Expression of yeast cyclophilin A (Cpr1) provides improved stress tolerance in Escherichia coli.
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.
Kim
Il-Sup
IS
Department of Biology, Kyungpook National University, Daegu 702-701, Korea.
Shin
Sun-Young
SY
Kim
Young-Saeng
YS
Kim
Hyun-Young
HY
Lee
Dong Hee
DH
Park
Kyung Moc
KM
Yoon
Ho-Sung
HS
Jin
Ingnyol
I
D021984:Cyclophilin A / Q000235:genetics* / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000502:physiology*; D015870:Gene Expression; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism*; D013312:Stress, Physiological
D029701:Saccharomyces cerevisiae Proteins; D021984:Cyclophilin A