Roland Zell, Yvonne Ihle, Madlen Effenberger, Simone Seitz, Peter Wutzler, Matthias Görlach
Institute for Virology and Antiviral Therapy, Friedrich Schiller University, Hans-Knöll-Str. 2, D-07745 Jena, Germany.
Biochemical and biophysical research communications 2008 Dec 12Recombinant hnRNP K-homology (KH) domains 1 and 3 of the poly(rC)-binding protein (PCBP) 2 were purified and assayed for interaction with coxsackievirus B3 RNA in electrophoretic mobility shift assays using in vitro transcribed RNAs which represent signal structures of the 5'-nontranslated region. KH domains 1 and 3 interact with the extended cloverleaf RNA and domain IV RNA of the internal ribosome entry site (IRES). KH1 but not KH3 interacts with subdomain IV/C RNA, whereas KH3 interacts with subdomain IV/B. All in vitro results are consistent with yeast three-hybrid experiments performed in parallel. The data demonstrate interaction of isolated PCBP2 KH1 and KH3 domains to four distinct target sites within the 5'-nontranslated region of the CVB3 genomic RNA.
Roland Zell, Yvonne Ihle, Madlen Effenberger, Simone Seitz, Peter Wutzler, Matthias Görlach. Interaction of poly(rC)-binding protein 2 domains KH1 and KH3 with coxsackievirus RNA. Biochemical and biophysical research communications. 2008 Dec 12;377(2):500-3
PMID: 18929541
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