Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2052202 | FEBS Letters | 2006 | 7 Pages |
Abstract
A novel ATPase activity that was strongly activated in the presence of either cobalt or manganese ion was discovered in the chaperonin from hyperthermophilic Pyrococcus furiosus (Pfu-cpn). Surprisingly, a significant ADPase activity was also detected under the same conditions. A more extensive search revealed similar nucleotide hydrolysis activities in other thermostable chaperonins. Chaperonin activity, i.e., thermal stabilization and refolding of malate dehydrogenase from the guanidine-hydrochloride unfolded state were also detected for Pfu-cpn under the same conditions. We propose that the novel cobalt/manganese-dependent ATP/ADPase activity may be a common trait of various thermostable chaperonins.
Keywords
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Kunihiro Hongo, Hidenori Hirai, Chisato Uemura, Shujiro Ono, Junjiro Tsunemi, Takashi Higurashi, Tomohiro Mizobata, Yasushi Kawata,