Bacterial cell-free system for high-throughput protein expression and a comparative analysis of Escherichia coli cell-free and whole cell expression systems

Protein Expression and Purification

Volumn 36, Issue 2, 2004, Pages 217-225

  Murthy, T V S ^a   Wu, Weilin ^a,b   Qiu, Q Q ^a   Shi, Zhenwei ^a   Labaer, Joshua ^a   Brizuela, Leonardo ^a  

^a Department of Biological Chemistry and Molecular Pharmacology   (United States)

^b KAROLINSKA INSTITUTE   (Sweden)

Author keywords

High throughput protein expression; In vitro protein synthesis; Pseudomonas aeruginosa; Two component system

Indexed keywords

BACTERIAL PROTEIN;

AFFINITY CHROMATOGRAPHY; ARTICLE; CELL FREE SYSTEM; CHEMISTRY; COMPARATIVE STUDY; ESCHERICHIA COLI; GENE EXPRESSION; GENETICS; ISOLATION AND PURIFICATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PSEUDOMONAS AERUGINOSA;

BACTERIAL PROTEINS; CELL-FREE SYSTEM; CHROMATOGRAPHY, AFFINITY; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; GENE EXPRESSION; PSEUDOMONAS AERUGINOSA;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; PSEUDOMONAS; PSEUDOMONAS AERUGINOSA;

EID: 3142533355     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2004.04.002     Document Type: Article

References (34)

