Abstract
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 Mg2+ 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.
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Andrä S, Frey G, Jaenicke R et al (1998) The thermosome from Methanopyrus kandleri possesses an NH4 +-dependent ATPase activity. Eur J Biochem 255:93–99
Baykove AA, Evtushewnko OA, Avaeva SM (1988) A Malachite green procedure for orthophosphate determination and its use in alkaline phosphatase-based enzyme immunoassay. Anal Biochem 171:266–270
Chen HY, Chu ZM, Zhang Y et al (2007) Expression and characterization of the chaperonin molecular machine from the hyperthermophilic archaeon Pyrococcus furiosus. J Basic Microbiol 47:132–137
Ellis RJ, van der Vies SM (1991) Molecular chaperones. Annu Rev Biochem 60:321–347
Furutani M, Iida T, Yoshida T et al (1998) Group II chaperonin in a thermophilic methanogen, Methanococcus thermolithotrophicus. Chaperone activity and filament-forming ability. J Biol Chem 273:28399–28407
Goldberg ME, Rudolph R, Jaenicke R et al (1991) A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme. Biochemistry 30:2790–2797
Gutsche I, Essen LO, Baumeister W (1999) Group II chaperonins: New TRic(k)s and turns of a protein folding machine. J Mol Biol 293:295–312
Hartl FU, Martin J, Neupert W (1992) Protein folding in the cell: the role of molecular chaperones hsp 70 and hsp 60. Annu Rev Biophys Biomol Struct 21:293–322
Hongo K, Hirai H, Uemura C et al (2006) A novel ATP/ADP hydrolysis activity of hyperthermostable group II chaperonin in the presence of cobalt or manganese ion. FEBS Lett 580:34–40
Iizuka R, Yoshida T, Maruyama T et al (2001) Glycine at the 65th position plays an essential role in ATP-dependent protein folding by archael group II chaperonin. Biochem Biophys Res Commun 289:1118–1124
Kusmierczyk AR, Martin J (2003) Nested cooperativity and salt dependence of the ATPase activity of the archaeal chaperonin Mm-cpn. FEBS Lett 547:201–204
Laksanalamai P, Pavlov AR, Slesarev AI et al (2006) Stabilization of Taq DNA polymerase at high temperature by protein folding pathways from a hyperthermophilic archaeon, Pyrococcus furiosus. Biotechnol Bioeng 93:1–5
Ranson NA, White HE, Saibil HR (1998) Chaperonins. Biochem J 333:233–242
Sigler PB, Xu Z, Rye HS et al (1998) Structure and function in GroEL-mediated protein folding. Annu Rev Biochem 67:581–608
Tanaka T, Izawa K, Okochi M et al (2005) Molecular characterization of the group II chaperonin from the hyperthermophilic archaeum Pyrococcus horikoshii OT3. Extremophiles 9:127–134
Acknowledgements
This work is supported by Open Funding Project of the State Key Laboratory of Bioreactor Engineering (Grant No. 2060204), by the National Basic Research Program of China (2004CB719606) and by the Research Program of Jiangsu University (08jdg011).
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Chen, Hy., Tan, Xl., Lu, J. et al. Characterization of ATPase activity of class II chaperonin from the hyperthermophilic archaeon Pyrococcus furiosus . Biotechnol Lett 31, 1753–1758 (2009). https://doi.org/10.1007/s10529-009-0070-x
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DOI: https://doi.org/10.1007/s10529-009-0070-x