Expression of yeast cyclophilin A (Cpr1) provides improved stress tolerance in Escherichia coli

J Microbiol Biotechnol. 2010 Jun;20(6):974-7. doi: 10.4014/jmb.0911.11005.

Abstract

Cyclophilins contain the conserved activity of cis-trans peptidyl-prolyl isomerase that is implicated in protein folding and function as molecular chaperones. The yeast cyclophilin A gene (cpr1) was subcloned to the prokaryotic expression vector pKM260. It was found that the expression of Cpr1 drastically increased the cell viability of E. coli BL21 in the presence of abiotic stress conditions, such as cadmium, copper, hydrogen peroxide, heat, and SDS. Thus, this study illustrates the importance of Cpr1 as a molecular chaperone that improved cellular stress responses when E. coli cells were exposed to adverse conditions, and it also shows the possibility of increasing the stability of E. coli strains utilized for the production of recombinant proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cyclophilin A / genetics*
  • Cyclophilin A / metabolism
  • Escherichia coli / genetics
  • Escherichia coli / physiology*
  • Gene Expression*
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Stress, Physiological

Substances

  • Saccharomyces cerevisiae Proteins
  • Cyclophilin A