16. 13C NMR flux ratio analysis of Escherichia coli central carbon metabolism in microaerobic bioprocesses. J Am Chem Soc 121:1407-1408.
17. Flores N, Xiao J, Berry A, Bolívar F, Valle F. 1996. Pathway engineering for the production of aromatic compounds in Escherichia coli. Nat Biotechnol 14:620-623.
18. 13C labeling and NMR spectroscopy. Metab Eng 4:124-137.
19. Fraenkel DG. 1968. The accumulation of glucose-6-phosphate from glucose and its effect in an Escherichia coli mutant lacking phosphoglucose isomerase and glucose-6-phosphate dehydrogenase. J Biol Chem 243:6451-6457.
20. Galkin A, Kulakova L, Yoshimura T, Soda K, Esaki N. 1997. Synthesis of optically active amino acids from α-keto acids with Escherichia coli cells expressing heterologous genes. Appl Environ Microbiol 63:4651-4656.
21. Glick BR. 1995. Metabolic load and heterologous gene expression. Biotechnol Adv 13:247-261.
22. Goeddel DV, Kleid DG, Bolívar F, Heyneker HL, Yansura DG, Crea R, Hirose T, Kraszewski A, Itakura K, Riggs AD. 1979. Expression in Escherichia coli of chemically synthesized genes for human insulin. Proc Natl Acad Sci USA 76:106-110.
23. Harrington TL, Glick BR, Lern NW. 1986. Molecular cloning of the phosphoenolpyruvate carboxylase gene of Anabaena variabilis. Gene 45:113-116.
24. Hoffman F, Rinas U. 2001. On-line estimation of the metabolic burden resulting from the synthesis of plasmid-encoded and heat-shock proteins by monitoring respiratory energy generation. Biotechnol Bioeng 76:333-340.
25. Hong Y, Pasternak JJ, Glick BR. 1995. Overcoming the metabolic load associated with the presence of plasmid DNA in the plant growth-promoting rhizobacterium Pseudomonas putida GR12-2. Can J Microbiol 41:624-628.
26. Itakura K, Hirose H, Crea R, Riggs AD, Heyndeker HL, Bolívar F, Boyer HW. 1977. Expression in Escherichia coli of a chemically synthesized gene for the hormone somatostatin. Science 198:1056-1063.
27. Jones KL, Kim S, Keasling JD. 2000. Low-copy plasmids can perform as well as or better than high-copy plasmids for metabolic engineering of bacteria. Metab Eng 3:328-338.
28. Kataoka M, Rohani LPS, Wada M, Kita K, Yanase H, Urabe I. 1998. Escherichia coli transformant expressing the glucose dehydrogenase gene from Bacillus megaterium as a cofactor regenerator in a chiral alcohol production system. Biosci Biotechnol Biochem 62:167-169.
29. 14C and estimation of the rates of transaldolase, transketolase, the contribution of the pentose cycle, and ribose phosphate synthesis. Biochemistry 6:2227-2247.
30. Kramer W, Elmecker G, Weik R, Mattanovich D, Bayer K. 1996. Kinetic studies for the optimization of recombinant protein formation. Ann NY Acad Sci 782:323-333.
31. LaDuca R, Berry A, Chotani G, Dodge T, Gosset G, Valle F, Liao J, Xiao J, and Power S. 1999. Metabolic pathway engineering of aromatic compounds. In: Davies JE, Demain AL, editors. Manual of industrial microbiology and biotechnology, 2nd edition. Washington, DC: American Society for Microbiology. p 605-615.
32. LaPorte DC, Walsh K, Koshland DE. 1984. The branch point effect. J Biol Chem 259:14068-14075.
33. Lessie TG, Vander-Wyk JC. 1972. Multiple forms of Pseudomonas multivorans glucose-6-phosphate and 6-phosphogluconate dehydrogenases: Differences in size, pyridine nucleotide specificity, and susceptibility to inhibition by adenosine 5′-triphosphate. J Bacteriol 110:1107-1117.
34. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. 1951. Protein measurement with the Folin phenol reagent. J Biol Chem 193:265-275.
35. Maitra PK, Lobo Z. 1971. A kinetic study of glycolytic enzyme synthesis in yeast. J Biol Chem 246:475-488.
36. Mendes P, Kell DB, Westerhoff HV. 1996. Why and when channeling can decrease pool size at constant net flux in a simple dynamic channel. Biochim Biophys Acta 1289:175-186.
37. Neidhardt FC, Ingraham JL, Scheachter M. 1990. Biosynthesis and fueling. In: Physiology of the bacterial cell. A molecular approach. Sunderland, MA: Sinauer Associates, Inc. p 133-173.
38. Olmos J, Cruz N, Sánchez M, López M, Balbás P, Gosset G, Valle F, Bolívar F. 1994. Production in Escherichia coli of a rat chimeric proinsulin polypeptide carrying a human A and B chains and its preparative chromatography. J Bacteriol 38:89-96.
39. Palmeros B, Wild J, Szybalski W, Le Borgne S, Hernández- Chávez G, Gosset G, Valle F, Bolívar F. 2000. A family of removable cassettes designed to obtain antibiotic-resistance-free genomic modifications of Escherichia coli and other bacteria. Gene 247:255-264.
40. Palmeros B. 2001. Diseño y construcción de sistemas genéticos para la regulación concertada de genes cromosomales en Escherichia coli. Ph.D. thesis. Cuernavaca, México: Instituto de Biotecnología-UNAM.
41. Rowley DL, Wolf RE Jr. 1991. Molecular characterization of the Escherichia coli K-12 zwf gene encoding glucose-6-phosphate dehydrogenase. J Bacteriol 173:968-997.
42. Schmidt M, Viaplana E, Hoffmann F, Marten S, Villaverde A, Rinas U. 1999. Secretion-dependent proteolysis of heterologous protein by recombinant Escherichia coli is connected to an increased activity of the energy-generating dissimilatory pathway. Biotechnol Bioeng 66:61-67.
43. Scorer CA, Carrier MJ, Rosenberger RF. 1991. Amino acid misincorporation during high-level expression of mouse epidermal growth factor in Escherichia coli. Nucleic Acids Res 19:3511-3516.
44. Seo JH, Bailey JE. 1985. Effects of recombinant plasmid content on growth properties and cloned gene product formation in Escherichia coli. Biotechnol Bioeng 27:1668-1674.
45. +-dependent malic enzyme in an Escherichia coli mutant. Appl Environ Microbiol 63:2695-2701.
46. Stephanopoulos GN, Aristidou AA, Nielsen J. 1998. Regulation of metabolic pathways. In: Stephanopoulos GN, editor. Metabolic engineering, principles and methodologies. San Diego: Academic Press. p 150-205.
47. 13C-labeling of proteinogenic amino acids: an efficient analytical tool to investigate intermediary metabolism. Eur J Biochem 232:433-448.
48. Tian WN, Braunstein LD, Pang J, Stuhlmeier KM, Xi QC, Tian X, Stanton RC. 1998. Importance of glucose-6-phosphate dehydrogenase activity for cell growth. J Biol Chem 273:10609-10617.