Burns R G, Surridge C D
Biophysics Section, Blackett Laboratory, Imperial College of Science, Technology and Medicine, London, UK.
FEBS Lett. 1994 Jun 27;347(2-3):105-111. doi: 10.1016/0014-5793(94)00522-2.
The TRiC (TCP1 Ring Complex) chaperonin complex participates in the functional folding of actin, centractin, alpha-, beta-, gamma-tubulin, and phytochrome. Each of the cytoskeletal proteins contain a peptide, RK(A,C,T)F/KRAF, located towards the C-terminus, which is homologous to a TCP1 alpha peptide, while the equivalent phytochrome peptide (RLKAF in certain isoforms) is very similar to the KLRAF peptide of TCP1 alpha. We propose that this TCP1 alpha peptide binds to the nascent polypeptides as they emerge from the ribosome, that this binding restricts the folding pathway, and that the TCP1 alpha peptide is subsequently displaced by the synthesis of the consensus peptide. This hypothesis is strongly supported by the crystallographic structure of actin.
TRiC（TCP1环复合物）伴侣蛋白复合物参与肌动蛋白、中心肌动蛋白、α-、β-、γ-微管蛋白和光敏色素的功能折叠。每种细胞骨架蛋白都含有一个位于C末端的肽段RK(A,C,T)F/KRAF，它与TCP1α肽同源，而等效的光敏色素肽段（某些异构体中的RLKAF）与TCP1α的KLRAF肽段非常相似。我们提出，这种TCP1α肽段在新生多肽从核糖体中出现时与其结合，这种结合限制了折叠途径，随后TCP1α肽段被共有肽段的合成所取代。肌动蛋白的晶体结构有力地支持了这一假说。
