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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Amyloid of Rnq1p, the basis of the [PIN~+] priori, has a parallel in-register β-sheet structure
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Amyloid of Rnq1p, the basis of the [PIN~+] priori, has a parallel in-register β-sheet structure

机译：Rnq1p的淀粉样蛋白是[PIN〜+]先验的基础，具有平行的寄存器内β-折叠结构

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摘要

The [PIN~+] priori, a self-propagating amyloid form of Rnq1p, increases the frequency with which the [PSI~+] or [URE3] prions arise de novo. Like the prion domains of Sup35p and Ure2p, Rnq 1p is rich in N and Q residues, but rnq1Δ strains have no known phenotype except for inability to propagate the [PIN~+] prion. We used solid-state NMR methods to examine amyloid formed in vitro from recombinant Rnq1 prion domain (residues 153-405) labeled with Tyr-1-~(13)C (14 residues), Leu-1-~(13)C (7 residues), or Ala-3-~(13)C (13 residues). The carbonyl chemical shifts indicate that most Tyr and Leu residues are in 0-sheet conformation. Experiments designed to measure the distance from each labeled residue to the next nearest labeled carbonyl showed that almost all Tyr and Leu carbonyl carbon atoms were ≈0.5 nm from the next nearest Tyr and Leu residues, respectively. This result indicates that the Rnq1 prion domain forms amyloid consisting of parallel β-strands that are either in register or are at most one amino acid out of register. Similar experiments with Ala-3-~(13)C indicate that the β-strands are indeed in-register. The parallel in-register structure, now demonstrated for each of the yeast prions, explains the faithful templat-ing of prion strains, and suggests as well a mechanism for the rare hetero-priming that is [PIN~+]'s defining characteristic.
机译：先验的[PIN〜+]是Rnq1p的自我繁殖的淀粉样蛋白形式，它会增加[PSI〜+]或[URE3] pr病毒从头出现的频率。像Sup35p和Ure2p的病毒结构域一样，Rnq 1p富含N和Q残基，但是rnq1Δ菌株除了无法传播[PIN〜+] ion病毒外，没有其他表型。我们使用固态NMR方法检查了由Tyr-1-〜（13）C（14个残基），Leu-1-〜（13）C标记的重组Rnq1 ion病毒域（残基153-405）体外形成的淀粉样蛋白（ 7个残基）或Ala-3-〜（13）C（13个残基）。羰基化学位移表明大多数Tyr和Leu残基为0-sheet构象。设计用于测量每个标记残基到下一个最近标记的羰基的距离的实验表明，几乎所有Tyr和Leu羰基碳原子分别距第二个最近的Tyr和Leu残基≈0.5 nm。该结果表明，Rnq1病毒结构域形成由平行β链组成的淀粉样蛋白，所述平行β链处于配准中或至多失配一个氨基酸。用Ala-3-〜（13）C进行的类似实验表明，β链确实在寄存器内。现在为每种酵母病毒所证实的平行的配准结构，解释了病毒菌株的忠实模板，并提出了罕见的异源引发机制，这是[PIN〜+]的定义特征。

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