Development of stable isotope and selenomethionine labeling methods for proteins expressed in Pseudomonas fluorescens

Protein Expression and Purification

Volumn 65, Issue 1, 2009, Pages 57-65

  Madduri, Krishna ^a   Badger, Monty ^a   Li, Ze Sheng ^a   Xu, Xiaoping ^a   Thornburgh, Scott ^a   Evans, Steve ^a   Dhadialla, Tarlochan S ^a  

^a DOW AGROSCIENCES LLC   (United States)

Author keywords

MALDI TOF; NMR; Protein expression; Protein labeling; Pseudomonas fluorescens; Purification; Selenomethionine; Stable isotope

Indexed keywords

BACTERIAL PROTEIN; BACTERIAL TOXIN; NITROGEN; RECOMBINANT PROTEIN; SELENOMETHIONINE; XPTA1 PROTEIN, XENORHABDUS NEMATOPHILUS;

ARTICLE; BACILLUS THURINGIENSIS; BIOSYNTHESIS; CHEMISTRY; CLASSIFICATION; GENETICS; ISOTOPE LABELING; METABOLISM; PSEUDOMONAS FLUORESCENS; XENORHABDUS;

BACILLUS THURINGIENSIS; BACTERIAL PROTEINS; BACTERIAL TOXINS; ISOTOPE LABELING; NITROGEN ISOTOPES; PSEUDOMONAS FLUORESCENS; RECOMBINANT PROTEINS; SELENOMETHIONINE; XENORHABDUS;

BACILLUS THURINGIENSIS; PSEUDOMONAS FLUORESCENS; XENORHABDUS NEMATOPHILA;

EID: 60349115855     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2008.12.012     Document Type: Article

References (29)

