| | | | | The R Protein of SARS-CoV: Analyses of Structure and Function Based on Four Complete Genome Sequences of Isolates BJ01-BJ04 | | | <正> The R (replicase) protein is the uniquely defined non-structural protein (NSP) responsible for RNA replication, mutation rate or fidelity, regulation of transcription in coronaviruses and many other ssRNA viruses. Based on our complete genome sequences of four isolates (BJ01-BJ04) of SARS-CoV from Beijing, China, we analyzed the structure and predicted functions of the R protein in comparison with 13 other isolates of SARS-CoV and 6 other coronaviruses. The entire ORF (open-reading frame) encodes for two major enzyme activities, RNA-dependent RNA polymerase (RdRp) and proteinase activities. The R polyprotein undergoes a complex proteolytic process to produce 15 function-related peptides. A hydrophobic domain (HOD) and a hydrophilic domain (HID) are newly identified within NSP1. The substitution rate of the R protein is close to the average of the SARS-CoV genome. The functional domains in all NSPs of the R protein give different phylogenetic results that suggest their different mutation rate under selec
【分类号】：Q51
【DOI】：cnki:ISSN:1672-0229.0.2003-02-007
【正文快照】：
IntroduetionIn the life eyele of eoronaviruses,theR(repliease)protein,the largest Protein of the virus,15 the firsttranslated Produet following the infeetion of host eellsby the virus.It 15 immediately translated场host ri-bosomes into a large PolyProtein.… | | | | | |  推荐 下载CAJ全文  下载PDF全文 | | | CAJViewer7.0阅读器支持所有CNKI文件格式，AdobeReader仅支持PDF格式 | | | | The R Protein of SARS-CoV: Analyses of Structure and Function Based on Four Complete Genome Sequences of Isolates BJ01-BJ04 | | | Zuyuan Xu;Haiqing Zhang;Xiangjun Tian;Jia Ji;Wei Li;Yan Li;Wei Tian;Yujun Han;Lili Wang;Zizhang Zhang;Jing Xu;Wei Wei;Jingui Zhu;Haiyan Sun;Xiaowei Zhang;Jun Zhou;Songgang Li;Jun Wang;Jian Wang;Shengli Bi;and Huanming Yang
Beijing Genomics Institute;Chinese Academy of Sciences;Beijing 101300;China; James D. Watson Institute of Genome Sciences;Zhijiang Campus;Zhejiang University;Hangzhou 310008;China; Medical College;Xi'an Jiaotong University;Xi'an 710049;China; College of Life Sciences;Peking University;Beijing 100871;China; Center of Disease Control and Prevention;Beijing 100050;China. | | | The R (replicase) protein is the uniquely defined non-structural protein (NSP) responsible for RNA replication, mutation rate or fidelity, regulation of transcription in coronaviruses and many other ssRNA viruses. Based on our complete genome sequences of four isolates (BJ01-BJ04) of SARS-CoV from Beijing, China, we analyzed the structure and predicted functions of the R protein in comparison with 13 other isolates of SARS-CoV and 6 other coronaviruses. The entire ORF (open-reading frame) encodes for two major enzyme activities, RNA-dependent RNA polymerase (RdRp) and proteinase activities. The R polyprotein undergoes a complex proteolytic process to produce 15 function-related peptides. A hydrophobic domain (HOD) and a hydrophilic domain (HID) are newly identified within NSP1. The substitution rate of the R protein is close to the average of the SARS-CoV genome. The functional domains in all NSPs of the R protein give different phylogenetic results that suggest their different mutation rate under selective pressure. Eleven highly conserved regions in RdRp and twelve cleavage sites by 3CLP (chymotrypsin-like protein) have been identified as potential drug targets. Findings suggest that it is possible to obtain information about the phy-logeny of SARS-CoV, as well as potential tools for drug design, genotyping and diagnostics of SARS.
【Keyword】：SARS, SARS-CoV, RNA-dependent RNA polymerase, RNA viruses, proteolysis |
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