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首页> 外文期刊>Biochemistry >Chicken prion tandem repeats form a stable, protease-resistant domain.
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Chicken prion tandem repeats form a stable, protease-resistant domain.

机译：鸡病毒串联重复序列形成稳定的，耐蛋白酶的结构域。

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摘要

Prion-linked diseases, such as mad cow disease, scrapie, and the human genetic disorder Creutzfeldt-Jakob disease, are fatal neurodegenerative diseases correlated with changes in the secondary structure of neural prion protein. We expressed recombinant chicken prion protein in Escherichia coli and purified the protein to homogeneity. Circular dichroism spectra of the 26 kDa recombinant protein closely resemble those of prion protein purified directly from healthy hamster brain. The chicken prion protein exists as a soluble, monodisperse monomer but can be forced to multimerize following lyophilization and resuspension. We analyzed the chicken prion protein domain structure by proteolysis and show that, unlike the mammalian homologues, the chicken prion protein N-terminal tandem amino acid repeats form a stable, protease-resistant domain. This domain probably represents a physiologically functional unit. As tested by both mass spectrometry and circular dichroism, the mature chicken prion protein does not bind copper, unlike synthetic peptides from the chicken prion N-terminus, suggesting that binding copper is not the physiological activity of the chicken prion. However, copper strongly destabilizes the prion protein and depresses the melting temperature by 30 degreesC, presumably by binding to the unfolded form of the prion protein. The chicken prion N-terminus may have evolved to fold without a cofactor, unlike mammalian prion proteins, whose N-termini are disordered without cofactors such as copper present. Chicken prion offers an alternative to intractable mammalian prions for structural studies of the amino-terminal domain.
机译：与on病毒有关的疾病，例如疯牛病，瘙痒病和人类遗传病Creutzfeldt-Jakob病，是致命的神经退行性疾病，与神经蛋白二级结构的变化有关。我们在大肠杆菌中表达了重组鸡病毒蛋白，并将其纯化至同质。 26 kDa重组蛋白的圆二色光谱与直接从健康仓鼠大脑中纯化的病毒蛋白的圆二色光谱非常相似。鸡病毒蛋白以可溶的单分散单体形式存在，但在冻干和重悬后会被迫聚合。我们通过蛋白水解分析了蛋白的蛋白质结构域结构，结果表明，与哺乳动物同源物不同，the蛋白的N端串联氨基酸重复序列形成了稳定的，耐蛋白酶的结构域。该结构域可能代表生理功能单元。通过质谱和圆二色性测试，成熟的鸡chicken病毒蛋白不结合铜，这与来自鸡chicken蛋白N端的合成肽不同，这表明结合铜不是鸡pr病毒的生理活性。但是，铜可能会严重破坏the病毒蛋白的稳定性，并使解链温度降低30摄氏度，这可能是由于与to蛋白蛋白质的未折叠形式结合所致。不同于蛋白的哺乳动物蛋白，其pr末端的N末端不存在诸如铜之类的辅因子，而-蛋白的N末端可能已经进化成没有辅因子的折叠。鸡蛋白为顽固的哺乳动物蛋白的氨基末端结构域研究提供了一种替代方法。

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