Over-expression and characterization of recombinant prefoldin from hyperthermophilic archaeum Pyrococcus furiosus in E. coli.
Prefoldin is a hexameric chaperone that has been identified in eukaryotic cells and in Archaea. E. coli cells over-expressing the prefoldin gene from the hyperthermophilic, archaeum, Pyrococcus furiosus, grew well at 48 degrees C while control cells were unable to grow above 46 degrees C. The isolated and purified Pfu-prefoldin (specially the beta subunit and the prefoldin) thermally protected the activity of lysozyme.
Chen
Hui
H
East China University of Science and Technology, Shanghai, China.
Yang
Lida
L
Zhang
Yi
Y
Yang
Shengli
S
D000222:Adaptation, Physiological; D003001:Cloning, Molecular; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000254:growth & development / Q000378:metabolism*; D050296:Microbial Viability; D018832:Molecular Chaperones / Q000302:isolation & purification / Q000378:metabolism*; D009113:Muramidase; D055550:Protein Stability; D020027:Pyrococcus furiosus / Q000737:chemistry*; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism*; D013696:Temperature; D014170:Transformation, Genetic
D018832:Molecular Chaperones; D011994:Recombinant Proteins; C112806:prefoldin; D009113:Muramidase