Escherichia coli heterologous expression

A. Galkin, L. Kulakova, T. Yoshimura, K. Soda, N. Esald, Synthesis of optically active amino acids from alpha-keto acids with Escherichia coli cells expressing heterologous genes, Appl. Environ. Microbiol. 63 (1997) 4651-4656. 

Vannelli, T., et al.. Production of p-hydroxycinnamic acid from glucose in Saccharomyces cerevisiae and Escherichia coli by expression of heterologous genes from plants and fungi. Metab. Eng., 2007. 9(2) 142-151. 

McGovern, A. C. Ernill, R. Kara, B. V. Kell, D. B. Goodacre, R. Rapid analysis of the expression of heterologous proteins in Escherichia coli using pyrolysis mass spectrometry and Fourier transform infrared spectroscopy with chemometrics Application to a2- interferon production. J. Biotechnol. 1999, 72,157-167. 

There is a broad diversity of heterologous hosts for gene expression, and there is no best or universal host which is suitable for the production of all possible proteins. Nevertheless, many proteins can be expressed cheaply and successfully in Escherichia coli, which is still the most preferred host for heterologous production of proteins without posttranslational modifications. 

Roberts, G.A., Staunton, J. and Leadlay, P.F. (1993) Heterologous expression in Escherichia coli of an intact multienzyme component of the erythromycin-producing polyketide synthase. European Journal of Biochemistry, 214, 305. 

A range of symmetrical bicyclic /3-diketones can be converted to 2,3-disubstituted cycloalkanones in high yield with high diastereomeric and enantiomeric excess using a cell-free preparation of a retro-Claisenase enzyme, or /3-diketone hydrolase, the gene for which has been heterologously expressed in Escherichia coli. ... 

Kane, J. E. (1995). Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli. Curr. Opin. Biotechnol. 6,494-500. 

G. Hannig and S. C. Makrides, Strategies for optimizing heterologous protein expression in Escherichia coli, Tiptech 1998, 16, 54-60. 

S. Tokuyama and K. Hatano, Cloning, DNA sequendng and heterologous expression of the gene for thermostable N-acylamino add racemase from Amycolatopsis sp. TS-1-60 in Escherichia coli, Appl. Microbiol. Biotechnol. 1995b, 42, 884-889. 

Table 7.1. Km values for ADP and ATP of several heterologously expressed adenine nucleotide carriers determined on intact Escherichia coli cells under various energy conditions (coupled and uncoupled). Km is given in nanomoles per milligram of protein per hour), E. coli cells were preincubated with 100 pM carbonyl cyanide 3-chlorophenylhydrazone (CCCP) for 2 min for uncoupling. Uptake studies were performed as described in Haferkamp et al. (2002), Tjaden et al. (2004) Leroch (2006), and Leroch et al. (2005)...

The cloning, overexpression, purification and characterization of the exopolyphosphatase (LmPPX) from Protozoa Leishmania major have been reported (Rodrigues et al., 2002a). The gene sequence shows a similarity with PPX1. The product of this gene (LmPPX) has 388 amino acids and a molecular mass of 48 kDa. Heterologous expression of LmPPX in Escherichia coli produced a functional enzyme that was similar to the... 

OBER, D THOLL, D., MARTIN, W., HARTMANN, T Homospermidine synthase of Rhodopseudomonas viridis Substrate specificity and effects of the heterologously expressed enzyme on polyamine metabolism of Escherichia coli. J. Gen. Appl. Microbiol., 1996,42,411-419. 

Intriguingly, the blue copper sites, especiaUy those with a carbonyl oxygen at the axial coordination position, display high affinity for Zn + ions. Mutants in which the Met is replaced by Gin or Glu preferentiaUy bind Zn + when expressed in heterologous systems, e.g., Escherichia coli. Examples include azurin, amicyanin, nitrite reductase, and possibly also plastocyanin (Diederix et al., 2000 Hibino et al., 1995 Murphy et al., 1995 Nar et al., 1992a Romero et al., 1993). In the case of azurin it has been shown that both wild-type and the Met—Gin mutant have the same affinity for both Zn +and Cu + (Romero ci a/., 1993). In addition, EXAFS studies showed that some preparations of blue copper proteins purihed from their natural sources also contain small fractions of Zn derivatives (DeBeer George, personal communication). 

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