Kafri G, Willison K R, Horovitz A
Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel.
Protein Sci. 2001 Feb;10(2):445-9. doi: 10.1110/ps.44401.
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 microM) 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.
测定了来自牛睾丸的含TCP-1伴侣蛋白(CCT)水解ATP的初始速率与ATP浓度的函数关系。观察到两个别构转变:一个发生在相对低浓度的ATP(<100微摩尔)时,另一个发生在较高浓度的ATP时。数据表明,与之前在GroEL中观察到的情况一样,就ATP而言,CCT在ATP水解中具有正向的环内协同性和负向的环间协同性。结果表明,在CCT中发现的相对较弱的正向环内协同性可能是由于其亚基组成的异质性。我们的结果表明,嵌套别构行为可能是伴侣蛋白双环系统共有的。