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Literature summary for 5.6.1.7 extracted from

  • Sahlan, M.; Kanzaki, T.; Yohda, M.
    Construction and characterization of the hetero-oligomer of the group II chaperonin from the hyperthermophilic archaeon, Thermococcus sp. strain KS-1 (2009), Extremophiles, 13, 437-445.
    View publication on PubMed
Search for more literature for 5.6.1.7

Organism

Organism UniProt Comment Textmining
Thermococcus sp. O24730 Cpnbeta
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Thermococcus sp. JCM 11816 P61112 Cpnalpha
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Thermococcus sp. KS-1 O24730 Cpnbeta
-

Purification (Commentary)

Purification (Comment) Organism
chaperonin complexes Thermococcus sp. JCM 11816
chaperonin complexes Thermococcus sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + a folded polypeptide the chaperonin heterooligomer Cpnab (containing both alpha and beta in the alternate order) protects citrate synthase from thermal aggregation, promotes the folding of acid-denatured Green fluorescence protein in an ATP-dependent manner, and exhibits an ATP-dependent conformational change Thermococcus sp. JCM 11816 ADP + phosphate + an unfolded polypeptide
-
 ?
ATP + H2O + a folded polypeptide the chaperonin heterooligomer Cpnab (containing both alpha and beta in the alternate order) protects citrate synthase from thermal aggregation, promotes the folding of acid-denatured Green fluorescence protein in an ATP-dependent manner, and exhibits an ATP-dependent conformational change Thermococcus sp. ADP + phosphate + an unfolded polypeptide
-
 ?
ATP + H2O + a folded polypeptide the chaperonin heterooligomer Cpnab (containing both alpha and beta in the alternate order) protects citrate synthase from thermal aggregation, promotes the folding of acid-denatured Green fluorescence protein in an ATP-dependent manner, and exhibits an ATP-dependent conformational change Thermococcus sp. KS-1 ADP + phosphate + an unfolded polypeptide
-
 ?

Subunits

Subunits Comment Organism
oligomer Thermococcus sp. expresses two different chaperonin subunits, alpha and beta, for the folding of its proteins. The composition of the subunits in the hexadecameric double ring changes with temperature. The content of the beta subunit significantly increases according to the increase in temperature. The homo-oligomer of the beta subunit, Cpnbeta, is more thermostable than that of the alpha subunit, Cpnalpha. Cpnalpha and Cpnbeta also have different protein folding activities and interactions with prefoldin. The alpha and beta subunits form hetero-oligomers of varying compositions when they are expressed simultaneously. Characterization of the Thermococcus KS-1 chaperonin heterooligomer, Cpnalphabeta, containing both alpha and beta in the alternate order Thermococcus sp. JCM 11816
oligomer Thermococcus sp. expresses two different chaperonin subunits, alpha and beta, for the folding of its proteins. The composition of the subunits in the hexadecameric double ring changes with temperature. The content of the beta subunit significantly increases according to the increase in temperature. The homo-oligomer of the beta subunit, Cpnbeta, is more thermostable than that of the alpha subunit, Cpnalpha. Cpnalpha and Cpnbeta also have different protein folding activities and interactions with prefoldin. The alpha and beta subunits form hetero-oligomers of varying compositions when they are expressed simultaneously. Characterization of the Thermococcus KS-1 chaperonin heterooligomer, Cpnalphabeta, containing both alpha and beta in the alternate order Thermococcus sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
80
-
 CPNalpha and Cpnalphabeta Thermococcus sp. JCM 11816

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
70 90 70°C: about 55% of maximal activity (CPnalpha), about 60% of maximal activity (CPNalphabeta) Thermococcus sp. JCM 11816

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
90
-
 half-life of ATPase activity of Cpnalpha: 9.6 min, half-life of ATPase activity of Cpnalphabeta: 6 min Thermococcus sp. JCM 11816
90
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 t1/2 of ATPase activity of Cpnbeta: 24.8 min Thermococcus sp.
95
-
 the oligomer of Cpnalphabeta is dissociated completely after 15 min incubation Thermococcus sp.
95
-
 the oligomers of Cpnalpha and Cpnalphabeta are dissociated completely after 15 min incubation Thermococcus sp. JCM 11816