Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins
By E. Stewart, F. Åslund, J. Beckwith. 1998
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- V. D. Nguyen
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- Eveliina Enlund
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].”
- Selenoproteins: molecular pathways and physiological roles. (2014, background): “Therefore, Trx and Grx systems have partially overlapping functions under conditions when one of the systems is disrupted, and it has been demonstrated that these reductive pathways can partially compensate for each other in bacteria (326, 360).”
- Recombinant protein expression in Escherichia coli: advances and challenges (2014, background): “The cytoplasm has a more negative redox potential and is maintained as a reducing environment by the thioredoxin–thioredoxin reductase (trxB) system and the glutaredoxin–glutaredoxin reductase (gor) system (Stewart et al., 1998).”
- Disruption of reducing pathways is not essential for efficient disulfide bond formation in the cytoplasm of E. coli (2010, background): “While Δgor ΔtrxB strains lack the reducing pathways and hence allow thioredoxins to transfer oxidizing equivalents from other metabolic pathways to folding proteins [7], there is no dedicated source or catalyst for disulfide bond formation.”
- Advanced genetic strategies for recombinant protein expression in Escherichia coli. (2005, background): “Folding and disul de bond formation in the target protein is enhan y fusion to thioredoxin in strains lacking thioredo eductase (trxB) (Stewart et al., 1998).”
- Glutaredoxins: Glutathione-Dependent Redox Enzymes with Functions Far Beyond a Simple Thioredoxin Backup System (2004, unknown): “When Grx1 was overexpressed to levels similar Trx1, Grx1 was able to rescue the growth defects of a trxAmetE null mutant, and could reduce methionine sulfoxide reductase (105).”