Cell-free synthesis of proteins that require disulfide bonds using glucose as an energy source

Biotechnology and Bioengineering

Volumn 97, Issue 4, 2007, Pages 901-908

  Knapp, Kurtis G ^a   Goerke, Aaron R ^a   Swartz, James R ^a  

^a Stanford University   (United States)

Author keywords

Cell free protein synthesis; Disulfide bond; Glucose; Protein folding; Urokinase

Indexed keywords

CELL-FREE PROTEIN SYNTHESIS; DISULFIDE BOND; UROKINASE;

CELLS; DRUG THERAPY; ENZYMES; GLUCOSE; SYNTHESIS (CHEMICAL); VACCINES;

PROTEIN FOLDING;

GLUCOSE; GLUTATHIONE REDUCTASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; IODOACETAMIDE; THIOREDOXIN REDUCTASE; UROKINASE;

AFFINITY CHROMATOGRAPHY; ARTICLE; BIOLOGICAL ACTIVITY; CELL FREE SYSTEM; DELETION MUTANT; DISULFIDE BOND; ENZYME ACTIVITY; PH MEASUREMENT; PROTEIN FOLDING; PROTEIN SYNTHESIS;

ANIMALS; CELL PROLIFERATION; CELL-FREE SYSTEM; CHROMATOGRAPHY, AFFINITY; CYTOPLASM; DISULFIDES; DOSE-RESPONSE RELATIONSHIP, DRUG; ENZYME INHIBITORS; GLUCOSE; GLUTATHIONE; GRANULOCYTE-MACROPHAGE COLONY-STIMULATING FACTOR; HYDROGEN-ION CONCENTRATION; IODOACETAMIDE; MICE; OXIDATION-REDUCTION; OXIDOREDUCTASES; PROTEIN FOLDING; THIOREDOXIN; URINARY PLASMINOGEN ACTIVATOR;

MAMMALIA; MURINAE;

EID: 34447324367     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.21296     Document Type: Article

References (23)

1. Calhoun KA, Swartz JR. 2005a. An economical method for cell-free protein synthesis using glucose and nucleoside monophosphates. Biotechnol Prog 21(4):1146-1153.
2. Calhoun KA, Swartz JR. 2005b. Energizing cell-free protein synthesis with glucose metabolism. Biotechnol Bioeng 90(5):606-613.
3. Calhoun KA, Swartz JR. 2006. Total amino acid stabilization during cell-free protein synthesis reactions. Biotechnol Bioeng 123(2):193-203.
4. Chivers PT, Prehoda KE, Raines RT. 1997. The CXXC motif: A rheostat in the active site. Biochemistry 36(14):4061-4066.
5. Cumming RC, Andon NL, Haynes PA, Park M, Fischer WH, Schubert D. 2004. Protein disulfide bond formation in the cytoplasm during oxidative stress. J Biol Chem 279(21):21749-21758.
6. Datsenko KA, Wanner BL. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci USA 97(12):6640-6645.
7. Davanloo P, Rosenberg AH, Dunn JJ, Studier FW. 1984. Cloning and expression of the gene for bacteriophage T7 RNA polymerase. Proc Natl Acad Sci USA 81(7):2035-2039.
8. Flashner M, Hollenberg PF, Coon MJ. 1972. Mechanism of action of pyruvate kinase. Role of sulfhydryl groups in catalytic activity as determined by disulfide interchange. J Biol Chem 247(24):8114-8121.
9. Jewett MC, Swartz JR. 2004. Mimicking the Escherichia coli cytoplasmic environment activates long-lived and efficient cell-free protein synthesis. Biotechnol Bioeng 86(1):19-26.
10. Kigawa T, Muto Y, Yokoyama S. 1995. Cell-free synthesis and amino acid-selective stable isotope labeling of proteins for NMR analysis. J Biomol NMR 6(2):129-134.
11. Kim DM, Swartz JR. 2004. Efficient production of a bioactive, multiple disulfide-bonded protein using modified extracts of Escherichia coli. Biotechnol Bioeng 85(2):122-129.
12. Knapp KG, Swartz JR. 2004. Cell-free production of active E. coli thioredoxin reductase and glutathione reductase. FEBS Lett 559(1-3):66-70.
13. Liu DV, Zawada JF, Swartz JR. 2005. Streamlining Escherichia coli S30 extract preparation for economical cell-free protein synthesis. Biotechnol Prog 21(2):460-465.
14. Michel-Reydellet N, Calhoun K, Swartz J. 2004. Amino acid stabilization for cell-free protein synthesis by modification of the Escherichia coli genome. Metab Eng 6(3):197-203.
15. O'Donnell ME, Williams CH, Jr. 1983. Proton stoichiometry in the reduction of the FAD and disulfide of Escherichia coli thioredoxin reductase. Evidence for a base at the active site. J Biol Chem 258(22):13795-13805.
16. Polgar L. 1973. On the mode of activation of the catalytically essential sulfhydryl group of papain. Eur J Biochem 33(1):104-109.
17. Polgar L. 1975. Ion-pair formation as a source of enhanced reactivity of the essential thiol group of D-glyceraldehyde-3-phosphate dehydrogenase. Eur J Biochem 51(1):63-71.
18. Ritz D, Lim J, Reynolds CM, Poole LB, Beckwith J. 2001. Conversion of a peroxiredoxin into a disulfide reductase by a triplet repeat expansion. Science 294(5540):158-160.
19. Thomas JA, Mallis RJ. 2001. Aging and oxidation of reactive protein sulfhydryls. Exp Gerontol 36(9):1519-1526.
20. Voloshin AM, Swartz JR. 2005. Efficient and scalable method for scaling up cell free protein synthesis in batch mode. Biotechnol Bioeng 91(4):516-521.
21. Yang J, Kanter G, Voloshin A, Levy R, Swartz JR. 2004. Expression of active murine granulocyte-macrophage colony-stimulating factor in an Escherichia coli cell-free system. Biotechnol Prog 20(6):1689-1696.
22. Yin G, Swartz JR. 2004. Enhancing multiple disulfide bonded protein folding in a cell-free system. Biotechnol Bioeng 86(2):188-195.
23. Zawada J, Swartz J. 2005. Maintaining rapid growth in moderate-density Escherichia coli fermentations. Biotechnol Bioeng 89(4):407-415.