Faculty of Science

Recombinant Protein Expression in E. coli
Recommended   Reading

General Reviews

1. Lebendiker M., Danieli T., Production of prone-to-aggregate proteins, FEBS Lett. 2014 588(2):236
2. Papaneophytou CP and Kontopidis G., Statistical approaches to maximize recombinant protein expression in Escherichia coli: a general review. Protein Expr purif. 2014 94:22-32
3. Vincentelli R and Romier C., Expression in Escherichia coli: becoming faster and more complex, Curr Opin Struct Biol. 2013 23(3):326-34
4. Gopal GJ, Kumar A., Strategies for the production of recombinant protein in Escherichia coli. Protein J. 2013 32(6):419 (PDF)
5. Chou CP, Engineering cell physiology to enhance recombinant protein production in Escherichia coli Appl Microbiol Biotechnol 2007 76:521–532 (PDF)
6. Saïda F, Uzan M, Odaert B, Bontems F. Expression of highly toxic genes in E. coli: special strategies and genetic tools. Curr Protein Pept Sci. 2006 Feb;7(1):47-56 (PDF).
7. Jana S, Deb JK., Strategies for efficient production of heterologous proteins in Escherichia coli., Appl Microbiol Biotechnol. 2005 Jan 6; [Epub ahead of print]
8. Sorensen HP, Mortensen KK., Advanced genetic strategies for recombinant protein expression in Escherichia coli.J Biotechnol. 2005 Jan 26;115(2):113-28.
9. Sorensen HP, Mortensen KK, Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli.Microb Cell Fact. 2005 Jan 4;4(1):1(PDF)
10. Hoffmann F. & Rinas U., Stress Induced by Recombinant Protein Production in Escherichia coli , Adv Biochem Engin/Biotechnol 2004; 89: 73–92
11. Jonasson P et. al., Genetic design for facilitated production and recovery of recombinant proteins in Escherichia coli. : Biotechnol Appl Biochem 2002 ;35(Pt 2):91-105 (PDF)
12. Swartz J.R., Advances in Escherichia coli production of therapeutic proteins. Curr Opin Biotechnol 2001 ;12(2):195-201 (PDF)
13. Cornelis P., Expressing genes in different Escherichia coli compartments. Curr Opin Biotechnol 2000 ;11(5):450-4 (PDF)
14. Baneyx F., Recombinant protein expression in Escherichia coli. Curr Opin Biotechnol1999 ;10(5):411-21(PDF)
15. Hannig G & Makrides SC, Strategies for optimizing heterologous protein expression in Escherichia coli. Trends in Biotechnol. 1998; 16:54-60 (PDF)
16. Murby M, Uhlen M, Stahl S. Upstream strategies to minimize proteolytic degradation upon recombinant production in Escherichia coli. Protein Expr Purif. 1996 Mar;7(2):129-36. (PDF)

1. Ramón A, Señorale-Pose M, Marín M, Inclusion bodies: not that bad. Front Microbiol. 2014 (5) Article 56.
2. Yamaguchi S et. al., Protein refolding using chemical refolding additives. Biotechnol J. 2013 Jan;8(1):17-31.
3. Berkmen M, Production of disulfide-bonded proteins in Escherichia coli. Protein Expr Purif. 2012 Mar;82(1):240-51
4. Qoronfleh MW, Hesterberg LK, Seefeldt MB. Confronting high-throughput protein refolding using high pressure and solution screens. Protein Expr Purif.2007 Jun 2; [Epub ahead of print](PDF)
5. Singh SM, Panda AK., Solubilization and refolding of bacterial inclusion body proteins. J Biosci Bioeng. 2005 Apr;99(4):303-10.(PDF)
6. De Marco A, Vigh L, Diamant S, Goloubinoff P. Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones. Cell Stress Chaperones. 2005, 10(4):329-39
7. Hoffmann F.  Rinas U., Roles of Heat-Shock Chaperones in the Production of Recombinant Proteins in Escherichia coli, Adv Biochem Engin/Biotechnol 2004; 89: 143–161
8. Fahnert B., Lilie H  Neubauer P., Inclusion Bodies: Formation and Utilisation, Adv Biochem Engin/Biotechnol2004; 89: 93–142
9. Baneyx F, Mujacic M., Recombinant protein folding and misfolding in Escherichia coli., Nat Biotechnol. 2004; 22(11):1399-408. (PDF
10. Waldo GS. Genetic screens and directed evolution for protein solubility. Curr Opin Chem Biol. 2003 Feb;7(1):33-8.
11. Imai J, Yashiroda H, Maruya M, Yahara I, Tanaka K. Proteasomes and molecular chaperones: cellular machinery responsible for folding and destruction of unfolded proteins. Cell Cycle. 2003 Nov-Dec;2(6):585-90 (PDF)
12. Walter S. and Buchner J., Molecular chaperones–cellular machines for protein folding. Angew. Chem. Int. Ed. 2002, 41, 1098-1113 (PDF)
13. Clark E.D., Protein refolding for industrial processes. Current Opinion in Biotechnology2001, 12:202–207 (PDF).
14. Ben-Zvi AP, Goloubinoff P. Review: mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones. J Struct Biol. 2001 Aug;135(2):84-93.
15. Diamant S, Eliahu N, Rosenthal D, Goloubinoff P. Chemical chaperones regulate molecular chaperones in vitro and in cells under combined salt and heat stresses. J Biol Chem. 2001 Oct 26;276(43):39586-91.
17. Kurokawa Y, Yanagi H, Yura T. Overproduction of bacterial protein disulfide isomerase (DsbC) and its modulator (DsbD) markedly enhances periplasmic production of human nerve growth factor in Escherichia coli. J Biol Chem. 2001 Apr 27;276(17):14393-9 (PDF)

