Yield, solubility and conformational quality of soluble proteins are not simultaneously favored in recombinant Escherichia coli

Biotechnology and Bioengineering

Volumn 101, Issue 6, 2008, Pages 1353-1358

  Martínez Alonso, Mónica ^a   García Fruitós, Elena ^a   Villaverde, Antonio ^a  

^a UNIVERSITAT AUTÒNOMA DE BARCELONA   (Spain)

Author keywords

IBs; Protein folding; Protein quality; Solubility

Indexed keywords

ESCHERICHIA COLI; FLUORESCENCE; GENE EXPRESSION; LIGHT EMISSION; LUMINESCENCE; PROTEINS; SOLUBILITY; TERNARY SYSTEMS;

FLUORESCENT PROTEINS; FUNCTIONAL PROTEINS; GREEN FLUORESCENT PROTEINS; HIGH QUALITIES; IBS; INCLUSION BODIES; INDEPENDENT CONTROLS; PROTEIN PRODUCTIONS; PROTEIN QUALITY; PROTEIN YIELDS; RECOMBINANT ESCHERICHIA COLI; RECOMBINANT PROTEINS; SECONDARY STRUCTURES; SOLUBLE PROTEINS;

PROTEIN FOLDING;

GREEN FLUORESCENT PROTEIN; RECOMBINANT PROTEIN;

ARTICLE; ESCHERICHIA COLI; NONHUMAN; PROTEIN CONFORMATION; PROTEIN QUALITY; PROTEIN SYNTHESIS; RECOMBINANT DNA TECHNOLOGY; SOLUBILITY;

ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENE DELETION; GENE EXPRESSION; GREEN FLUORESCENT PROTEINS; HSP70 HEAT-SHOCK PROTEINS; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SOLUBILITY; TEMPERATURE;

ESCHERICHIA COLI;

EID: 56749148173     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.21996     Document Type: Article

References (37)

