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放线菌 CDC48 样蛋白（Cpa）是分枝杆菌和相关生物中一种新型的蛋白酶体相互作用蛋白。

Cdc48-like protein of actinobacteria (Cpa) is a novel proteasome interactor in mycobacteria and related organisms.

机构信息

Institute of Molecular Biology & Biophysics, ETH Zurich, Zurich, Switzerland.

Laboratory of Biomolecular Research, Paul Scherrer Institute, ETH Zurich, Villigen, Switzerland.

出版信息

Elife. 2018 May 29;7:e34055. doi: 10.7554/eLife.34055.

DOI:10.7554/eLife.34055
PMID:29809155
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6017811/
Abstract

Cdc48 is a AAA+ ATPase that plays an essential role for many cellular processes in eukaryotic cells. An archaeal homologue of this highly conserved enzyme was shown to directly interact with the 20S proteasome. Here, we analyze the occurrence and phylogeny of a Cdc48 homologue in and assess its cellular function and possible interaction with the bacterial proteasome. Our data demonstrate that Cdc48-like protein of actinobacteria (Cpa) forms hexameric rings and that the oligomeric state correlates directly with the ATPase activity. Furthermore, we show that the assembled Cpa rings can physically interact with the 20S core particle. Comparison of the wild-type with a knockout strain under carbon starvation uncovers significant changes in the levels of around 500 proteins. Pathway mapping of the observed pattern of changes identifies ribosomal proteins as a particular hotspot, pointing amongst others toward a role of Cpa in ribosome adaptation during starvation.

摘要

Cdc48 是一种 AAA+ ATP 酶，在真核细胞的许多细胞过程中发挥着重要作用。这种高度保守酶的古菌同源物被证明可以直接与 20S 蛋白酶体相互作用。在这里，我们分析了 和 的 Cdc48 同源物的发生和系统发育，并评估了其细胞功能以及与细菌蛋白酶体可能的相互作用。我们的数据表明，放线菌的 Cdc48 样蛋白（Cpa）形成六聚体环，并且寡聚状态与 ATP 酶活性直接相关。此外，我们表明组装的 Cpa 环可以与 20S 核心颗粒进行物理相互作用。在碳饥饿下比较 野生型和 敲除菌株，发现约 500 种蛋白质的水平发生了显著变化。观察到的变化模式的途径映射将核糖体蛋白鉴定为一个特定的热点，除其他外，表明 Cpa 在饥饿期间核糖体适应中起作用。

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