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首页> 外文期刊>The Biochemical Journal >The two PAN ATPases from Halobacterium display N-terminal heterogeneity and form labile complexes with the 20S proteasome
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The two PAN ATPases from Halobacterium display N-terminal heterogeneity and form labile complexes with the 20S proteasome

机译：嗜盐杆菌中的两个PAN ATPase显示N末端异质性并与20S蛋白酶体形成不稳定的复合物

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摘要

The PAN (proteasome-activating nucleotidase) proteins from archaea represent homologues of the eukaryotic 26S proteasome regulatory ATPases. In vitro the PAN complex has been previously shown to have a stimulatory effect on the peptidase activities of the 20S core. By using gradient ultracentrifugation we found that, in cellular extracts, the two PAN proteins from Halobacterium do not form stable high-molecular-mass complexes. Only PAN B was found to associate transiently with the 20S proteasome, thus suggesting that the two PAN proteins are not functionally redundant. The PAN B-20S proteasome complexes associate in an ATP-dependent manner and are stabilized upon nucleotide binding. The two PAN proteins were immunodetected in cellular extracts as N-terminal-truncated polypeptides. RNA-mapping experiments and sequence analysis indicated that this process involved transcript heterogeneities and dual translational initiation mechanisms. Taken together, our results suggest that PAN N-terminal modifications and their intracellular dynamics of assembly/association may constitute important determinants of proteolysis regulation.
机译：来自古细菌的PAN（蛋白酶体激活核苷酸酶）蛋白代表真核26S蛋白酶体调节ATP酶的同源物。在体外，PAN复合物先前已显示出对20S核心的肽酶活性具有刺激作用。通过使用梯度超速离心，我们发现，在细胞提取物中，来自嗜盐杆菌的两种PAN蛋白无法形成稳定的高分子复合物。发现仅PAN B与20S蛋白酶体瞬时缔合，因此表明这两种PAN蛋白在功能上不是多余的。 PAN B-20S蛋白酶体复合物以ATP依赖性方式结合，并在核苷酸结合时稳定。两种PAN蛋白在细胞提取物中被免疫检测为N端截短的多肽。 RNA映射实验和序列分析表明，该过程涉及转录本异质性和双重翻译起始机制。两者合计，我们的结果表明，PAN N末端修饰及其组装/关联的细胞内动力学可能构成蛋白水解调控的重要决定因素。

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