1. Albala J.S., Franke K., McConnell I.R., Pak K.L., Folta P.A., Karlak B., Rubinfeld B., Davies A.H., Lennon G.G., and Clark R. From genes to proteins: high-throughput expression and purification of the human proteome. J. Cell. Biochem. 80 (2000) 187-191
2. Boettner M., Prinz B., Holz C., Stahl U., and Lang C. High-throughput screening for expression of heterologous proteins in the yeast Pichia pastoris. J. Biotechnol. 99 (2002) 51-62
3. Holz C., Hesse O., Bolotina N., Stahl U., and Lang C. A micro-scale process for high-throughput expression of cDNAs in the yeast Saccharomyces cerevisiae. Protein Exp. Purif. 25 (2002) 372-378
4. Yokoyama S. Protein expression systems for structural genomics and proteomics. Curr. Opin. in Chem. Biol. 7 (2003) 39-43
5. Chew L.C., Ramseier T.M., Retallack D.M., Schneider J.C., Squires C.H., and Talbot H.W. Pseudomonas fluorescens. In: Gellison G. (Ed). Production of Recombinant Protein (2005), Wiley-VCH
6. Madduri K., and Snodderley E.M. Expression of phosphinothricin N-acetyltransferase in Escherichia coli and Pseudomonas fluorescens: influence of mRNA secondary structure, host, and other physiological conditions. Protein Expr. Purif. 55 (2007) 352-360
7. Retallack D.M., Schneider J.C., Mitchell J., Chew L., and Liu H. Transport of heterologous proteins to the periplasmic space of Pseudomonas fluorescens using a variety of native signal sequences. Biotechnol. Lett. 29 (2007) 1483-1491
8. Tyler R.C., et al. Comparison of cell-based and cell-free protocols for producing target proteins from the Arabidopsis thaliana genome for structural studies. Proteins: Structure, Function, and Bioinformatics 59 (2005) 633-643
9. Jin H., Retallack D., Schneider J., Coleman R., Shao Y., Liu H., Woodard K., and Chew L. High throughput strain evaluation for therapeutic protein expression using Pfēnex Expression Technology (2007), Society for Industrial Microbiology, Denver, CO
10. Retallack D.M., Thomas T.C., Shao Y., Haney K.L., Resnick S.M., Lee V.D., and Squires C.H. Identification of anthranilate and benzoate metabolic operons of Pseudomonas fluorescens and functional characterization of their promoter regions. Microb. Cell Fact. 5 (2006) 1-13
11. Wishart D.S., Bigam C.G., Yao J., Abildgaard F., Dyson H.J., Oldfield E., Markley J.L., and Sykes B.D. J. Biomolecular NMR 6 (1995) 135-140
12. Dong L., Burton S., Glancy T., Li Z.-S., Hamptom R., Meade T., and Merlo D.J. Insect resistance conferred by 283-kDa Photorhabdus luminescens protein TcdA in Arabidopsis thaliana. Nat. Biotechnol. 21 (2003) 1222-1228
13. Shaw D., Odom J.D., and Dunlap R.B. High expression and steady-state kinetic characterization of methionine site-directed mutants of Escherichia coli methionyl- and selenomethionyl-dihydrofolate reductase. Biochem. Biophys. Acta 1429 (1999) 401-410
14. Wang W., Kappock J.T., Stubbe J.-A., and Ealick S.E. X-ray crystal structure of glycinamide ribonucleotide synthetase from Escherichia coli. Biochemistry 37 (1998) 15647-15662
15. Budisa N., Steipe B., Demange P., Eckerskorn C., Kellerman J., and Huber R. High-level biosynthetic substitution of methionine in proteins by its analogs 2-aminohexanoic acid, selenomethionine, telluromethionine and ethionine in Escherichia coli. Eur. J. Biochem. 230 (1995) 788-796
16. Yang W., Hendrickson W.A., Crouch R.J., and Satow Y. Structure of ribonuclease H phased at 2 A resolution by MAD analysis of the selenomethionyl protein. Science 21 249 (1990) 1398-1405
17. Morgan J.A.M., Sergeant M., Ellis D., Ousley M., and Jarrett P. Sequence analysis of insecticidal genes from Xenorhabdus nematophilus PMFI296. Appl. Environ. Microbiol. 67 (2001) 2062-2069
18. Sergeant M., Jarrett P., Ousley M., and Morgan J.A.M. Interactions of insecticidal toxin gene products from Xenorhabdus nematophilus PMFI296. Appl. Environ. Microbiol. 69 (2003) 3344-3349
19. Deidda D., Lampis G., Maullu C., Pompei R., Isaia F., Lippolis V., and Verani G. Antifungal, antibacterial, antiviral and cytotoxic activity of novel thio- and seleno-azoles. Pharmacol. Res. 36 (1997) 193-197
20. French-Constant R.H., Dowling A., and Waterfield N.R. Insecticidal toxins from Photorhabdus bacteria and their potential use in agriculture. Toxicon 49 (2007) 436-451
21. Hendrickson W.A., Horton J.R., and LeMaster D.M. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure. EMBO J. 9 (1990) 1665-1672
22. Doublie S. Preparation of selenomethionyl proteins for phase determination. In: Carter C.W., and Sweet R.M. (Eds). Methods in Enzymology 276 (1997), Academic Press, San Diego, CA 523-530
23. Alamitos M., and Ramos J. The methionine biosynthetic pathway from homoserine in Pseudomonas putida involves the metW, metX, metZ, metH and metE gene products. Arch. Microbiol. 176 (2001) 151-154
24. Chen W.Y., and Bahl O.P. Recombinant carbohydrate and selenomethionyl variants of human choriogonadotropin. J. Biol. Chem. 266 (1991) 8192-8197
25. Chen W.Y., and Bahl O.P. Selenomethionyl analog of recombinant human choriogonadotropin. J. Biol. Chem. 266 (1991) 9355-9358
26. Goulding C.W., and Perry L.J. Protein production in Escherichia coli for structural studies by X-ray crystallography. J. Struct. Biol. 142 (2003) 133-143
27. P.F.Berne, S. Doulie, C.W. Carter, in. Crystallization of Nucleic Acids and Proteins, Oxford, 1999, pp. 45-73.
28. Bernard A.R., Wells T.N., Cleasby A., Borlat F., Payton M.A., and Proudfoot A.E. Selenomethionine labelling of phosphomannose isomerase changes its kinetic properties. Eur. J. Biochem. 230 (1995) 111-118
29. Yang W., Hendrickson W.A., Kalman E.T., and Crouch R.J. Expression, purification, and crystallization of natural and selenomethionyl recombinant ribonuclease H from Escherichia coli. J. Biol. Chem. 265 (1990) 13553