1. Low KO et. al., Optimisation of signal peptide for recombinant protein secretion in bacterial hosts. Appl Microbiol Biotechnol. 2013 May;97(9):3811-26
2. Reed B and Chen R., Biotechnological applications of bacterial protein secretion: from therapeutics to biofuel production. Res. Microbiol. 2013 164(6):675-682
3. Mergulhão FJ, Summers DK, Monteiro GA. Recombinant protein secretion in Escherichia coli. Biotechnol Adv. 2005 May;23(3):177-202 (PDF)
4. Choi JH, Lee SY. Secretory and extracellular production of recombinant proteins using Escherichia coli.  Appl Microbiol Biotechnol. 2004 Jun;64(5):625-35 (PDF)
5. Cornelis P., Expressing genes in different Escherichia coli compartments. Curr Opin Biotechnol. 2000 Oct;11(5):450-4. (PDF)
6. Thanassi DG, Hultgren SJ., Multiple pathways allow protein secretion across the bacterial outer membrane. Curr Opin Cell Biol 2000 ;12(4):420-30 (PDF)
7. Braun P, Gerritse G, van Dijl JM, Quax WJ., Improving protein secretion by engineering components of the bacterial translocation machinery. Curr Opin Biotechnol 1999 ;10(4):376-81(PDF)

1. Pina AS et. al., Challenges and opportunities in the purification of recombinant taggedproteins. Biotechnol. Adv. 2014 March-April 32(2): 366-381
2. Costa S et. al., Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: the novel Fh8 system. Front Microbiol. 2014 February; 5:63
3. Hwang PM et. al., Targeted expression, purification, and cleavage of fusion proteins from inclusion bodies in Escherichia coli. FEBS Lett. 2014 January 2 588(2):247-252
4. Lebendiker M., Danieli T., Purification of proteins fused to maltose-binding protein Methods Mol Biol, 2011 681:281
5. Zuo X, Li S, Hall J, Mattern MR, Tran H, Shoo J, Tan R, Weiss SR, Butt TR. Enhanced expression and purification of membrane proteins by SUMO fusion in Escherichia coli. J Struct Funct Genomics. 2005;6(2-3):103-11 (PDF)
6. Smyth DR, Mrozkiewicz MK, McGrath WJ, Listwan P, Kobe B. Crystal structures of fusion proteins with large-affinity tags. Protein Sci. 2003 Jul;12(7):1313-22 (PDF)

1. Bill RM, von der Haar T., Hijacked then lost in translation: the plight of the recombinant host cell in membrane proteinstructural biology projects. Curr Opin Struct Biol. 2015 Jun;32:147-55.
2. Columbus L, Post-expression strategies for structural investigations of membrane proteins, Curr Opin Struct Biol. 2015 Jun;32:131-8
3. Wagner S, Bader ML, Drew D, de Gier JW. Rationalizing membrane protein overexpression. Trends Biotechnol. 2006 Aug;24(8):364-71 (PDF)
4. Roosild TP, Greenwald J, Vega M, Castronovo S, Riek R, Choe S., NMR structure of Mistic, a membrane-integrating protein for membrane protein expression.  Science. 2005 ;307(5713):1317-21 (PDF)
5. Dumon-Seignovert L, Cariot G, Vuillard L. The toxicity of recombinant proteins in Escherichia coli: a comparison of overexpression in BL21(DE3), C41(DE3), and C43(DE3) Protein Expr Purif. 2004 Sep;37(1):203-6 (PDF)
6. Miroux B, Walker JE. 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. 1996 Jul 19;260(3):289-98 (PDF)

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entries since October 2003