Human coronavirus 229E nonstructural protein 13: characterization of duplex-unwinding, nucleoside triphosphatase, and RNA 5'-triphosphatase activities.


Autoria(s): Ziebuhr, John
Data(s)

01/07/2004

Resumo

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.

Identificador

http://pure.qub.ac.uk/portal/en/publications/human-coronavirus-229e-nonstructural-protein-13-characterization-of-duplexunwinding-nucleoside-triphosphatase-and-rna-5triphosphatase-activities(4a92ec26-fef3-4452-9337-37eb4f25bc0d).html

http://dx.doi.org/10.1128/JVI.78.14.7833-7838.2004

http://www.scopus.com/inward/record.url?scp=3142689813&partnerID=8YFLogxK

Idioma(s)

eng

Direitos

info:eu-repo/semantics/restrictedAccess

Fonte

Ziebuhr , J 2004 , ' Human coronavirus 229E nonstructural protein 13: characterization of duplex-unwinding, nucleoside triphosphatase, and RNA 5'-triphosphatase activities. ' Journal of Virology , vol 78 , no. 14 , pp. 7833-7838 . DOI: 10.1128/JVI.78.14.7833-7838.2004

Palavras-Chave #/dk/atira/pure/subjectarea/asjc/2400/2403 #Immunology
Tipo

article