Source:http://linkedlifedata.com/resource/pubmed/id/10744754
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
14
|
| pubmed:dateCreated |
2000-5-8
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| pubmed:databankReference | |
| pubmed:abstractText |
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.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factor-4E,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Initiation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Caps,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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| pubmed:status |
MEDLINE
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| pubmed:month |
Apr
|
| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
7
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| pubmed:volume |
275
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
10590-6
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:10744754-Amino Acid Sequence,
pubmed-meshheading:10744754-Animals,
pubmed-meshheading:10744754-Binding Sites,
pubmed-meshheading:10744754-Caenorhabditis elegans,
pubmed-meshheading:10744754-Cloning, Molecular,
pubmed-meshheading:10744754-Embryo, Nonmammalian,
pubmed-meshheading:10744754-Eukaryotic Initiation Factor-4E,
pubmed-meshheading:10744754-Humans,
pubmed-meshheading:10744754-Molecular Sequence Data,
pubmed-meshheading:10744754-Oligodeoxyribonucleotides,
pubmed-meshheading:10744754-Peptide Initiation Factors,
pubmed-meshheading:10744754-Phylogeny,
pubmed-meshheading:10744754-Protein Isoforms,
pubmed-meshheading:10744754-RNA Caps,
pubmed-meshheading:10744754-Recombinant Proteins,
pubmed-meshheading:10744754-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:10744754-Sequence Alignment,
pubmed-meshheading:10744754-Sequence Homology, Amino Acid
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| pubmed:year |
2000
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| pubmed:articleTitle |
Functional characterization of five eIF4E isoforms in Caenorhabditis elegans.
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| pubmed:affiliation |
Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, Shreveport, Louisiana 71130-3932, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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