呼肠孤病毒双链RNA结合蛋白sigma3在HeLa细胞中的表达受调控、稳定且定位于细胞核。
Regulated, stable expression and nuclear presence of reovirus double-stranded RNA-binding protein sigma3 in HeLa cells.
作者信息
Yue Z, Shatkin A J
机构信息
Graduate Program in Biochemistry, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, Piscataway, USA.
出版信息
J Virol. 1996 Jun;70(6):3497-501. doi: 10.1128/JVI.70.6.3497-3501.1996.
Abstract
Reovirus genome segment S4 codes for polypeptide sigma3, a major outer capsid component of virions and a double-stranded RNA (dsRNA)-binding protein implicated in viral cytopathogenesis. We have constructed a stable HeLa cell line (S4tTA) that produces functional sigma3 under tetracycline transactivator control. In the absence of tetracycline, S4tTA cells synthesized stable dsRNA-binding sigma3 that accumulated in the nucleus as well as in the cytoplasm. However, in induced S4tTA cells also expressing reovirus outer shell polypeptide mu1/mu1C, migration of sigma3 into the nucleus was blocked, probably as a result of formation of a complex with mu1/mu1C which was exclusively in the cytoplasm. Mutant analyses indicated a correlation between dsRNA-binding activity and nuclear entry of sigma3, suggesting an additional role(s) for this capsid protein in virus-cell interactions.
摘要
呼肠孤病毒基因组片段S4编码σ3多肽，它是病毒粒子的主要外衣壳成分，也是一种双链RNA（dsRNA）结合蛋白，与病毒细胞病变机制有关。我们构建了一个稳定的HeLa细胞系（S4tTA），该细胞系在四环素反式激活因子的控制下产生功能性σ3。在没有四环素的情况下，S4tTA细胞合成稳定的dsRNA结合性σ3，其在细胞核和细胞质中积累。然而，在诱导的同时也表达呼肠孤病毒外壳多肽μ1/μ1C的S4tTA细胞中，σ3向细胞核的迁移被阻断了，这可能是由于与仅存在于细胞质中的μ1/μ1C形成复合物的结果。突变分析表明dsRNA结合活性与σ3的核进入之间存在相关性，这表明这种衣壳蛋白在病毒-细胞相互作用中还有其他作用。
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