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Protein Science (2001), 10:445-449.
Copyright © 2001 The Protein Society

FOR THE RECORD

Nested allosteric interactions in the cytoplasmic chaperonin containing TCP-1

Galit Kafri1, Keith R. Willison2 and Amnon Horovitz1

1 Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel
2 Institute of Cancer Research, Chester Beatty Laboratories, London SW3 6JB, United Kingdom

Reprint requests to: Amnon Horovitz, Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel; e-mail: Amnon.Horovitz{at}weizmann.ac.il; fax: 972-8-9344188.

Initial rates of ATP hydrolysis by the chaperonin containing TCP-1 (CCT) from bovine testis were measured as a function of ATP concentration. Two allosteric transitions are observed: one at relatively low concentrations of ATP (<100 µM) and the second at higher concentrations of ATP. The data suggest that CCT has positive intra-ring cooperativity and negative inter-ring cooperativity in ATP hydrolysis, with respect to ATP, as previously observed in the case of GroEL. It is shown that the relatively weak positive intra-ring cooperativity found in the case of CCT may be due to heterogeneity in its subunit composition. Our results suggest that nested allosteric behavior may be common to chaperone double-ring systems.

Keywords: Protein folding; chaperonins; CCT; cooperativity; allostery


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Copyright © 2001 by The Protein Society.