1. Ami D, Natalello A, Gatti-Lafranconi P, Lotti M, Doglia SM. 2005. Kinetics of inclusion body formation studied in intact cells by FT-IR spectroscopy. FEBS Lett 579:3433-3436.
2. Ami D, Natalello A, Taylor G, Tonon G, Maria DS. 2006. Structural analysis of protein inclusion bodies by Fourier transform infrared microspectroscopy. Biochim Biophys Acta 1764:793-799.
3. Arie JP, Miot M, Sassoon N, Betton JM. 2006. Formation of active inclusion bodies in the periplasm of Escherichia coli. Mol Microbiol 62:427-437.
4. Baneyx F, Mujacic M. 2004. Recombinant protein folding and misfolding in Escherichia coli. Nat Biotechnol 22:1399-1408.
5. Baneyx F, Palumbo JL. 2003. Improving heterologous protein folding via molecular chaperone and foldase co-expression. Methods Mol Biol 205:171-197.
6. Carrio MM, Cubarsi R, Villaverde A. 2000. Fine architecture of bacterial inclusion bodies. FEBS Lett 471:7-11.
7. de Groot NS, Ventura S. 2006. Protein activity in bacterial inclusion bodies correlates with predicted aggregation rates. J Biotechnol 125:110-113.
8. de Marco A, Schroedel A. 2005. Characterization of the aggregates formed during recombinant protein expression in bacteria. BMC Biochem 6:10.
9. de Marco A, Volrath S, Bruyere T, Law M, Fonne-Pfister R. 2000. Recombinant maize protoporphyrinogen IX oxidase expressed in Escherichia coli forms complexes with GroEL and DnaK chaperones. Protein Exp Purif 20:81-86.
10. de Marco A. 2007. Protocol for preparing proteins with improved solubility by co-expressing with molecular chaperones in Escherichia coli. Nat Protoc 2:2632-2639.
11. de Marco A, De Marco V. 2004. Bacteria co-transformed with recombinant proteins and chaperones cloned in independent plasmids are suitable for expression tuning. J Biotechnol 109:45-52.
12. de Marco A, Deuerling E, Mogk A, Tomoyasu T, Bukau B. 2007. Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli. BMC Biotechnol 7:32.
13. Feliu JX, Cubarsi R, Villaverde A. 1998. Optimized release of recombinant proteins by ultrasonication of E. coli cells. Biotechnol Bioeng 58:536-540.
14. Garcia-Fruitos E, Carrio MM, Aris A, Villaverde A. 2005a. Folding of a misfolding-prone beta-galactosidase in absence of DnaK. Biotechnol Bioeng 90:869-875.
15. Garcia-Fruitos E, Gonzalez-Montalban N, Morell M, Vera A, Ferraz RM, Aris A, Ventura S, Villaverde A. 2005b. Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins. Microb Cell Fact 4:27.
16. Garcia-Fruitos E, Martinez-Alonso M, Gonzalez-Montalban N, Valli M, Mattanovich D, Villaverde A. 2007. Divergent genetic control of protein solubility and conformational quality in Escherichia coli. J Mol Biol 374:195-205.
17. Gonzalez-Montalban N, Garcia-Fruitos E, Ventura S, Aris A, Villaverde A. 2006. The chaperone DnaK controls the fractioning of functional protein between soluble and insoluble cell fractions in inclusion body-forming cells. Microb Cell Fact 5:26.
18. Gonzalez-Montalban N, Garcia-Fruitos E, Villaverde A. 2007. Recombinant protein solubility - Does more mean better? Nat Biotechnol 25:718-720.
19. Herberhold H, Marchal S, Lange R, Scheyhing CH, Vogel RF, Winter R. 2003. Characterization of the pressure-induced intermediate and unfolded state of red-shifted green fluorescent protein - a static and kinetic FTIR, UV/VIS and fluorescence spectroscopy study. J Mol Biol 330:1153-1164.
20. Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
21. Lin GZ, Lian YJ, Ryu JH, Sung MK, Park JS, Park HJ, Park BK, Shin JS, Lee MS, Cheon CI. 2007. Expression and purification of His-tagged flavonol synthase of Camellia sinensis from Escherichia coli. Protein Exp Purif 55:287-292.
22. Martinez-Alonso M, Vera A, Villaverde A. 2007. Role of the chaperone DnaK in protein solubility and conformational quality in inclusion body-forming Escherichia coli cells. FEMS Microbiol Lett 273:187-195.
23. Nishihara K, Kanemori M, Kitagawa M, Yanagi H, Yura T. 1998. Chaperone coexpression plasmids: Differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Escherichia coli. Appl Environ Microbiol 64:1694-1699.
24. Oberg K, Chrunyk BA, Wetzel R, Fink AL. 1994. Nativelike secondary structure in interleukin-1 beta inclusion bodies by attenuated total reflectance FTIR. Biochemistry 33:2628-2634.
25. Sambrook J, Fritsch E, Maniatis T. 1989. Molecular Cloning, A Laboratory Manual. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
26. Scheyhing CH, Meersman F, Ehrmann MA, Heremans K, Vogel RF. 2002. Temperature-pressure stability of green fluorescent protein: A Fourier transform infrared spectroscopy study. Biopolymers 65:244-253.
27. Schultz T, Martinez L, de MA, 2006. The evaluation of the factors that cause aggregation during recombinant expression in E. coli is simplified by the employment of an aggregation-sensitive reporter. Microb Cell Fact 5:28.
28. Sorensen HP, Mortensen KK. 2005a. Advanced genetic strategies for recombinant protein expression in Escherichia coli. J Biotechnol 115:113-128.
29. Sorensen HP, Mortensen KK. 2005b. Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli. Microb Cell Fact 4:1.
30. Thomas JG, Baneyx F. 1996. Protein folding in the cytoplasm of Escherichia coli: Requirements for the DnaK-DnaJ-GrpE and GroEL-GroES molecular chaperone machines. Mol Microbiol 21:1185-1196.
31. Tomoyasu T, Mogk A, Langen H, Goloubinoff P, Bukau B. 2001. Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol. Mol Microbiol 40:397-413.
32. Ventura S, Villaverde A. 2006. Protein quality in bacterial inclusion bodies. Trends Biotechnol 24:179-185.
33. Villaverde A, Benito A, Viaplana E, Cubarsi R. 1993. Fine regulation of cI857-controlled gene expression in continuous culture of recombinant Escherichia coli by temperature. Appl Environ Microbiol 59:3485-3487.
34. Villaverde A, Carrio MM. 2003. Protein aggregation in recombinant bacteria: Biological role of inclusion bodies. Biotechnol Lett 25:1385-1395.
35. Wang J, Tan H, Zhao ZK. 2007. Over-expression, purification, and characterization of recombinant NAD-malic enzyme from Escherichia coli K12. Protein Exp Purif 53:97-103.
36. Zhang L, Patel HN, Lappe JW, Wachter RM. 2006. Reaction progress of chromophore biogenesis in green fluorescent protein. J Am Chem Soc 128:4766-4772.
37. Ziemienowicz A, Skowyra D, Zeilstra-Ryalls J, Fayet O, Georgopoulos C, Zylicz M. 1993. Both the Escherichia coli chaperone systems, GroEL/ GroES and DnaK/DnaJ/GrpE, can reactivate heat-treated RNA polymerase. Different mechanisms for the same activity. J Biol Chem 268:25425-25431.