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     Several years ago we showed that CCT displays positive intra-ring cooperativity and negative inter-ring cooperativity with respect to ATP (Kafri et al., 2001). Virtually nothing is known about the mechanism of allosteric transitions in CCT and the role of allostery in its function. One attractive hypothesis is that the subunit heterogeneity of CCT facilitates sequential progression of conformational changes around the ring (Rivenzon-Segal et al., 2005) which, in turn, facilitates sequential folding of protein domains (Jacob et al., 2007). We are carrying out kinetic experiments on ATP binding to CCT with the hope of obtaining evidence for (or against) such a model (Kafri and Horovitz, 2003). We are also carrying out genetic and biochemical experiments on CCT from yeast (Shimon et al., 2008).
To this end, we are collaborating with Prof. Keith Willison from Chester Beatty Laboratories, London.