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Schlagwörter:
Allostery; Chaperonin; Protein folding; Thermosome; Atpase.; Group-ii chaperonin; In-vitro; Thermoplasma-acidophilum; Crystal-structure; Functional-characterization; Acidothermophilic archaeon; Homooligomeric complexes; Sulfolobus-solfataricus; Escherichia-coli; Alpha-chaperonin.; Molecular Biology & Genetics in Current Contents(R)/Life Sciences.
Zusammenfassung:
Recent structural data imply differences in allosteric behavior of the group I chaperonins, typified by GroEL from Escherichia coli, and the group II chaperonins, which comprise archaeal thermosome and eukaryotic TRiC/CCT. Therefore, this study addresses the mechanism of interaction of adenine nucleotides with recombinant alpha-only and native alpha beta-thermosomes from Thermoplasma acidophilum acidophilum, which also enables us to analyze the role of the heterooligomeric composition of the natural thermosome. Although all subunits of the alpha-only thermosome seem to bind nucleotides tightly and independently, the native chaperonin has two different classes of ATP-binding sites. Furthermore, for the alpha-only thermosome, the steady-state ATPase rate is determined by the cleavage reaction itself, whereas, for the alpha beta-thermosome, the rate-limiting step is associated with a post-hydrolysis isomerisation into a non-covalent ADP*P-i species prior to the release of the gamma-phosphate group. After half-saturation with ATP, a negative cooperativity in hydrolysis is observed for both thermosomes. The effect of Mg2+ and K+ nucleotide cycling is documented. We conclude that archaeal chaperonins have unique allosteric properties and discuss them in the light of the mechanism established for the group I chaperonins. (C) 2000 Academic Press. [References: 52]
