Related Experiment Video
Updated: Jul 15, 2026

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
Published on: October 23, 2016
Expression and characterization of the chaperonin molecular machine from the hyperthermophilic archaeon Pyrococcus
Hua-You Chen1, Zhong-Mei Chu, Yan-He Ma
1Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China.
Abstract:
The chaperonin molecular machine from hyperthermophilic archaeon Pyrococcus furiosus was studied in this paper. The Pyrococcus furiosus chaperonin gene (PfCPN) was amplified by PCR from the Pyrococcus furiosus genomic DNA, and expressed in Escherichia coli BL21-Codonplus(DE)(3)-RIL. The recombinant PfCPN was purified to homogeneity by using ion-exchange and size-exclusion chromatography. It was found that the ATPase activity of the PfCPN was highest at 88 degrees C, and there existed a nested cooperativity of the ATPase activity of the PfCPN. This result suggested that nested allosteric behavior may be common to chaperonin molecular machines from archaea. The half-life (t(1/2)) of the ATPase activity of the PfCPN at 100 degrees C was about 60 min. The PfCPN displayed chaperone activity in preventing lysozyme from thermal inactivation. This chaperone activity was in an ATP-dependent manner.
Related Concept Videos
Molecular Chaperones and Protein Folding
The...
Molecular Chaperones and Protein Folding
The...
Diversity of Archaea IV
Diversity of Archaea III
Bacterial Protein Maturation
Surface Appendages of Archaea

