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首页> 外文期刊>Molecular and Cellular Biology >Distinct binding sites for zinc and double-stranded RNA in the reovirus outer capsid protein sigma 3.
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Distinct binding sites for zinc and double-stranded RNA in the reovirus outer capsid protein sigma 3.

机译：呼肠孤病毒外衣壳蛋白sigma 3中锌和双链RNA的不同结合位点。

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By atomic absorption analysis, we determined that the reovirus outer capsid protein sigma 3, which binds double-stranded RNA (dsRNA), is a zinc metalloprotein. Using Northwestern blots and a novel zinc blotting technique, we localized the zinc- and dsRNA-binding activities of sigma 3 to distinct V8 protease-generated fragments. Zinc-binding activity was contained within an amino-terminal fragment that contained a transcription factor IIIA-like zinc-binding sequence, and dsRNA-binding activity was associated with a carboxy-terminal fragment. By these techniques, new zinc- and dsRNA-binding activities were also detected in reovirus core proteins. A sequence similarity was observed between the catalytic site of the picornavirus proteases and the transcription factor IIIA-like zinc-binding site within sigma 3. We suggest that the zinc- and dsRNA-binding activities of sigma 3 may be important for its proposed regulatory effects on viral and host cell transcription and translation.
机译：通过原子吸收分析，我们确定呼肠孤病毒外衣壳蛋白sigma 3（结合双链RNA（dsRNA））是锌金属蛋白。使用西北印迹和新颖的锌印迹技术，我们将锌3和dsRNA的结合活性定位到不同的V8蛋白酶生成的片段。锌结合活性包含在含有转录因子IIIA样锌结合序列的氨基末端片段内，而dsRNA结合活性与羧基末端片段相关。通过这些技术，在呼肠孤病毒核心蛋白中还检测到新的锌和dsRNA结合活性。在小核糖核酸病毒蛋白酶的催化位点和sigma 3中的转录因子IIIA样锌结合位点之间观察到序列相似性。我们建议sigma 3的锌和dsRNA结合活性可能对拟议的调节作用很重要病毒和宿主细胞的转录和翻译。

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