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首页> 外文期刊>Molecular and Cellular Biology >Interactions between double-stranded RNA regulators and the protein kinase DAI.
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Interactions between double-stranded RNA regulators and the protein kinase DAI.

机译：双链RNA调节剂和蛋白激酶DAI之间的相互作用。

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The interferon-induced protein kinase DAI, the double-stranded RNA (dsRNA)-activated inhibitor of translation, plays a key role in regulating protein synthesis in higher cells. Once activated, in a process that involves autophosphorylation, it phosphorylates the initiation factor eIF-2, leading to inhibition of polypeptide chain initiation. The activity of DAI is controlled by RNA regulators, including dsRNA activators and highly structured single-stranded RNAs which block activation by dsRNA. To elucidate the mechanism of activation, we studied the interaction of DAI with RNA duplexes of discrete sizes. Molecules shorter than 30 bp fail to bind stably and do not activate the enzyme, but at high concentrations they prevent activation by long dsRNA. Molecules longer than 30 bp bind and activate the enzyme, with an efficiency that increases with increasing chain length, reaching a maximum at about 85 bp. These dsRNAs fail to activate at high concentrations and also prevent activation by long dsRNA. Analysis of complexes between dsRNA and DAI suggests that at maximal packing the enzyme interacts with as little as a single helical turn of dsRNA (11 bp) but under conditions that allow activation the binding site protects about 80 bp of duplex. When the RNA-binding site is fully occupied with an RNA activator, the complex appears to undergo a conformational change.
机译：干扰素诱导的蛋白激酶DAI，双链RNA（dsRNA）激活的翻译抑制剂，在调节高等细胞的蛋白合成中起关键作用。一旦被激活，在涉及自磷酸化的过程中，它会磷酸化起始因子eIF-2，从而抑制多肽链的起始。 DAI的活性受RNA调节剂的控制，包括dsRNA激活剂和高度结构化的单链RNA，它们可阻止dsRNA激活。为了阐明激活机制，我们研究了DAI与离散大小的RNA双链体的相互作用。短于30 bp的分子不能稳定结合并且不能激活该酶，但是在高浓度下它们会阻止长dsRNA的激活。大于30 bp的分子结合并激活酶，效率随着链长的增加而增加，在约85 bp时达到最大值。这些dsRNA在高浓度下不能激活，并且还阻止了长dsRNA的激活。对dsRNA与DAI之间的复合物的分析表明，在最大包装下，酶与dsRNA的单个螺旋圈（11 bp）相互作用时少，但在允许激活的条件下，结合位点可保护约80 bp的双链体。当RNA结合位点被RNA激活剂完全占据时，复合物似乎发生构象变化。

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