New nsp8 isoform suggests mechanism for tuning viral RNA synthesis

作     者：Shuang Li Qi Zhao Yinjie Zhang Yang Zhang Mark Bartlam Xuemei Li Zihe Rao 

作者机构：National Laboratory of MacromoleculesInstitute of BiophysicsChinese Academy of SciencesBeijing 100101China Structural Biology LaboratoryTsinghua UniversityBeijing 100084China Tianjin Key Laboratory of Protein ScienceCollege of Life SciencesNankai UniversityTianjin 300071China 

出 版 物：《Protein & Cell》 (蛋白质与细胞（英文版）)

年 卷 期：2010年第1卷第2期

页      面：198-204页

核心收录：

学科分类：0710[理学-生物学] 0831[工学-生物医学工程（可授工学、理学、医学学位）] 1007[医学-药学(可授医学、理学学位)] 1002[医学-临床医学] 081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术] 070303[理学-有机化学] 0703[理学-化学] 0836[工学-生物工程] 

基　　金：This work was supported by Project 973 of the Ministry of Science and Technology of China(Nos.2006CB806503,2007CB914301) the National Natural Science Foundation of China(Grant Nos.30221003,30730022) 

主　　题：nsp8 SARS-CoV RNA primase viral life cycle 

摘      要：During severe acute respiratory syndrome coronavirus(SARS-CoV)infection,the activity of the replication/transcription complexes(RTC)quickly peaks at 6 hours post infection(h.p.i)and then diminishes significantly in the late post-infection ***“down-up-downregulation of RNA synthesis distinguishes different viral stages:primary translation,genome replication,and finally viron *** the nsp8 as the primase in RNA synthesis,we confirmed that the proteolysis product of the primase(nsp8)contains the globular domain(nsp8C),and indentified the resectioning site that is notably conserved in all the three groups of *** subsequently crystallized the complex of SARS-CoV nsp8C and nsp7,and the 3-D structure of this domain revealed its capability to interfuse into the hexadecamer *** specific proteolysis may indicate one possible mechanism by which coronaviruses to switch from viral infection to genome replication and viral assembly stages.