New vectors for co-expression of proteins: Structure of Bacillus subtilis ScoAB obtained by high-throughput protocols

Protein Expression and Purification

Volumn 53, Issue 2, 2007, Pages 396-403

  Stols, Lucy ^a   Zhou, Min ^a   Eschenfeldt, William H ^a   Millard, Cynthia Sanville ^a   Abdullah, James ^a   Collart, Frank R ^a   Kim, Youngchang ^a   Donnelly, Mark I ^a  

^a ARGONNE NATIONAL LABORATORY   (United States)

Author keywords

Co expression; Co purification; Coenzyme A transferase; Expression vectors; High throughput; Structural genomics

Indexed keywords

3 OXOACID COENZYME A TRANSFERASE; 3-KETOACID COA-TRANSFERASE; BACTERIAL DNA; BACTERIAL PROTEIN; COENZYME A TRANSFERASE; PROTEIN SUBUNIT; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BACILLUS SUBTILIS; BACTERIAL GENE; CHEMICAL STRUCTURE; CRYSTALLIZATION; ENZYMOLOGY; GENE EXPRESSION; GENE VECTOR; GENETICS; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR CLONING; NUCLEOTIDE SEQUENCE; X RAY CRYSTALLOGRAPHY;

BACILLUS SUBTILIS; BACTERIAL PROTEINS; BASE SEQUENCE; CLONING, MOLECULAR; COENZYME A-TRANSFERASES; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DNA, BACTERIAL; GENE EXPRESSION; GENES, BACTERIAL; GENETIC VECTORS; MODELS, MOLECULAR; PROTEIN SUBUNITS; RECOMBINANT PROTEINS;

BACILLUS SUBTILIS; NICOTIANA TABACUM; TOBACCO ETCH VIRUS;

EID: 33947419312     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2007.01.013     Document Type: Article

References (41)

