人冠状病毒229E非结构蛋白13：双链解旋、核苷三磷酸酶及RNA 5'-三磷酸酶活性的特性
Human coronavirus 229E nonstructural protein 13: characterization of duplex-unwinding, nucleoside triphosphatase, and RNA 5'-triphosphatase activities.
作者信息
Ivanov Konstantin A, Ziebuhr John
机构信息
Institute of Virology and Immunology, University of Würzburg, Würzburg, Germany.
出版信息
J Virol. 2004 Jul;78(14):7833-8. doi: 10.1128/JVI.78.14.7833-7838.2004.
Abstract
The human coronavirus 229E (HCoV-229E) replicase gene-encoded nonstructural protein 13 (nsp13) contains an N-terminal zinc-binding domain and a C-terminal superfamily 1 helicase domain. A histidine-tagged form of nsp13, which was expressed in insect cells and purified, is reported to unwind efficiently both partial-duplex RNA and DNA of up to several hundred base pairs. Characterization of the nsp13-associated nucleoside triphosphatase (NTPase) activities revealed that all natural ribonucleotides and nucleotides are substrates of nsp13, with ATP, dATP, and GTP being hydrolyzed most efficiently. Using the NTPase active site, HCoV-229E nsp13 also mediates RNA 5'-triphosphatase activity, which may be involved in the capping of viral RNAs.
摘要
人冠状病毒229E（HCoV-229E）复制酶基因编码的非结构蛋白13（nsp13）包含一个N端锌结合结构域和一个C端超家族1解旋酶结构域。据报道，一种在昆虫细胞中表达并纯化的组氨酸标签形式的nsp13能够有效解开长达数百个碱基对的部分双链RNA和DNA。对nsp13相关核苷三磷酸酶（NTPase）活性的表征表明，所有天然核糖核苷酸和核苷酸都是nsp13的底物，其中ATP、dATP和GTP的水解效率最高。利用NTPase活性位点，HCoV-229E nsp13还介导RNA 5'-三磷酸酶活性，这可能参与病毒RNA的加帽过程。
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