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Recombinant Protein Expression in E. coli
Recommended   Reading


General Reviews
Protein Foldind & Disulfide Bridges
Protein Secretion
Fusion Proteins & Tags
Membrane Proteins

General Reviews

  1. 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)
  2. Swartz J.R., Advances in Escherichia coli production of therapeutic proteins. Curr Opin Biotechnol 2001 ;12(2):195-201 (PDF)
  3. Baneyx F., Recombinant protein expression in Escherichia coli. Curr Opin Biotechnol1999 ;10(5):411-21(PDF)
  4. Hannig G & Makrides SC, Strategies for optimizing heterologous protein expression in Escherichia coli. Trends in Biotechnol. 1998; 16:54-60 (PDF)
  5. Cornelis P., Expressing genes in different Escherichia coli compartments. Curr Opin Biotechnol 2000 ;11(5):450-4 (PDF)
  6. 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)
  7. Hoffmann F. & Rinas U., Stress Induced by Recombinant Protein Production in Escherichia coli , Adv Biochem Engin/Biotechnol 2004; 89: 73–92
  8. Jana S, Deb JK., Strategies for efficient production of heterologous proteins in Escherichia coli., Appl Microbiol Biotechnol. 2005 Jan 6; [Epub ahead of print]
  9. Sorensen HP, Mortensen KK., Advanced genetic strategies for recombinant protein expression in Escherichia coli.J Biotechnol. 2005 Jan 26;115(2):113-28.
  10. 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)
  11. Saïda F, Uzan M, Odaert B, Bontems F. Expression of highly toxic genes in E. coli: special strategies and genetic toolsCurr Protein Pept Sci.2006 Feb;7(1):47-56 (PDF).
  12. Chou CP, Engineering cell physiology to enhance recombinant protein production in Escherichia coli Appl Microbiol Biotechnol 2007 76:521–532 (PDF)
Protein Folding & Disulfide Bridges
  1. Clark E.D., Protein refolding for industrial processes. Current Opinion in Biotechnology2001, 12:202–207 (PDF).
  2. Walter S. and Buchner J., Molecular chaperones–cellular machines for protein folding. Angew. Chem. Int. Ed. 2002, 41, 1098-1113 (PDF)
  3. 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.
  4. 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.
  5. 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
  6. 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)
  7. Waldo GS. Genetic screens and directed evolution for protein solubility. Curr Opin Chem Biol. 2003 Feb;7(1):33-8.
  8. 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)
  9. 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
  10. Fahnert B., Lilie H  Neubauer P., Inclusion Bodies: Formation and Utilisation, Adv Biochem Engin/Biotechnol2004; 89: 93–142
  11. Baneyx F, Mujacic M., Recombinant protein folding and misfolding in Escherichia coli., Nat Biotechnol. 2004; 22(11):1399-408. (PDF)
  12. Singh SM, Panda AK., Solubilization and refolding of bacterial inclusion body proteinsJ Biosci Bioeng. 2005 Apr;99(4):303-10.(PDF)
  13. Qoronfleh MW, Hesterberg LK, Seefeldt MB. Confronting high-throughput protein refolding using high pressure and solution screensProtein Expr Purif.2007 Jun 2; [Epub ahead of print](PDF)
Protein Secretion
  1. Cornelis P., Expressing genes in different Escherichia coli compartments. Curr Opin Biotechnol. 2000 Oct;11(5):450-4. (PDF)
  2. Thanassi DG, Hultgren SJ., Multiple pathways allow protein secretion across the bacterial outer membrane. Curr Opin Cell Biol 2000 ;12(4):420-30 (PDF)
  3. 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)
  4. Choi JH, Lee SY. Secretory and extracellular production of recombinant proteins using Escherichia coliAppl Microbiol Biotechnol. 2004 Jun;64(5):625-35 (PDF)
  5. Mergulhão FJ, Summers DK, Monteiro GA. Recombinant protein secretion in Escherichia coli. Biotechnol Adv. 2005 May;23(3):177-202 (PDF)
Fusion Proteins & Tags
  1. 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)
  2. 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)
Membrane Proteins
  1. Wagner S, Bader ML, Drew D, de Gier JW. Rationalizing membrane protein overexpression. Trends Biotechnol. 2006 Aug;24(8):364-71 (PDF)
  2. Roosild TP, Greenwald J, Vega M, Castronovo S, Riek R, Choe S., NMR structure of Mistic, a membrane-integrating protein for membrane protein expressionScience. 2005 ;307(5713):1317-21 (PDF)
  3. 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)
  4. 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)

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entries since October 2003