1. Creighton T.E. Proteins: Structures and Molecular Properties (1993), W.H. Freeman and Company, New York
2. Petsko G., and Ringe D. Protein Structure and Function (2003), Sinauer Associates, Sunderland, Massachusetts
3. Wold F. Macromolecules: Structure and Function (1971), Prentice-Hall, London
4. Gavin A.C., and Superti-Furga G. Protein complexes and proteome organization from yeast to man. Curr. Opin. Chem. Biol. 7 (2003) 21-27
5. Harrison S.C. Whither structural biology?. Nat. Struct. Mol. Biol. 11 (2004) 12-15
6. Stevens R.C. Long live structural biology. Nat. Struct. Mol. Biol. 11 (2004) 293-295
7. Parrish J.R., Gulyas K.D., and Finley Jr. R.L. Yeast two-hybrid contributions to interactome mapping. Curr. Opin. Biotechnol. 17 (2006) 387-393
8. Pitre S., Dehne F., Chan A., Cheetham J., Duong A., Emili A., Gebbia M., Greenblatt J., Jessulat M., Krogan N., Luo X., and Golshani A. PIPE: a protein-protein interaction prediction engine based on the re-occurring short polypeptide sequences between known interacting protein pairs. BMC Bioinformatics 7 (2006) 365
9. Strong M., Sawaya M.R., Wang S., Phillips M., Cascio D., and Eisenberg D. Toward the structural genomics of complexes: crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. USA 103 (2006) 8060-8065
10. Suter B., Auerbach D., and Stagljar I. Yeast-based functional genomics and proteomics technologies: the first 15 years and beyond. Biotechniques 40 (2006) 625-644
11. Fu H. Protein-protein interactions: methods and applications (2004), Humana Press, Totowa, NJ
12. Alexandrov A., Vignali M., LaCount D.J., Quartley E., de Vries C., De Rosa D., Babulski J., Mitchell S.F., Schoenfeld L.W., Fields S., Hol W.G., Dumont M.E., Phizicky E.M., and Grayhack E.J. A facile method for high-throughput co-expression of protein pairs. Mol. Cell. Proteomics 3 (2004) 934-938
13. Chanda P.K., Edris W.A., and Kennedy J.D. A set of ligation-independent expression vectors for co-expression of proteins in Escherichia coli. Protein Expr. Purif. 47 (2006) 217-224
14. Dzivenu O.K., Park H.H., and Wu H. General co-expression vectors for the overexpression of heterodimeric protein complexes in Escherichia coli. Protein Expr. Purif. 38 (2004) 1-8
15. Johnston K., Clements A., Venkataramani R.N., Trievel R.C., and Marmorstein R. Coexpression of proteins in bacteria using T7-based expression plasmids: expression of heteromeric cell-cycle and transcriptional regulatory complexes. Protein Expr. Purif. 20 (2000) 435-443
16. Johnston K., and Marmorstein R. Co-expression of proteins in E. coli using dual expression vectors. Methods Mol. Biol. 205 (2003) 205-213
17. Kholod N., and Mustelin T. Novel vectors for co-expression of two proteins in E. coli. Biotechniques 31 (2001) 322-3-326-8
18. Kim K.J., Kim H.E., Lee K.H., Han W., Yi M.J., Jeong J., and Oh B.H. Two-promoter vector is highly efficient for overproduction of protein complexes. Protein Sci. 13 (2004) 1698-1703
19. Lueking A., Horn S., Lehrach H., and Cahill D.J. A dual-expression vector allowing expression in E. coli and P. pastoris, including new modifications. Methods Mol. Biol. 205 (2003) 31-42
20. Mullinax R.L., Wong D.T., Davis H.A., Padgett K.A., and Sorge J.A. Dual-expression vectors for efficient protein expression in both E. coli and mammalian cells. Methods Mol. Biol. 205 (2003) 19-30
21. Tolia N., and Joshua-Tor L. Strategies for protein coexpression in Escherichia coli. Nature Methods 3 (2006) 55-64
22. Romier C., Ben Jelloul M., Albeck S., Buchwald G., Busso D., Celie P.H., Christodoulou E., De Marco V., van Gerwen S., Knipscheer P., Lebbink J.H., Notenboom V., Poterszman A., Rochel N., Cohen S.X., Unger T., Sussman J.L., Moras D., Sixma T.K., and Perrakis A. Co-expression of protein complexes in prokaryotic and eukaryotic hosts: experimental procedures, database tracking and case studies. Acta Crystallogr. D Biol. Crystallogr. 62 (2006) 1232-1242
23. Studier F.W., Rosenberg A.H., Dunn J.J., and Dubendorff J.W. Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol. 185 (1990) 60-89
24. Parks T.D., Leuther K.K., Howard E.D., Johnston S.A., and Dougherty W.G. Release of proteins and peptides from fusion proteins using a recombinant plant virus proteinase. Anal. Biochem. 216 (1994) 413-417
25. Kim Y., Dementieva I., Zhou M., Wu R., Lezondra L., Quartey P., Joachimiak G., Korolev O., Li H., and Joachimiak A. Automation of protein purification for structural genomics. J. Struct. Funct. Genomics 5 (2004) 111-118
26. Stols L., Gu M., Dieckman L., Raffen R., Collart F.R., and 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
27. Raines R.T., McCormick M., Van Oosbree T.R., and Mierendorf R.C. The S tag fusion system for protein purification. Methods Enzymol. 326 (2000) 362-376
28. Yoon J.R., Laible P.D., Gu M., Scott H.N., and Collart F.R. Express primer tool for high-throughput gene cloning and expression. Biotechniques 33 (2002) 1328-1333
29. Moy S., Dieckman L., Schiffer M., Maltsev N., Yu G.X., and Collart F.R. Genome-scale expression of proteins from Bacillus subtilis. J. Struct. Funct. Genomics 5 (2004) 103-109
30. Corthesy-Theulaz I.E., Bergonzelli G.E., Henry H., Bachmann D., Schorderet D.F., Blum A.L., and Ornston L.N. Cloning and characterization of Helicobacter pylori succinyl CoA:acetoacetate CoA-transferase, a novel prokaryotic member of the CoA-transferase family. J. Biol. Chem. 272 (1997) 25659-25667
31. Howard J.B., Zieske L., Clarkson J., and Rathe L. Mechanism-based fragmentation of coenzyme A transferase. Comparison of alpha 2-macroglobulin and coenzyme A transferase thiol ester reactions. J. Biol. Chem. 261 (1986) 60-65
32. Stols L., Millard C.S., Dementieva I., and Donnelly M.I. Production of selenomethionine-labeled proteins in two-liter plastic bottles for structure determination. J. Struct. Funct. Genomics 5 (2004) 95-102
33. Sambrook J., Fritsch E.F., and Maniatis T. Molecular Cloning: A Laboratory Manual. 2nd ed. (1989), Cold Spring Harbor Press, Cold Spring Harbor, NY
34. Coros A.M., Swenson L., Wolodko W.T., and Fraser M.E. Structure of the CoA transferase from pig heart to 1.7 A resolution. Acta Crystallogr. D Biol. Crystallogr. 60 (2004) 1717-1725
35. Bateman K.S., Brownie E.R., Wolodko W.T., and Fraser M.E. Structure of the mammalian CoA transferase from pig heart. Biochemistry 41 (2002) 14455-14462
36. Parales R.E., and Harwood C.S. Characterization of the genes encoding beta-ketoadipate: succinyl-coenzyme a transferase in Pseudomonas putida. J. Bacteriol. 174 (1992) 4657-4666
37. Jacob U., Mack M., Clausen T., Huber R., Buckel W., and Messerschmidt A. Glutaconate CoA-transferase from Acidaminococcus fermentans: the crystal structure reveals homology with other CoA-transferases. Structure 5 (1997) 415-426
38. Korolev S., Koroleva O., Petterson K., Gu M., Collart F., Dementieva I., and Joachimiak A. Autotracing of Escherichia coli acetate CoA-transferase alpha-subunit structure using 3.4 A MAD and 1.9 A native data. Acta Crystallogr. D Biol. Crystallogr. 58 (2002) 2116-2121
39. Rochet J.C., Brownie E.R., Oikawa K., Hicks L.D., Fraser M.E., James M.N., Kay C.M., Bridger W.A., and Wolodko W.T. Pig heart CoA transferase exists as two oligomeric forms separated by a large kinetic barrier. Biochemistry 39 (2000) 11291-11302
40. Donnelly M.I., Zhou M., Millard C.S., Clancy S., Stols L., Eschenfeldt W.H., Collart F.R., and Joachimiak A. An expression vector tailored for large-scale, high-throughput purification of recombinant proteins. Protein Expr. Purif. 47 (2006) 446-454
41. Dieckman L.J., Zhang W., Rodi D.J., Donnelly M.I., and Collart F.R. Bacterial expression strategies for human angiogenesis proteins. J. Struct. Funct. Genomics 7 (2006) 23-30