A novel ATP/ADP hydrolysis activity of hyperthermostable group II chaperonin in the presence of cobalt or manganese ion.
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.
Hongo
Kunihiro
K
Department of Biotechnology, Faculty of Engineering, Tottori University, Tottori 680-8552, Japan.
Hirai
Hidenori
H
Uemura
Chisato
C
Ono
Shujiro
S
Tsunemi
Junjiro
J
Higurashi
Takashi
T
Mizobata
Tomohiro
T
Kawata
Yasushi
Y
D000251:Adenosine Triphosphatases / Q000235:genetics / Q000378:metabolism*; D019843:Archaeal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D018833:Chaperonins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D003001:Cloning, Molecular; D003035:Cobalt / Q000378:metabolism* / Q000494:pharmacology; D006358:Hot Temperature; D008291:Malate Dehydrogenase / Q000737:chemistry; D008345:Manganese / Q000378:metabolism* / Q000494:pharmacology; D017510:Protein Folding; D019711:Pyrococcus / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics
D019843:Archaeal Proteins; D003035:Cobalt; D008345:Manganese; D008291:Malate Dehydrogenase; D000251:Adenosine Triphosphatases; D018833:Chaperonins