RNA interaction and cleavage of poly(C)-binding protein 2 by hepatitis A virus protease.
RNA interaction and cleavage of poly(C)-binding protein 2 by hepatitis A virus protease.
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DOI：
10.1016/j.bbrc.2007.09.133
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发表时间：
2007-12
影响因子：
3.1
通讯作者：
Bo Zhang;S. Seitz;Y. Kusov;R. Zell;V. Gauss-Müller
中科院分区：
文献类型：
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作者：
Bo Zhang;S. Seitz;Y. Kusov;R. Zell;V. Gauss-Müller
Poly(RC)结合蛋白PCBP2在宿主和病毒基因表达的转录后调控中具有多种功能。由于PCBP2与微小核糖核酸结构相互作用，因此有人认为PCBP2调控病毒基因组的翻译和复制。甲型肝炎病毒(HAV)是一种非典型的微小核糖核酸病毒，它含有一个功能未知的异常的富含嘧啶的途径(PY1)。利用体内和体外实验，我们提供了PCBP2与pY1相互作用的直接证据，这种结合是由KH结构域1和3介导的。病毒蛋白酶3C的蛋白水解性裂解产生了一个C端截短的多肽，其RNA亲和力大大降低。结果表明，在甲型肝炎病毒感染期间，PCBP2裂解可能特异性地下调病毒蛋白质的合成，从而让位于病毒RNA的合成。
The poly(rC)-binding protein PCBP2 has multiple functions in post-transcriptional control of host and viral gene expression. Since it interacts with picornaviral RNA structures, it was proposed that PCBP2 regulates viral genome translation and replication. The hepatitis A virus (HAV), an atypical picornavirus, contains an unusual pyrimidine-rich tract (pY1) with unknown functions. Using in vivo and in vitro assays, we provide direct evidence that PCBP2 interacts with pY1 and that binding is mediated by KH domains 1 and 3. Proteolytic cleavage by the viral protease 3C generates a C-terminally truncated polypeptide with highly reduced RNA affinity. The results suggest that during HAV infection PCBP2 cleavage might specifically down-regulate viral protein synthesis, thereby giving way to viral RNA synthesis.