Please use this identifier to cite or link to this item:
標題: HuR binding to AU-rich elements present in the 3 ' untranslated region of Classical swine fever virus
作者: Nadar, M.
Chan, M.Y.
Huang, S.W.
Huang, C.C.
Tseng, J.T.
Tsai, C.H.
關鍵字: messenger-rna degradation;ribosomal entry site;hepatitis-c virus;minus-strand rna;3'-untranslated region;elav protein;translation;genome;alpha;stabilization
Project: Virology Journal
期刊/報告no:: Virology Journal, Volume 8.
Background: Classical swine fever virus (CSFV) is the member of the genus Pestivirus under the family Flaviviridae. The 5' untranslated region (UTR) of CSFV contains the IRES, which is a highly structured element that recruits the translation machinery. The 3' UTR is usually the recognition site of the viral replicase to initiate minus-strand RNA synthesis. Adenosine-uridine rich elements (ARE) are instability determinants present in the 3' UTR of short-lived mRNAs. However, the presence of AREs in the 3' UTR of CSFV conserved in all known strains has never been reported. This study inspects a possible role of the ARE in the 3' UTR of CSFV. Results: Using RNA pull-down and LC/MS/MS assays, this study identified at least 32 possible host factors derived from the cytoplasmic extracts of PK-15 cells that bind to the CSFV 3' UTR, one of which is HuR. HuR is known to bind the AREs and protect the mRNA from degradation. Using recombinant GST-HuR, this study demonstrates that HuR binds to the ARE present in the 3' UTR of CSFV in vitro and that the binding ability is conserved in strains irrespective of virulence. Conclusions: This study identified one of the CSFV 3' UTR binding proteins HuR is specifically binding to in the ARE region.
ISSN: 1743-422X
DOI: 10.1186/1743-422x-8-340
Appears in Collections:期刊論文

Show full item record

Google ScholarTM




Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.