Refolding, purification, and characterization of a loop deletion mutant of human Bcl-2 from bacterial inclusion bodies

Protein Expression and Purification

Volumn 15, Issue 2, 1999, Pages 162-170

  Anderson, Malcolm ^a   Blowers, David ^a   Hewitt, Neil ^a   Hedge, Philip ^a   Breeze, Alexander ^a   Hampton, Ian ^a   Taylor, Ian ^a  

^a Cancer and Infect Res Depts   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CHELATE; CHROMATOGRAPHY; MUTANT PROTEIN; NICKEL; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN STRUCTURE; RECOMBINANT PROTEIN;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0033102489     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1998.0996     Document Type: Article

References (37)

1. Thompson C. B. Apoptosis in the pathogenesis and treatment of disease. Science. 267:1995;1456-1462.
2. Raff M. C. Social controls on cell survival and cell death. Nature. 356:1992;397-400.
3. Tsujimoto Y., Gorham J., Cossman J., Jaffe E., Croce C. M. The t(14;18) chromosome translocations involved in B-cell neoplasms result from mistakes in VDJ joining. Science. 229:1985;1390-1393.
4. Korsmeyer S. J. Regulators of cell death. Trends Genet. 11:1995;101-105.
5. Vaux D. L., Cory S., Adams J. M. Bcl-2 gene promotes haemopoietic cell survival and cooperates with c-myc to immortalize pre-B cells. Nature. 335:1988;440-442.
6. Nunez G., London L., Hockenbery D., Alexander M., McKearn J. P., Korsmeyer S. J. Deregulated Bcl-2 gene expression selectively prolongs survival of growth factor-deprived hemopoietic cell lines. J. Immunol. 144:1990;3602-3610.
7. Hockenbery D. M., Oltvai Z. N., Yin X.-M., Milliman C. L., Korsmeyer S. J. Bcl-2 functions in an antioxidant pathway to prevent apoptosis. Cell. 75:1993;241-251.
8. L. EMBO J. 16:1997;1686-1694.
9. White E. Life, death, and the pursuit of apoptosis. Genes Dev. 10:1996;1-15.
10. O'Connor L., Strasser A., O'Reilly L. A., Hausmann G., Adams J. M., Cory S., Huang D. C. S. Bim: a novel member of the Bcl-2 family that promotes apoptosis. EMBO J. 17:1998;384-395.
11. Farrow S. N., Brown R. New members of the Bcl-2 family and their protein partners. Curr. Opin. Genet. Dev. 6:1996;45-49.
12. Reed J. C. Double identity for proteins of the Bcl-2 family. Nature. 387:1997;773-776.
13. Oltvai Z. N., Korsmeyer S. J. Checkpoints of dueling dimers foil death wishes. Cell. 79:1994;189-192.
14. L. Nature. 381:1996;335-341.
15. L. Nature. 385:1997;353-357.
16. Schendel S. L., Xie Z., Montal M. O., Matsuyama S., Montal M., Reed J. C. Channel formation by antiapoptotic protein Bcl-2. Proc. Natl. Acad. Sci. USA. 94:1997;5113-5118.
17. Cosulich S. C., Green S., Clarke P. R. Bcl-2 regulates activation of apoptotic proteases in a cell-free system. Curr. Biol. 6:1996;997-1005.
18. Rao L., White W. Bcl-2 and ICE family of apoptotic regulators: making a connection. Curr. Opin. Genet. Dev. 7:1997;52-58.
19. Yuan J., Horvitz H. R. TheCaenorhabditis elegansced-3ced-4. Dev. Biol. 138:1990;33-41.
20. Alnemri E. S., Livingston D. J., Nicholson D. W., Salvesen G., Thornberry N. A., Wong W. W., Yuan J. Human ICE/CED-3 protease nomenclature. Cell. 87:1996.
21. Liu X., Kim C. N., Yang J., Jemmerson R., Wang X. Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c. Cell. 86:1996;147-157.
22. Kluck R. M., Bossy-Wetzel E., Green D. R., Newmeyer D. D. The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis. Science. 275:1997;1132-1136.
23. Yang J., Liu X., Bhalla K., Kim C. N., Ibrado A. M., Cai J., Peng T.-I., Jones D. P., Wang X. Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked. Science. 275:1997;1129-1132.
24. Vance B. A., Zacharchuk C. M., Segal D. M. Recombinant mouse Bcl-2(1-203). Two domains connected by a long protease-sensitive linker. J. Biol. Chem. 271:1996;30811-30815.
25. Haldar S., Jena N., Dubois G. C., Takayama S., Reed J. C., Fu S. S., Croce C. M. Purification and characterization of the bcl-2 protein. Arch. Biochem. Biophys. 315:1994;483-488.
26. Studier F. W., Moffatt B. A. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189:1986;113-130.
27. Kara B. V., Hockney R. C. Leucine imbalance stimulates accumulation of G-CSF inE. coli. Biologicals from Recombinant Microorganisms: Production and Recovery. 1991;VCH, Weinheim. p. 47-53.
28. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
29. Cosulich S. C., Worrall V., Hedge P. J., Green S., Clarke P. R. Regulation of apoptosis by BH3 domains In a cell-free system. Curr. Biol. 7:1997;913-920.
30. Lazebnik S. H., Kaufmann S. H., Desnoyers S., Poirier G. G., Earnshaw W. C. Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE. Nature. 371:1994;346-347.
31. Nicholson D. W., Ali A., Thornberry N. A., Vaillancourt J. P., Ding C. K., Gallant M. Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. Nature. 376:1995;37-43.
32. Rudolph R. Renaturation of recombinant, disulfide-bonded proteins from inclusion bodies. Tschesche H. Modern Methods in Protein and Nucleic Acid Research. 1990;149-172 de Gruyter, New York.
33. abEscherichia coli. Bio/Technology. 9:1991;157-162.
34. Brinkmann U., Buchner J., Pastan I. Independent domain folding ofPseudomonas. Proc. Natl. Acad. Sci. USA. 89:1992;3075-3079.
35. Lin W. J., Traugh J. A. Renaturation of casein kinase II from recombinant subunits produced inEscherichia coli: Protein Expression Purif. 4:1993;256-264.
36. Rudolph R., Lilie H. In vitro folding of inclusion body proteins. FASEB J. 10:1996;49-56.
37. Hirel P.-H., Schmitter J.-M., Dessen P., Fayat G., Blanquet S. Extent of N-terminal methionine excision fromEscherichia coli. Proc. Natl. Acad. Sci. USA. 86:1989;8247-8251.