Correlation of Levels of Folded Recombinant p53 in Escherichia coli with Thermodynamic Stability in Vitro

Journal of Molecular Biology

Volumn 372, Issue 1, 2007, Pages 268-276

  Mayer, Sebastian ^a   Rüdiger, Stefan ^a   Ang, Hwee Ching ^a   Joerger, Andreas C ^a   Fersht, Alan R ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

cancer; expression; folding; GFP; protein stability

Indexed keywords

GREEN FLUORESCENT PROTEIN; PROTEIN P53; RECOMBINANT PROTEIN;

ARTICLE; ESCHERICHIA COLI; IN VITRO STUDY; IN VIVO STUDY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN STABILITY; THERMODYNAMICS;

ESCHERICHIA COLI;

EID: 34547687667     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.06.044     Document Type: Article

References (44)

1. Serrano L., Day A.G., and Fersht A.R. Step-wise mutation of barnase to binase. A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability. J. Mol. Biol. 233 (1993) 305-312
2. Meiering E.M., Serrano L., and Fersht A.R. Effect of active site residues in barnase on activity and stability. J. Mol. Biol. 225 (1992) 585-589
3. Gething M.J., and Sambrook J. Protein folding in the cell. Nature 355 (1992) 33-45
4. Bullock A.N., and Fersht A.R. Rescuing the function of mutant p53. Nature Rev. Cancer 1 (2001) 68-76
5. Joerger A.C., Ang H.C., and Fersht A.R. Structural basis for understanding oncogenic p53 mutations and designing rescue drugs. Proc. Natl Acad. Sci. USA 103 (2006) 15056-15061
6. Canadillas J.M., Tidow H., Freund S.M., Rutherford T.J., Ang H.C., and Fersht A.R. Solution structure of p53 core domain: structural basis for its instability. Proc. Natl Acad. Sci. USA 103 (2006) 2109-2114
7. Fersht A.R., and Serrano L. Principles of protein stability derived from protein engineering experiments. Curr. Opin. Struct. Biol. 3 (1993) 75-83
8. Parsell D.A., and Sauer R.T. The structural stability of a protein is an important determinant of its proteolytic susceptibility in Escherichia coli. J. Biol. Chem. 264 (1989) 7590-7595
9. Ghaemmaghami S., and Oas T.G. Quantitative protein stability measurement in vivo. Nature Struct. Biol. 8 (2001) 879-882
10. Philipps B., Hennecke J., and Glockshuber R. FRET-based in vivo screening for protein folding and increased protein stability. J. Mol. Biol. 327 (2003) 239-249
11. Ignatova Z., and Gierasch L.M. Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling. Proc. Natl Acad. Sci. USA 101 (2004) 523-528
12. Davis-Searles P.R., Saunders A.J., Erie D.A., Winzor D.J., and Pielak G.J. Interpreting the effects of small uncharged solutes on protein-folding equilibria. Annu. Rev. Biophys. Biomol. Struct. 30 (2001) 271-306
13. Ellis R.J., and Minton A.P. Cell biology: join the crowd. Nature 425 (2003) 27-28
14. Hartl F.U., and Hayer-Hartl M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295 (2002) 1852-1858
15. Naylor D.J., and Hartl F.U. Contribution of molecular chaperones to protein folding in the cytoplasm of prokaryotic and eukaryotic cells. Biochem. Soc. Symp. (2001) 45-68
16. Prakash S., and Matouschek A. Protein unfolding in the cell. Trends Biochem. Sci. 29 (2004) 593-600
17. Cheung M.S., Klimov D., and Thirumalai D. Molecular crowding enhances native state stability and refolding rates of globular proteins. Proc. Natl Acad. Sci. USA 102 (2005) 4753-4758
18. Ellis R.J. Macromolecular crowding: an important but neglected aspect of the intracellular environment. Curr. Opin. Struct. Biol. 11 (2001) 114-119
19. Ellis R.J. Macromolecular crowding: obvious but underappreciated. Trends Biochem. Sci. 26 (2001) 597-604
20. Minton A.P. Implications of macromolecular crowding for protein assembly. Curr. Opin. Struct. Biol. 10 (2000) 34-39
21. Zimmerman S.B., and Minton A.P. Macromolecular crowding: biochemical, biophysical, and physiological consequences. Annu. Rev. Biophys. Biomol. Struct. 22 (1993) 27-65
