Characterization of ATPase activity of class II chaperonin from the hyperthermophilic archaeon Pyrococcus furiosus.
To understand how molecular damage under harsh environmental conditions can be controlled, we investigated the properties of ATPase activity of the chaperonin molecular machinery from the hyperthermophilic archaeon Pyrococcus furiosus (PfCPN). PfCPN ATPase activity depended on K(+) and Mg(2+) and its optimal pH was 7.5. PfCPN had almost no ADPase activity. ADP strongly competitively inhibited PfCPN ATPase activity. Inhibition of PfCPN ATPase decreased its chaperonin activity in protecting lysozyme from heat-induced inactivation.
Chen
Hua-you
HY
Institute for Biological Sciences, Jiangsu University, Zhenjiang, Jiangsu, 212013, China. hyc@ujs.edu.cn
Tan
Xiao-li
XL
Lu
Jian
J
Zhang
Chun-xia
CX
Zhang
Yi
Y
Yang
Sheng-li
SL
D000244:Adenosine Diphosphate / Q000494:pharmacology; D000249:Adenosine Monophosphate / Q000494:pharmacology; D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D019843:Archaeal Proteins / Q000378:metabolism*; D002413:Cations, Divalent / Q000494:pharmacology; D002414:Cations, Monovalent / Q000494:pharmacology; D018833:Chaperonins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration / Q000187:drug effects; D008274:Magnesium / Q000494:pharmacology; D011188:Potassium / Q000494:pharmacology; D020027:Pyrococcus furiosus / Q000187:drug effects / Q000201:enzymology*; D013379:Substrate Specificity / Q000187:drug effects; D013696:Temperature
D019843:Archaeal Proteins; D002413:Cations, Divalent; D002414:Cations, Monovalent; D000249:Adenosine Monophosphate; D000244:Adenosine Diphosphate; D000251:Adenosine Triphosphatases; D018833:Chaperonins; D008274:Magnesium; D011188:Potassium