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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 the chaperone Hsp104 with yeast Sup35 and mammalian PrP
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Interactions of the chaperone Hsp104 with yeast Sup35 and mammalian PrP

机译:伴侣蛋白Hsp104与酵母Sup35和哺乳动物PrP的相互作用

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摘要

[PSI+] is a genetic element in yeast for which a heritable change in phenotype appears to be caused by a heritable change in the conformational state of the Sup35 protein. The inheritance of [PSI+] and the physical state of Sup35 in vivo depend on the protein chaperone Hsp104 (heat shock protein 104). Although these observations provide a strong genetic argument in support of the "protein-only" or "prion" hypothesis for [PSI+], there is, as yet, no direct evidence of an interaction between the two proteins. We report that when purified Sup35 and Hsp104 are mixed, the circular dichroism (CD) spectrum differs from that predicted by the addition of the proteins' individual spectra, and the ATPase activity of Hsp104 is inhibited.
机译:[PSI +]是酵母中的一种遗传元件,其表型可遗传改变似乎是由Sup35蛋白的构象状态可遗传改变引起的。 [PSI +]的遗传和体内Sup35的物理状态取决于蛋白伴侣Hsp104(热激蛋白104)。尽管这些发现为[PSI +]的“仅蛋白质”或“ pr病毒”假说提供了有力的遗传学依据,但迄今为止,尚无直接证据表明这两种蛋白质之间存在相互作用。我们报告说,当纯化的Sup35和Hsp104混合时,圆二色性(CD)谱不同于通过添加蛋白质的单个谱所预测的谱,并且Hsp104的ATPase活性受到抑制。

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