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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Cytosolic chaperonin protects folding intermediates of Gβ from aggregation by recognizing hydrophobic β-strands
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Cytosolic chaperonin protects folding intermediates of Gβ from aggregation by recognizing hydrophobic β-strands

机译：胞质伴侣蛋白通过识别疏水性β链保护Gβ折叠中间体免受聚集

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摘要

Cytosolic chaperonin containing t-complex polypeptide 1 (CCT)/ TRiC is a group Ⅱ chaperonin that assists in the folding of newly synthesized proteins. It is a eukaryotic homologue of the bacterial group Ⅰ chaperonin GroEL. In contrast to the well studied functions of GroEL, the substrate recognition mechanism of CCT/TRiC is poorly understood. Here, we established a system for analyzing CCT/TRiC functions by using a reconstituted protein synthesis by using recombinant elements system and show that CCT/TRiC strongly recognizes WD40 proteins particularly at hydrophobic β-strands. Using the G protein β subunit (Gβ), a WD40 protein that is very rich in β-sheets, as a model substrate, we found that CCT/TRiC prevents aggregation and assists in folding of Gβ, whereas GroEL does not. Gβ has a seven-bladed β-propeller structure; each blade is formed from a WD40 repeat sequence encoding four β-strands. Detailed mutational analysis of Gβ indicated that CCT/TRiC, but not GroEL, preferentially recognizes hydrophobic residues aligned on surfaces of β-strands in the second WD40 repeat of Gβ. These findings indicate that one of the CCT/TRiC-specific targets is hydrophobic β-strands, which are highly prone to aggregation.
机译：含有t-复合多肽1（CCT）/ TRiC的胞质伴侣蛋白是Ⅱ类伴侣蛋白，可协助新合成蛋白质的折叠。它是细菌Ⅰ类伴侣蛋白GroEL的真核同源物。与深入研究GroEL的功能相反，对CCT / TRiC的底物识别机制了解得很少。在这里，我们建立了一个通过使用重组元件系​​统通过重组蛋白质合成来分析CCT / TRiC功能的系统，并表明CCT / TRiC特别是在疏水性β链上强烈识别WD40蛋白。使用G蛋白β亚基（Gβ）（一种非常富含β-折叠的WD40蛋白）作为模型底物，我们发现CCT / TRiC阻止了聚集并有助于Gβ折叠，而GroEL却没有。 Gβ具有七叶β螺旋桨结构；每个叶片由编码四个β链的WD40重复序列形成。对Gβ的详细突变分析表明，CCT / TRiC而不是GroEL优先识别Gβ的第二个WD40重复序列中β链表面排列的疏水残基。这些发现表明，CCT / TRiC特异的靶标之一是疏水性β链，极易发生聚集。

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