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Related Experiment Videos

Nested allosteric interactions in the cytoplasmic chaperonin containing TCP-1.

G Kafri1, K R Willison, A Horovitz

  • 1Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel.

Protein Science : a Publication of the Protein Society
|March 27, 2001
PubMed
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Chaperonin containing TCP-1 (CCT) exhibits distinct allosteric transitions during ATP hydrolysis, suggesting nested cooperativity in double-ring chaperones.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Folding

Background:

  • Chaperonins are essential molecular machines that assist protein folding.
  • The chaperonin containing TCP-1 (CCT) is a key eukaryotic chaperonin involved in protein folding.
  • Understanding CCT's mechanism, particularly its ATP hydrolysis activity, is crucial for elucidating its function.

Purpose of the Study:

  • To investigate the allosteric behavior of bovine testis CCT during ATP hydrolysis.
  • To determine the cooperativity patterns of ATP hydrolysis in CCT.

Main Methods:

  • Measurement of initial rates of ATP hydrolysis by CCT.
  • Analysis of ATP hydrolysis rates as a function of ATP concentration.

Main Results:

Related Experiment Videos

  • Two distinct allosteric transitions were observed in ATP hydrolysis rates at low (<100 microM) and high ATP concentrations.
  • CCT displays positive intra-ring cooperativity and negative inter-ring cooperativity in ATP hydrolysis.
  • Weak positive intra-ring cooperativity in CCT may stem from subunit heterogeneity.

Conclusions:

  • Nested allosteric behavior is likely a common feature of double-ring chaperone systems like CCT.
  • The observed cooperativity patterns provide insights into the functional mechanism of CCT.