1. Brizuela L., Braun P., Labaer J. FLEXGene repository: from sequenced genomes to gene repositories for high-throughput functional biology and proteomics. Mol. Biochem. Parasitol. 118:2001;155-165
2. Dieckman L., Gu M., Stols L., Donnelly M.I., Collart F.R. High-throughput methods for gene cloning and expression. Protein Expr. Purif. 25:2002;1-7
3. Reboul J., Vaglio P., Rual J.F., et al. C. elegans ORFeome version 1.1: experimental verification of the genome annotation and resource for proteome-scale protein expression. Nat. Genet. 34(1):2003;35-41
4. Braun P., Hu Y., Shen B., Halleck A., Koundinya M., Harlow E., LaBaer J. Proteome-scale purification of human proteins from bacteria. Proc. Natl. Acad. Sci. USA. 99(5):2002;2654-2659
5. Scheich C., Sievert V., Bussow K. An automated method for high-throughput protein purification applied to a comparison of His-tag and GST-tag affinity chromatography. Bio. Med. Central Biotechnol. 12:2003;1-8
6. Miroux B., Walker J.E. Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260:1996;289-298
7. Braun P., LaBaer J. High throughput protein production for functional proteomics. Trends Biotechnol. 21(9):2003;383-388
8. Holz C., Hesse O., Bolotina N., Stahl U., Lang C. A micro-scale process for high-throughput expression of cDNAs in the yeast Saccharomyces cerevisiae. Protein Expr. Purif. 25(3):2002;372-378
9. Stols L., Gu M., Dieckman L., Raffen R., Collart F.R., Donnelly M.I. A new vector for high-throughput, ligation-independent cloning encoding a tobacco etch virus protease cleavage site. Protein Expr. Purif. 25:2002;8-15
10. Kurland C.G. Translational accuracy in vitro. Cell. 28:1982;201-202
11. Golf S.A., Goldberg A.L. An increased content of protease La, the lone gene product, increases protein degradation and blocks growth in Escherichia coli. J. Biol. Chem. 262:1987;4508-4515
12. Kigawa T., Muto Y., Yokoyama S. Cell-free synthesis and amino acid-selective stable isotope labeling of proteins for NMR analysis. J. Biomol. NMR. 6(2):1995;129-134
13. Hirao I., Ohtsuki T., Fujiwara T., Mitsui T., Yokogawa T., Okuni T., Nakayama H., Takio K., Yabuki T., Kigawa T., Kodama K., Nishikawa K., Yokoyama S. An unnatural base pair for incorporating amino acid analogs into proteins. Nat. Biotechnol. 20:2002;177-182
14. Gite S., Lim M., Carlson R., Olejnik J., Zehnbauer B., Rothschild K. A high-throughput nonisotopic protein truncation test. Nat. Biotechnol. 21:2003;194-197
15. Traverso G., Diehl F., Hurst R., Shuber A., Whitney D., Johnson C., Levin B., Kinzler K.W., Vogelstein B. Multicolor in vitro translation. Nat. Biotechnol. 9:2003;1093-1097
16. Jermutus L., Ryabova L.A., Pluckthun A. Recent advances in producing and selecting functional proteins by using cell-free translation. Curr. Opin. Biotechnol. 9:1998;534-548
17. Devries J.K., Zubay G. DNA-directed peptide synthesis. 3. Repression of beta-galactosidase synthesis and inhibition of repressor by inducer in a cell-free system. Proc. Natl. Acad. Sci. USA. 58(4):1967;1669-1675
18. Kim D.M., Kigawa T., Choi C.Y., Yokoyama S. A highly efficient cell-free protein synthesis system from Escherichia coli. Eur. J. Biochem. 239(3):1996;881-886
19. Kigawa T., Yabuki T., Yoshida Y., Tsutsui M., Ito Y., Shibata T., Yokoyama S. Cell-free production and stable-isotope labeling of milligram quantities of proteins. FEBS Lett. 442(1):1999;9-15
20. Kim D.M., Swartz J.R. Prolonging cell-free protein synthesis with a novel ATP regeneration system. Biotechnol. Bioeng. 66(3):1999;180-188
21. Kitaoka Y., Nishimura N., Niwano M. Cooperativity of stabilized mRNA and enhanced translation activity in the cell-free system. J. Biotechnol. 48:1996;1-8
22. Spirin A.S., Baranov V.I., Ryabova L.A., Ovodov S.Y., Alakhov Y.B. A continuous cell-free translation system capable of producing polypeptides in high yield. Science. 242:1988;1162-1164
23. Sawasaki T., Hasegawa Y., Tsuchimochi M., Kamura N., Ogasawara T., Kuroita T., Endo Y. A bilayer cell-free protein synthesis system for high-throughput screening of gene products. FEBS Lett. 514(1):2002;102-105
24. Renesto P., Raoult D. From genes to proteins: in vitro expression of rickettsial proteins. Ann. N. Y. Acad. Sci. 990:2003;642-652
25. Betton J.M. Rapid translation system (RTS): a promising alternative for recombinant protein production. Curr. Protein Pept. Sci. 4(1):2003;73-80
26. Lesley S.A., Brow M.A., Burgess R.R. Use of in vitro protein synthesis from polymerase chain reaction-generated templates to study interaction of Escherichia coli transcription factors with core RNA polymerase and for epitope mapping of monoclonal antibodies. J. Biol. Chem. 266:1991;2632-2638
27. Rodrigue A., Quentin Y., Lazdunski A., Mejean V., Foglino M. Two-component systems in Pseudomonas aeruginosa: why so many? Trends Microbiol. 8(11):2000;498-504
28. Davanloo P., Rosenberg A.H., Dunn J.J., Studier F.W. Cloning and expression of the gene for bacteriophage T7 RNA polymerase. Proc. Natl. Acad. Sci. USA. 81(7):1984;2035-2039
29. Harlow E., Lane D. Using Antibodies: A Laboratory Manual. 1999;Cold Spring Harbor Laboratory Press, Plainview, NY
30. Ramachandiran V., Kramer G., Hardesty B. Expression of different coding sequences in cell-free bacterial and eukaryotic systems indicates translational pausing on Escherichia coli ribosomes. FEBS Lett. 482:2000;185-188
31. Busso D., Kim R., Kim S.-H. Expression of soluble recombinant proteins in a cell-free system using a 96-well format. J. Biochem. Biophys. Methods. 55:2003;233-240
32. Kawahashi Y., Doi N., Takashima H., Tsuda C., Oishi Y., Oyama R., Yonezawa M., Miyamoto-Sato E., Yanagawa H. In vitro protein microarrays for detecting protein-protein interactions: application of a new method for fluorescence labeling of proteins. Proteomics. 3:2003;1236-1243
33. MacBeath G., Schreiber S.L. Printing proteins as microarrays for high-throughput function determination. Science. 289:2000;1760-1763
34. Huang R.Y., Boulton S.J., Vidal M., Almo S.C., Bresnick A.R., Chance M.R. High-throughput expression, purification, and characterization of recombinant Caenorhabditis elegans proteins. Biochem. Biophys. Res. Commun. 307(4):2003;928-934