22. Waldo G.S., Standish B.M., Berendzen J., and Terwilliger T.C. Rapid protein-folding assay using green fluorescent protein. Nature Biotechnol. 17 (1999) 691-695
23. Wang H., and Chong S. Visualization of coupled protein folding and binding in bacteria and purification of the heterodimeric complex. Proc. Natl Acad. Sci. USA 100 (2003) 478-483
24. Vousden K.H., and Lu X. Live or let die: the cell's response to p53. Nature Rev. Cancer 2 (2002) 594-604
25. Dawson R., Muller L., Dehner A., Klein C., Kessler H., and Buchner J. The N-terminal domain of p53 is natively unfolded. J. Mol. Biol. 332 (2003) 1131-1141
26. Cho Y., Gorina S., Jeffrey P.D., and Pavletich N.P. Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations. Science 265 (1994) 346-355
27. Jeffrey P.D., Gorina S., and Pavletich N.P. Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms. Science 267 (1995) 1498-1502
28. Bell S., Klein C., Muller L., Hansen S., and Buchner J. p53 contains large unstructured regions in its native state. J. Mol. Biol. 322 (2002) 917-927
29. Joerger A.C., and Fersht A.R. Structure-function-rescue: the diverse nature of common p53 cancer mutants. Oncogene 26 (2007) 2226-2242
30. Roemer L., Klein C., Dehner A., Kessler H., and Buchner J. p53 - a natural cancer killer: structural insights and therapeutic concepts. Angew Chem. Int. Ed. Engl. 45 (2006) 6440-6460
31. Ang H.C., Joerger A.C., Mayer S., and Fersht A.R. Effects of common cancer mutations on stability and DNA binding of full-length p53 compared with isolated core domains. J. Biol. Chem. 281 (2006) 21934-21941
32. Bullock A.N., Henckel J., DeDecker B.S., Johnson C.M., Nikolova P.V., Proctor M.R., et al. Thermodynamic stability of wild-type and mutant p53 core domain. Proc. Natl Acad. Sci. USA 94 (1997) 14338-14342
33. Olivier M., Eeles R., Hollstein M., Khan M.A., Harris C.C., and Hainaut P. The IARC TP53 database: new online mutation analysis and recommendations to users. Hum. Mutat. 19 (2002) 607-614
34. Bullock A.N., Henckel J., and Fersht A.R. Quantitative analysis of residual folding and DNA binding in mutant p53 core domain: definition of mutant states for rescue in cancer therapy. Oncogene 19 (2000) 1245-1256
35. Nikolova P.V., Henckel J., Lane D.P., and Fersht A.R. Semirational design of active tumor suppressor p53 DNA binding domain with enhanced stability. Proc Natl Acad. Sci. USA 95 (1998) 14675-14680
36. Joerger A.C., Allen M.D., and Fersht A.R. Crystal structure of a superstable mutant of human p53 core domain. Insights into the mechanism of rescuing oncogenic mutations. J. Biol. Chem. 279 (2004) 1291-1296
37. Toledo F., and Wahl G.M. Regulating the p53 pathway: in vitro hypotheses, in vivo veritas. Nature Rev. Cancer 6 (2006) 909-923
38. Brooks C.L., and Gu W. p53 ubiquitination: Mdm2 and beyond. Mol. Cell 21 (2006) 307-315
39. Bond G.L., Hu W., and Levine A.J. MDM2 is a central node in the p53 pathway: 12 years and counting. Curr. Cancer Drug Targets 5 (2005) 3-8
40. Joerger A.C., Ang H.C., Veprintsev D.B., Blair C.M., and Fersht A.R. Structures of p53 cancer mutants and mechanism of rescue by second-site suppressor mutations. J. Biol. Chem. 280 (2005) 16030-16037
41. Nagy A., Malnasi-Csizmadia A., Somogyi B., and Lorinczy D. Thermal stability of chemically denatured green fluorescent protein (GFP)- A preliminary study. Thermochim. Acta 410 (2004) 161-163
42. Zimmer M. Green fluorescent protein (GFP): applications, structure, and related photophysical behavior. Chem. Rev. 102 (2002) 759-781
43. Friedler A., Veprintsev D.B., Hansson L.O., and Fersht A.R. Kinetic instability of p53 core domain mutants: implications for rescue by small molecules. J. Biol. Chem. 278 (2003) 24108-24112
44. Miroux B., and 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