Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm.

By Paul H. Bessette, F. Åslund, J. Beckwith, George R. Georgiou. 1999

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Citations in the corpus

Pre-expression of a sulfhydryl oxidase significantly increases the yields of eukaryotic disulfide bond containing proteins expressed in the cytoplasm of E.coli (2011, background): “coli are based on the disruption of the thioredoxin/thioredoxin reductase and glutathione/glutathione reductase pathways present in this cytoplasm [4-11].”
Recombinant protein expression in Escherichia coli: advances and challenges (2014, methodology): “We described earlier the OrigamiTM strain, as having a trxB− gor− genotype in the K-12 background (as this double mutant is not viable, a suppressor mutation in the ahpC gene is necessary to maintain viability; Bessette et al., 1999).”
Production of recombinant proteins in Escherichia coli (2004, unknown): “This strain called Origami contains four mutations: knock-outs of the genes coding for thioredoxin and glutathione reductase, a third allows cytoplasmic expression of the DsbC isomerase and the fourth is within a so far uncharacterized suppressor gene allowing improved growth of this strain (Bessett”
Disruption of reducing pathways is not essential for efficient disulfide bond formation in the cytoplasm of E. coli (2010, background): “coli are based on the disruption of one, or more usually both, of the reducing pathways normally present in this compartment [5-8], with a concomitant mutation in aphC [9-11] which restores growth rates in rich media.”
Advanced genetic strategies for recombinant protein expression in Escherichia coli. (2005, background): “ThetrxB (Noagen AD494) andtrxB/gor (Novagen Origami) neg tive strains ofE. coli have been selected in seve xpression situations (Bessette et al., 1999; Lehma t al., 2003; Premkumar et al., 2003).”
Properties, Potentials, and Prospects of Antifreeze Proteins (2008, background): “Bessette et al. (1999) showed that an even higher yield of oxidized disulfide-bonded proteins could be obtained in the cytoplasm of double mutant E. coli for GOR (glutathione oxidoreductase) and Trx (thioredoxin).”
Recombinant protein folding and misfolding in Escherichia coli (2004, background): “, suppressor strains exhibiting good growth characteristics were isolated and shown to be suitable for enhancing disulfide bond formation in heterologous protein”
Overview of bacterial expression systems for heterologous protein production: from molecular and biochemical fundamentals to commercial systems (2006, background): “Alternatively, proteins with disulfide bonds can be overexpressed in the cytoplasm by thioreductase-deficient (trxB) and glutathione reductase (gor) deficient strains (Bessette et al. 1999; Ritz et al. 2001; see Table 1).”
Production of recombinant proteins by high cell density culture of Escherichia coli (2006, background): “These include the co-expression of molecular chaperones (Bessette et al., 1999; Wall and Pluckthun, 1995), the use of thioredoxin-deficient host strains to maintain a favorable redox potential (Derman et al., 1993; Proba et al., 1995), the reduction of protein synthesis rate (Bowden and Georgiou,…”