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首页> 外文期刊>Molecular and Cellular Biology >Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates.
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Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates.

机译：肌动蛋白和微管蛋白的促进折叠通过细胞质伴侣蛋白和独特的折叠中间体之间的核苷酸依赖性相互作用而发生。

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In the cytoplasm of eukaryotes, the folding of actins and tubulins is facilitated via interaction with a heteromeric toroidal complex (cytoplasmic chaperonin). The folding reaction consists of the formation of a binary complex between the unfolded target protein and the chaperonin, followed by the ultimate release of the native polypeptide in an ATP-dependent reaction. Here we show that the mitochondrial chaperonin (cpn60) and the cytoplasmic chaperonin both recognize a range of target proteins with different relative affinities; however, the cytoplasmic chaperonin shows the highest affinity for intermediates derived from unfolded tubulins and actins. These high-affinity actin and tubulin folding intermediates are distinct from the "molten globule" intermediates formed by noncytoskeletal target proteins in that they form relatively slowly. We show that the interaction between cytoplasmic chaperonin and unfolded target proteins depends on the chaperonin being in its ADP-bound state and that the release of the target protein occurs after a transition of the chaperonin to the ATP-bound state. Our data suggest a model in which ATP hydrolysis acts as a switch between conformational forms of the cytoplasmic chaperonin that interact either strongly or weakly with unfolded substrates.
机译：在真核生物的细胞质中，肌动蛋白和微管蛋白的折叠通过与异聚体环状复合物（细胞质伴侣蛋白）的相互作用而促进。折叠反应包括在未折叠的靶蛋白和伴侣蛋白之间形成二元复合物，然后在依赖ATP的反应中最终释放天然多肽。在这里，我们显示线粒体伴侣蛋白（cpn60）和细胞质伴侣蛋白都可以识别具有不同相对亲和力的一系列靶蛋白。然而，细胞质伴侣蛋白对衍生自未折叠微管蛋白和肌动蛋白的中间体显示出最高的亲和力。这些高亲和力肌动蛋白和微管蛋白折叠中间体不同于非细胞骨架靶蛋白形成的“熔融小球”中间体，因为它们形成的速度相对较慢。我们表明，细胞质伴侣蛋白和未折叠的靶蛋白之间的相互作用取决于伴侣蛋白处于其ADP结合状态，并且在伴侣蛋白转变为ATP结合状态后发生靶蛋白的释放。我们的数据提出了一个模型，其中ATP水解充当细胞质伴侣蛋白的构象形式之间的转换，该构象形式与未折叠的底物发生强弱相互作用。

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