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学科主题: Virology
题名: De novo RNA synthesis and homology modeling of the classical swine fever virus RNA polymerase
作者: Zhang, PW; Xie, J; Yi, GH; Zhang, CY; Zhou, R
通讯作者: Zhang, CY, Guangzhou Children Hosp, Cent Lab, Guangzhou, Guangdong, Peoples R China
关键词: de novo RNA synthesis ; homology modeling ; classical swine fever ; RNA polymerase
刊名: VIRUS RESEARCH
发表日期: 2005-09-01
DOI: 10.1016/j.virusres.2005.03.003
卷: 112, 期:1-2, 页:9-23
收录类别: SCI
文章类型: Article
部门归属: Guangzhou Children Hosp, Cent Lab, Guangzhou, Guangdong, Peoples R China; Chinese Acad Sci, Inst Hydrobiol, Wuhan, Hubei, Peoples R China
WOS标题词: Science & Technology ; Life Sciences & Biomedicine
类目[WOS]: Virology
研究领域[WOS]: Virology
摘要: Classical swine fever virus (CSFV) non-structural protein 5B (NS5B) encodes an RNA-dependent RNA polymerase (RdRp), a key enzyme which initiates RNA replication by a de novo mechanism without a primer and is a potential target for anti-virus therapy. We expressed the NS5B protein in Escherichia coli. The rGTP can stimulate de novo initiation of RNA synthesis and mutation of the GDD motif to Gly-Asp-Asp (GAA) abolishes the RNA synthesis. To better understand the mechanism of viral RNA synthesis in CSFV, a three-dimensional model was built by homology modeling based on the alignment with several virus RdRps. The model contains 605 residues folded in the characteristic fingers, palm and thumb domains. The fingers domain contains an N-terminal region that plays an important role in conformational change. We propose that the experimentally observed promotion of polymerase efficiency by rGTP is probably due to the conformational changes of the polymerase caused by binding the rGTP. Mutation of the GDD to GAA interferes with the interaction between the residues at the polymerase active site and metal ions, and thus renders the polymerase inactive. (c) 2005 Elsevier B.V. All rights reserved.
英文摘要: Classical swine fever virus (CSFV) non-structural protein 5B (NS5B) encodes an RNA-dependent RNA polymerase (RdRp), a key enzyme which initiates RNA replication by a de novo mechanism without a primer and is a potential target for anti-virus therapy. We expressed the NS5B protein in Escherichia coli. The rGTP can stimulate de novo initiation of RNA synthesis and mutation of the GDD motif to Gly-Asp-Asp (GAA) abolishes the RNA synthesis. To better understand the mechanism of viral RNA synthesis in CSFV, a three-dimensional model was built by homology modeling based on the alignment with several virus RdRps. The model contains 605 residues folded in the characteristic fingers, palm and thumb domains. The fingers domain contains an N-terminal region that plays an important role in conformational change. We propose that the experimentally observed promotion of polymerase efficiency by rGTP is probably due to the conformational changes of the polymerase caused by binding the rGTP. Mutation of the GDD to GAA interferes with the interaction between the residues at the polymerase active site and metal ions, and thus renders the polymerase inactive. (c) 2005 Elsevier B.V. All rights reserved.
关键词[WOS]: HEPATITIS-C VIRUS ; VIRAL DIARRHEA VIRUS ; SECONDARY STRUCTURE PREDICTION ; MULTIPLE SEQUENCE ALIGNMENT ; REVERSE-TRANSCRIPTASE ; CRYSTAL-STRUCTURE ; ESCHERICHIA-COLI ; STRAND RNA ; ANGSTROM RESOLUTION ; ENZYMATIC-ACTIVITY
语种: 英语
WOS记录号: WOS:000231004300002
ISSN号: 0168-1702
Citation statistics:
内容类型: 期刊论文
URI标识: http://ir.ihb.ac.cn/handle/152342/9182
Appears in Collections:中科院水生所知识产出(2009年前)_期刊论文

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作者单位: 1.Guangzhou Children Hosp, Cent Lab, Guangzhou, Guangdong, Peoples R China
2.Chinese Acad Sci, Inst Hydrobiol, Wuhan, Hubei, Peoples R China

Recommended Citation:
.De novo RNA synthesis and homology modeling of the classical swine fever virus RNA polymerase,VIRUS RESEARCH,2005,112(1-2):9-23
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