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http://purl.uniprot.org/citations/10744754http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10744754http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10744754http://www.w3.org/2000/01/rdf-schema#comment"Recognition of the 5'-cap structure of mRNA by eIF4E is a critical step in the recruitment of most mRNAs to the ribosome. In Caenorhabditis elegans, approximately 70% of mRNAs contain an unusual 2,2,7-trimethylguanosine cap structure as a result of trans-splicing onto the 5' end of the pre-mRNA. The characterization of three eIF4E isoforms in C. elegans (IFE-1, IFE-2, and IFE-3) was reported previously. The present study describes two more eIF4E isoforms expressed in C. elegans, IFE-4 and IFE-5. We analyzed the requirement of each isoform for viability by RNA interference. IFE-3, the most closely related to mammalian eIF4E-1, binds only 7-methylguanosine caps and is essential for viability. In contrast, three closely related isoforms (IFE-1, IFE-2, and IFE-5) bind 2,2, 7-trimethylguanosine caps and are partially redundant, but at least one functional isoform is required for viability. IFE-4, which binds only 7-methylguanosine caps, is most closely related to an unusual eIF4E isoform found in plants (nCBP) and mammals (4E-HP) and is not essential for viability in any combination of IFE knockout. ife-2, ife-3, ife-4, and ife-5 mRNAs are themselves trans-spliced to SL1 spliced leaders. ife-1 mRNA is trans-spliced to an SL2 leader, indicating that its gene resides in a downstream position of an operon."xsd:string
http://purl.uniprot.org/citations/10744754http://purl.org/dc/terms/identifier"doi:10.1074/jbc.275.14.10590"xsd:string
http://purl.uniprot.org/citations/10744754http://purl.org/dc/terms/identifier"doi:10.1074/jbc.275.14.10590"xsd:string
http://purl.uniprot.org/citations/10744754http://purl.uniprot.org/core/author"Blumenthal T."xsd:string
http://purl.uniprot.org/citations/10744754http://purl.uniprot.org/core/author"Blumenthal T."xsd:string
http://purl.uniprot.org/citations/10744754http://purl.uniprot.org/core/author"Rhoads R.E."xsd:string
http://purl.uniprot.org/citations/10744754http://purl.uniprot.org/core/author"Rhoads R.E."xsd:string
http://purl.uniprot.org/citations/10744754http://purl.uniprot.org/core/author"Keiper B.D."xsd:string
http://purl.uniprot.org/citations/10744754http://purl.uniprot.org/core/author"Keiper B.D."xsd:string
http://purl.uniprot.org/citations/10744754http://purl.uniprot.org/core/author"Deshpande A.M."xsd:string
http://purl.uniprot.org/citations/10744754http://purl.uniprot.org/core/author"Deshpande A.M."xsd:string
http://purl.uniprot.org/citations/10744754http://purl.uniprot.org/core/author"Jankowska-Anyszka M."xsd:string
http://purl.uniprot.org/citations/10744754http://purl.uniprot.org/core/author"Jankowska-Anyszka M."xsd:string
http://purl.uniprot.org/citations/10744754http://purl.uniprot.org/core/author"Aamodt E.J."xsd:string
http://purl.uniprot.org/citations/10744754http://purl.uniprot.org/core/author"Aamodt E.J."xsd:string
http://purl.uniprot.org/citations/10744754http://purl.uniprot.org/core/author"Lamphear B.J."xsd:string
http://purl.uniprot.org/citations/10744754http://purl.uniprot.org/core/author"Lamphear B.J."xsd:string
http://purl.uniprot.org/citations/10744754http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10744754http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10744754http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10744754http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10744754http://purl.uniprot.org/core/pages"10590-10596"xsd:string
http://purl.uniprot.org/citations/10744754http://purl.uniprot.org/core/pages"10590-10596"xsd:string