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  ATPase cycle of an archaeal chaperonin

Gutsche, I., Mihalache, O., & Baumeister, W. (2000). ATPase cycle of an archaeal chaperonin. Journal of Molecular Biology, 300(1), 187-196.

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Datensatz-Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-7169-9 Versions-Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-716A-7
Genre: Zeitschriftenartikel
Alternativer Titel : J. Mol. Biol

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 Urheber:
Gutsche, I., Autor
Mihalache, O.1, Autor              
Baumeister, W.1, Autor              
Affiliations:
1External Organizations, escidoc:persistent22              

Inhalt

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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]

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 Datum: 2000
 Publikationsstatus: Im Druck publiziert
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 Ort, Verlag, Ausgabe: -
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 Identifikatoren: eDoc: 318653
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Titel: Journal of Molecular Biology
  Alternativer Titel : J. Mol. Biol
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 300 (1) Artikelnummer: - Start- / Endseite: 187 - 196 Identifikator: -