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首页> 外文期刊>Journal of Molecular Biology >Guanylyltransferase and RNA 5 '-triphosphatase activities of the purified expressed VP4 protein of bluetongue virus
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Guanylyltransferase and RNA 5 '-triphosphatase activities of the purified expressed VP4 protein of bluetongue virus

机译：蓝舌病毒纯化表达的VP4蛋白的鸟嘌呤基转移酶和RNA 5'-三磷酸酶活性

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摘要

We have examined the RNA-capping enzyme activities of bluetongue virus (BTV) minor core protein, VP4. Recombinant BTV VP4 protein was purified to homogeneity from insect cell culture infected with a baculovirus VP4 of BTV serotype 10. We demonstrate that the purified protein, and VP4 encapsidated in core-like particles, react with GTP and covalently bind GMP via a phosphoamide linkage, a characteristic feature of guanylyltransferase enzyme. VP4 also catalyses a GTP-PPi exchange reaction indicating that the protein is the guanylyltransferase of the virus. In addition, VP4 possesses an RNA 5'-triphosphatase activity which catalyses the first step in the RNA-capping sequence. Further, an inorganic pyrophosphatase activity was identified which may aid the transcription activity within the virus by removing inorganic pyrophosphate which is an inhibitor of the polymerization reaction. Finally, the direct evidence of VP4 capping activity has been obtained by demonstrating in vitro transfer of GMP to the 5' end of in vitro synthesized BTV ssRNA transcripts to form a cap structure. (C) 1998 Academic Press. [References: 17]
机译：我们已经检查了蓝舌病毒（BTV）次要核心蛋白VP4的RNA上限酶活性。从感染了BTV血清型10的杆状病毒VP4的昆虫细胞培养物中纯化重组BTV VP4蛋白，使其具有同质性。我们证明，纯化的蛋白和VP4包裹在核样颗粒中，与GTP反应并通过磷酰胺键共价结合GMP，胍基转移酶的特征。 VP4还催化GTP-PPi交换反应，表明该蛋白质是病毒的鸟苷酸转移酶。此外，VP4具有RNA 5'-三磷酸酶活性，可催化RNA封闭序列的第一步。此外，鉴定了无机焦磷酸酶活性，其可以通过除去作为聚合反应抑制剂的无机焦磷酸盐来辅助病毒内的转录活性。最后，通过证明GMP体外转移到体外合成的BTV ssRNA转录本的5'端以形成帽结构，获得了VP4帽活性的直接证据。 （C）1998年学术出版社。 [参考：17]

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