文献类型: 外文期刊
作者: Yu, Xuekui 1 ; Jiang, Jiansen 1 ; Sun, Jingchen 1 ; Zhou, Z. Hong 1 ;
作者机构: 1.Univ Calif Los Angeles, Dept Microbiol Immunol & Mol Genet, Los Angeles, CA 90089 USA
2.Univ Calif Los Angeles, Calif Nanosyst Inst, Los Angeles, CA USA
3.South China Agr Univ, Coll Anim Sci, Guangdong Prov Key Lab Agroanim Genom & Mol Breed, Subtrop Sericulture & Mulberry Resources Protect, Guangzhou, Guangdong, Peoples R China
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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