Association of CCT/TriC with other substrates during biosynthesis (unknown chaperone)

A combination of proteomic and bioinformatics analyses of TRiC substrates has revealed that they have complex topologies that are slow folding and aggregation prone (Yam et al., 2008). These substrates are also enriched in proteins that belong to oligomeric assemblies suggesting that TRiC plays a role in promoting complex assembly (Yam et al., 2008). Two possible mechanisms describing the role of TriC have been suggested (Yam et al., 2008). The processes of TRiC-mediated folding and assembly could be directly coupled, or TRiC could fold monomeric subunits and hold them in an assembly-competent state until they associate with the appropriate partner subunits. The complete list of TriC subsrates is not yet known. Many of its substrates that are targeted during biosynthesis are conserved between mammals and yeast (Yam et al. 2008).

对 TRiC 底物进行蛋白质组学和生物信息学分析，揭示了其复杂的拓扑结构，这些结构具有缓慢折叠和易于聚集的特性（Yam 等，2008年）。这些底物富含属于寡聚组装的蛋白质，表明 TRiC 在促进复杂组装中发挥着作用（Yam 等，2008年）。已提出了两种描述 TriC 作用的可能机制（Yam 等，2008年）。TRiC 介导的折叠和组装过程可能直接偶联，或者 TriC 可折叠单体亚基并将其保持在组装竞争状态，直至它们与适当的伙伴亚基结合。TriC 底物的完整列表尚不清楚。在其生物合成过程中被靶向的许多底物在哺乳动物和酵母之间保持保守（Yam 等，2008年）。