A putative ATPase mediates RNA transcription and capping in a dsRNA virus

文献类型： 外文期刊

第一作者： Yu, Xuekui

作者： Yu, Xuekui;Jiang, Jiansen;Sun, Jingchen;Zhou, Z. Hong;Yu, Xuekui;Jiang, Jiansen;Zhou, Z. Hong;Sun, Jingchen

作者机构：

期刊名称：ELIFE （ 影响因子：8.14； 五年影响因子：9.056 ）

ISSN： 2050-084X

年卷期： 2015 年 4 卷

页码：

收录情况： SCI

摘要： mRNA transcription in dsRNA viruses is a highly regulated process but the mechanism of this regulation is not known. Here, by nucleoside triphosphatase (NTPase) assay and comparisons of six high-resolution (2.9-3.1 angstrom) cryo-electron microscopy structures of cytoplasmic polyhedrosis virus with bound ligands, we show that the large sub-domain of the guanylyltransferase (GTase) domain of the turret protein (TP) also has an ATP-binding site and is likely an ATPase. S-adenosyl-L-methionine (SAM) acts as a signal and binds the methylase-2 domain of TP to induce conformational change of the viral capsid, which in turn activates the putative ATPase. ATP binding/hydrolysis leads to an enlarged capsid for efficient mRNA synthesis, an open GTase domain for His217-mediated guanylyl transfer, and an open methylase-1 domain for SAM binding and methyl transfer. Taken together, our data support a role of the putative ATPase in mediating the activation of mRNA transcription and capping within the confines of the virus.

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