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10.1371/journal.pone.0140291 http://scihub22266oqcxt.onion/10.1371/journal.pone.0140291 C4599798!4599798 !26451954     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26451954 &cmd=llinks): Failed to open stream: HTTP request failed! 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HuR and Ago2 Bind the Internal Ribosome Entry Site of Enterovirus 71 and Promote Virus Translation and Replication |pdf=|usr=}}{{26451954 }} gab.com Text HuR and Ago2 Bind the Internal Ribosome Entry Site of Enterovirus 71 and Promote Virus Translation and Replication JO: PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=26451954 #FOAvip EV71 (enterovirus 71) RNA contains an internal ribosomal entry site (IRES) that directs cap-independent initiation of translation. IRES-dependent translation requires the host's translation initiation factors and IRES-associated trans-acting factors (ITAFs). We reported recently that mRNA decay factor AUF1 is a negative-acting ITAF that binds IRES stem-loop II. We also reported that the small RNA-processing enzyme Dicer produces at least four small RNAs (vsRNAs) from the EV71 IRES. One of these, vsRNA1, derived from IRES stem-loop II, reduces IRES activity and virus replication. Since its mechanism of action is unknown, we hypothesized that it might control association of ITAFs with the IRES. Here, we identified the mRNA stability factor HuR and the RISC subunit Argonaute 2 (Ago2) as two ITAFs that bind stem-loop II. In contrast to AUF1, HuR and Ago2 promote EV71 IRES activity and virus replication. In vitro RNA-binding assays revealed that vsRNA1 can alter association of Ago2, HuR, and AUF1 with stem-loop II. This presents a possible mechanism by which vsRNA1 could control viral translation and replication. Twit Text FOAVip HuR and Ago2 Bind the Internal Ribosome Entry Site of Enterovirus 71 and Promote Virus Translation and Replication ????PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=26451954 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26451954 #FOAvip English Wikipedia <ref>{{Cite pmid|26451954 }}</ref> HuR and Ago2 Bind the Internal Ribosome Entry Site of Enterovirus 71 and Promote Virus Translation and Replication #MMPMID26451954 Lin JY ; Brewer G ; Li ML PLoS One 2015[]; 10 (10 ): e0140291 PMID26451954 show ga EV71 (enterovirus 71) RNA contains an internal ribosomal entry site (IRES) that directs cap-independent initiation of translation. IRES-dependent translation requires the host's translation initiation factors and IRES-associated trans-acting factors (ITAFs). We reported recently that mRNA decay factor AUF1 is a negative-acting ITAF that binds IRES stem-loop II. We also reported that the small RNA-processing enzyme Dicer produces at least four small RNAs (vsRNAs) from the EV71 IRES. One of these, vsRNA1, derived from IRES stem-loop II, reduces IRES activity and virus replication. Since its mechanism of action is unknown, we hypothesized that it might control association of ITAFs with the IRES. Here, we identified the mRNA stability factor HuR and the RISC subunit Argonaute 2 (Ago2) as two ITAFs that bind stem-loop II. In contrast to AUF1, HuR and Ago2 promote EV71 IRES activity and virus replication. In vitro RNA-binding assays revealed that vsRNA1 can alter association of Ago2, HuR, and AUF1 with stem-loop II. This presents a possible mechanism by which vsRNA1 could control viral translation and replication. |*Internal Ribosome Entry Sites [MESH] |*Protein Biosynthesis [MESH] |5' Untranslated Regions/genetics [MESH] |Animals [MESH] |Argonaute Proteins/deficiency/genetics/*metabolism [MESH] |Cell Line, Tumor [MESH] |Chlorocebus aethiops [MESH] |ELAV-Like Protein 1/deficiency/genetics/*metabolism [MESH] |Enterovirus A, Human/*genetics/metabolism/*physiology [MESH] |Gene Knockdown Techniques [MESH] |Heterogeneous Nuclear Ribonucleoprotein D0 [MESH] |Heterogeneous-Nuclear Ribonucleoprotein D/metabolism [MESH] |Humans [MESH] |Inverted Repeat Sequences/genetics [MESH] |Protein Binding [MESH] |RNA, Viral/genetics/metabolism [MESH] |Vero Cells [MESH]HuR and Ago2 Bind the Internal Ribosome Entry Site of Enterovirus 71 a(epmc).pdf DeepDyve Pubget Overpricing