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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Interactions of subunit CCT3 in the yeast chaperonin CCT/TRiC with Q/N-rich proteins revealed by high-throughput microscopy analysis
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Interactions of subunit CCT3 in the yeast chaperonin CCT/TRiC with Q/N-rich proteins revealed by high-throughput microscopy analysis

机译：高通量显微镜分析揭示了酵母伴侣蛋白CCT / TRiC中亚基CCT3与富含Q / N的蛋白质的相互作用

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摘要

The eukaryotic chaperonin containing t-complex polypeptide 1 (CCT/TRiC) is an ATP-fueled machine that assists protein folding. It consists of two back-to-back stacked rings formed by eight different subunits that are arranged in a fixed permutation. The different subunits of CCT are believed to possess unique substrate binding specificities that are still mostly unknown. Here, we used high-throughput microscopy analysis of yeast cells to determine changes in protein levels and localization as a result of a Glu to Asp mutation in the ATP binding site of subunits 3 (CCT3) or 6 (CCT6). The mutation in subunit CCT3 was found to induce cytoplasmic foci termed P-bodies where mRNAs, which are not translated, accumulate and can be degraded. Analysis of the changes in protein levels and structural modeling indicate that P-body formation in cells with the mutation in CCT3 is linked to the specific interaction of this subunit with Gln/Asn-rich segments that are enriched in many P-body proteins. An in vitro gel-shift analysis was used to show that the mutation in subunit CCT3 interferes with the ability of CCT to bind a Gln/Asn-rich protein aggregate. More generally, the strategy used in this work can be used to unravel the substrate specificities of other chaperone systems.
机译：含有t-复合多肽1（CCT / TRiC）的真核伴侣蛋白是辅助蛋白质折叠的ATP辅助机器。它由两个背对背堆叠的环组成，这些环由固定排列的八个不同的子单元组成。据信CCT的不同亚基具有独特的底物结合特异性，但仍几乎未知。在这里，我们使用了酵母细胞的高通量显微镜分析来确定蛋白质水平和定位的变化，这是亚基3（CCT3）或6（CCT6）的ATP结合位点从Glu突变为Asp的结果。发现亚基CCT3中的突变诱导了称为P体的细胞质灶，其中未翻译的mRNA会积累并可以降解。对蛋白质水平变化和结构建模的分析表明，在CCT3中发生突变的细胞中P体形成与该亚基与富含Gln / Asn片段的特异性相互作用有关，后者富含许多P体蛋白。体外凝胶转移分析用于显示CCT3亚基的突变会干扰CCT结合Gln / Asn富蛋白聚集体的能力。更一般而言，这项工作中使用的策略可用于阐明其他分子伴侣系统的底物特异性。

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