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The nonstructural protein 2C of Coxsackie B virus has RNA helicase and chaperoning activities

The nonstructural protein 2C of Coxsackie B virus has RNA helicase and chaperoning activities

作     者:Ziyu Chen Xiaobei Xiong Yiyang Li Muhan Huang Yujie Ren Di Wu Yang Qiu Mingzhou Chen Ting Shu Xi Zhou Ziyu Chen;Xiaobei Xiong;Yiyang Li;Muhan Huang;Yujie Ren;Di Wu;Yang Qiu;Mingzhou Chen;Ting Shu;Xi Zhou

作者机构:State Key Laboratory of VirologyCollege of Life SciencesWuhan UniversityWuhan430072China State Key Laboratory of VirologyWuhan Institute of VirologyChinese Academy of SciencesWuhan430071China University of Chinese Academy of SciencesBeijing100081China 

出 版 物:《Virologica Sinica》 (中国病毒学(英文版))

年 卷 期:2022年第37卷第5期

页      面:656-663页

核心收录:

学科分类:1007[医学-药学(可授医学、理学学位)] 100705[医学-微生物与生化药学] 1001[医学-基础医学(可授医学、理学学位)] 100103[医学-病原生物学] 10[医学] 

基  金:supported by the National Natural Science Foundation of China (82002155 to T.S.  and U21A20423 and 31670161 to X.Z.) 

主  题:2C protein Coxsackieviruses B3(CVB3) Coxsackieviruses B5(CVB5) NTPase RNA helicase RNA chaperon 

摘      要:RNA-remodeling proteins,including RNA helicases and chaperones,play vital roles in the remodeling of structured *** viral replication,viruses require RNA-remodeling proteins to facilitate proper folding and/or re-folding the viral RNA *** B3(CVB3)and Coxsackieviruses B5(CVB5),belonging to the genus Enterovirus in the family Picornaviridae,have been reported to cause various infectious diseases such as hand-foot-and-mouth disease,aseptic meningitis,and viral ***,little is known about whether CVB3 and CVB5 encode any RNA remodeling *** this study,we showed that 2C proteins of CVB3 and CVB5 contained the conserved SF3 helicase A,B,and C motifs,and functioned not only as RNA helicase that unwound RNA helix bidirectionally in an NTP-dependent manner,but also as RNA chaperone that remodeled structured RNAs and facilitated RNA strand annealing independently of *** addition,we determined that the NTPase activity and RNA helicase activity of 2C proteins of CVB3 and CVB5 were dependent on the presence of divalent metallic *** findings demonstrate that 2C proteins of CVBs possess RNA-remodeling activity and underline the functional importance of 2C protein in the life cycle of CVBs.

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