Source:http://linkedlifedata.com/resource/pubmed/id/15034551
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2004-3-29
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pubmed:abstractText |
The exon junction complex (EJC), a set of proteins deposited on mRNAs as a consequence of pre-mRNA splicing, is a key effector of downstream mRNA metabolism. We have identified eIF4AIII, a member of the eukaryotic translation initiation factor 4A family of RNA helicases (also known as DExH/D box proteins), as a novel EJC core component. Crosslinking and antibody inhibition studies suggest that eIF4AIII constitutes at least part of the platform anchoring other EJC components to spliced mRNAs. A nucleocytoplasmic shuttling protein, eIF4AIII associates in vitro and in vivo with two other EJC core factors, Y14 and Magoh. In mammalian cells, eIF4AIII is essential for nonsense-mediated mRNA decay (NMD). Finally, a model is proposed by which eIF4AIII represents a new functional class of DExH/D box proteins that act as RNA clamps or 'place holders' for the sequence-independent attachment of additional factors to RNAs.
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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/Codon, Nonsense,
http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factor-4A,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1545-9993
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
346-51
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:15034551-Binding Sites,
pubmed-meshheading:15034551-Codon, Nonsense,
pubmed-meshheading:15034551-Eukaryotic Initiation Factor-4A,
pubmed-meshheading:15034551-Exons,
pubmed-meshheading:15034551-Genes, Reporter,
pubmed-meshheading:15034551-Glutathione Transferase,
pubmed-meshheading:15034551-Humans,
pubmed-meshheading:15034551-Kinetics,
pubmed-meshheading:15034551-Polymerase Chain Reaction,
pubmed-meshheading:15034551-RNA, Messenger,
pubmed-meshheading:15034551-RNA Splicing,
pubmed-meshheading:15034551-Recombinant Fusion Proteins
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pubmed:year |
2004
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pubmed:articleTitle |
eIF4AIII binds spliced mRNA in the exon junction complex and is essential for nonsense-mediated decay.
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pubmed:affiliation |
Howard Hughes Medical Institute, Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02454, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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