Interaction of poly(rC)-binding protein 2 domains KH1 and KH3 with coxsackievirus RNA

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• 作者：Rol ; Zell ; Yvonne Ihle ; Madlen Effenberger ; Simone Seitz ; Peter Wutzler ; Matthias Gö ; rlach
• 关键词：Enterovirus ; Picornavirus ; Replication ; Translation ; RNA secondary structure ; PCBP
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2008
• 出版时间：12 December 2008
• 年：2008
• 卷：377
• 期：2
• 页码：500-503
• 全文大小：402 K

文摘

Recombinant 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.