Cross-system excision of chaperone-mediated proteolysis in chaperone-assisted recombinant protein production

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Abstract

Main Escherichia coli cytosolic chaperones such as DnaK are key components of the control quality network designed to minimize the prevalence of polypeptides with aberrant conformations. This is achieved by both favoring refolding activities but also stimulating proteolytic degradation of folding reluctant species. This last activity is responsible for the decrease of the proteolytic stability of recombinant proteins when co-produced along with DnaK, where an increase in solubility might be associated to a decrease in protein yield. However, when DnaK and its co-chaperone DnaJ are co-produced in cultured insect cells or whole insect larvae (and expectedly, in other heterologous hosts), only positive, folding-related effects of these chaperones are observed, in absence of proteolysis- mediated reduction of recombinant protein yield. © 2010 Landes Bioscience.
Original languageEnglish
Pages (from-to)148-150
JournalBioengineered Bugs
Volume1
Issue number2
DOIs
Publication statusPublished - 11 Oct 2010

Keywords

  • Cell factories
  • Chaperones
  • E. coli
  • Insect cells
  • Protein folding
  • Protein production

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